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 |
| BPSL0763 | dnaJ | BPSL0763 | BPSL2826 | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | Putative DnaJ chaperone protein; 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 betwee [...] | 0.836 |
| BPSL0763 | dnaK | BPSL0763 | BPSL2827 | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.818 |
| BPSL0763 | groEL | BPSL0763 | BPSL2697 | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.523 |
| BPSL0763 | groL | BPSL0763 | BPSS0477 | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.523 |
| BPSL0763 | htpG | BPSL0763 | BPSL1087 | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.785 |
| dnaJ | BPSL0763 | BPSL2826 | BPSL0763 | Putative DnaJ chaperone protein; 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 betwee [...] | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | 0.836 |
| dnaJ | dnaK | BPSL2826 | BPSL2827 | Putative DnaJ chaperone protein; 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 betwee [...] | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ | groEL | BPSL2826 | BPSL2697 | Putative DnaJ chaperone protein; 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 betwee [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.892 |
| dnaJ | groES1 | BPSL2826 | BPSL2698 | Putative DnaJ chaperone protein; 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 betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.826 |
| dnaJ | groES2 | BPSL2826 | BPSL2919 | Putative DnaJ chaperone protein; 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 betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.828 |
| dnaJ | groL | BPSL2826 | BPSS0477 | Putative DnaJ chaperone protein; 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 betwee [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.899 |
| dnaJ | groS | BPSL2826 | BPSS0476 | Putative DnaJ chaperone protein; 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 betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.828 |
| dnaJ | grpE | BPSL2826 | BPSL2829 | Putative DnaJ chaperone protein; 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 betwee [...] | Conserved hypothetical protein (pseudogene); 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. Se [...] | 0.997 |
| dnaJ | htpG | BPSL2826 | BPSL1087 | Putative DnaJ chaperone protein; 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 betwee [...] | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.996 |
| dnaK | BPSL0763 | BPSL2827 | BPSL0763 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative helicase SNF2 family protein; Similar to Bacteroides nodosus putative DEAH ATP-dependent helicase SWALL:O32494 (EMBL:U20246) (965 aa) fasta scores: E(): 2.4e-28, 28.84% id in 780 aa, and to Xanthomonas campestris helicase xcc0524 SWALL:AAM39840 (EMBL:AE012150) (967 aa) fasta scores: E(): 1.8e-11, 25.36% id in 962 aa, and to Halobacterium sp. similar to Escherichia coli vng5141g or vng6139G SWALL:O52003 (EMBL:AF016485) (979 aa) fasta scores: E(): 1.9e-10, 27.33% id in 995 aa. Possible alternative translational start site. | 0.818 |
| dnaK | dnaJ | BPSL2827 | BPSL2826 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative DnaJ chaperone protein; 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 betwee [...] | 0.998 |
| dnaK | groEL | BPSL2827 | BPSL2697 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.934 |
| dnaK | groES1 | BPSL2827 | BPSL2698 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.832 |
| dnaK | groES2 | BPSL2827 | BPSL2919 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.834 |
| dnaK | groL | BPSL2827 | BPSS0477 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.935 |
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