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 |
| AEX85087.1 | AEX85401.1 | Marpi_0649 | Marpi_0989 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.786 |
| AEX85087.1 | AEX86131.1 | Marpi_0649 | Marpi_1745 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.786 |
| AEX85087.1 | dnaK | Marpi_0649 | Marpi_0460 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
| AEX85087.1 | groL | Marpi_0649 | Marpi_1900 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.768 |
| AEX85087.1 | groS | Marpi_0649 | Marpi_1899 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.704 |
| AEX85087.1 | grpE | Marpi_0649 | Marpi_1207 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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. [...] | 0.912 |
| AEX85087.1 | hrcA | Marpi_0649 | Marpi_1208 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.717 |
| AEX85087.1 | rplP | Marpi_0649 | Marpi_0873 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Ribosomal protein L16, bacterial/organelle; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family. | 0.781 |
| AEX85401.1 | AEX85087.1 | Marpi_0989 | Marpi_0649 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.786 |
| AEX85401.1 | dnaJ | Marpi_0989 | Marpi_1206 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein 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, D [...] | 0.786 |
| AEX85401.1 | dnaK | Marpi_0989 | Marpi_0460 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.957 |
| AEX85401.1 | groL | Marpi_0989 | Marpi_1900 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.697 |
| AEX85401.1 | groS | Marpi_0989 | Marpi_1899 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.706 |
| AEX85401.1 | grpE | Marpi_0989 | Marpi_1207 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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. [...] | 0.816 |
| AEX85401.1 | hrcA | Marpi_0989 | Marpi_1208 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.637 |
| AEX85706.1 | dnaK | Marpi_1303 | Marpi_0460 | PFAM: NifU-like N terminal domain; TIGRFAM: SUF system FeS assembly protein, NifU family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.930 |
| AEX86131.1 | AEX85087.1 | Marpi_1745 | Marpi_0649 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.786 |
| AEX86131.1 | dnaJ | Marpi_1745 | Marpi_1206 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein 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, D [...] | 0.786 |
| AEX86131.1 | dnaK | Marpi_1745 | Marpi_0460 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.957 |
| AEX86131.1 | groL | Marpi_1745 | Marpi_1900 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.697 |
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