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 |
| azo2661 | azo3626 | azo2661 | azo3626 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 0.963 |
| azo2661 | dnaK | azo2661 | azo1063 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.963 |
| azo2661 | groEL1 | azo2661 | azo0974 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.660 |
| azo2661 | groEL2 | azo2661 | azo1223 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Probable chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.660 |
| azo2661 | groEL3 | azo2661 | azo2366 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.660 |
| azo2661 | grpE | azo2661 | azo1064 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Probable heat shock protein GrpE; 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. Several round [...] | 0.920 |
| azo2661 | hrcA | azo2661 | azo2581 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Heat-inducible transcriptional repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.716 |
| azo2661 | hscA | azo2661 | azo2012 | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.963 |
| azo3626 | azo2661 | azo3626 | azo2661 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs. | 0.963 |
| azo3626 | dnaJ1 | azo3626 | azo1062 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 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 [...] | 0.973 |
| azo3626 | dnaJ2 | azo3626 | azo1266 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | 0.973 |
| azo3626 | groEL1 | azo3626 | azo0974 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.846 |
| azo3626 | groEL2 | azo3626 | azo1223 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Probable chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.846 |
| azo3626 | groEL3 | azo3626 | azo2366 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.846 |
| azo3626 | grpE | azo3626 | azo1064 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Probable heat shock protein GrpE; 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. Several round [...] | 0.978 |
| azo3626 | hrcA | azo3626 | azo2581 | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | Heat-inducible transcriptional repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.826 |
| dnaJ1 | azo3626 | azo1062 | azo3626 | 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 [...] | Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership. | 0.973 |
| dnaJ1 | dnaK | azo1062 | azo1063 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ1 | groEL1 | azo1062 | azo0974 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.782 |
| dnaJ1 | groEL2 | azo1062 | azo1223 | 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 [...] | Probable chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.781 |
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