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 |
| CAZ95679.1 | trxA-3 | ZOBELLIA_1624 | ZOBELLIA_3485 | Rubredoxin family protein; Conserved protein containing a C-terminal Rubredoxin-like domain. The most conserved feature of the rubredoxin-like domain is the cluster of four cysteines involved in iron binding (Cys-x-x-Cys-x(n)-Cys-x-x-Cys). This domain folds into a short three-stranded antiparallel beta-sheet and a number of loops; Localized in the cytoplasm; Family membership. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.479 |
| CAZ97621.1 | CAZ97622.1 | ZOBELLIA_3483 | ZOBELLIA_3484 | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains two copies of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS- box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains one N-terminal copy of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS-box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | 0.639 |
| CAZ97621.1 | trxA-3 | ZOBELLIA_3483 | ZOBELLIA_3485 | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains two copies of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS- box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.465 |
| CAZ97622.1 | CAZ97621.1 | ZOBELLIA_3484 | ZOBELLIA_3483 | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains one N-terminal copy of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS-box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains two copies of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS- box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | 0.639 |
| CAZ97622.1 | trxA-3 | ZOBELLIA_3484 | ZOBELLIA_3485 | Stress protein probably induced when the cell is exposed to stress agents or when conditions cause growth arrest; Contains one N-terminal copy of the universal stress protein (usp) domain; Belongs to the Usp family. Members of the Usp family are predicted to be related to the MADS-box proteins and bind to DNA; Localized in the cytoplasm; Family membership. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.570 |
| CAZ97624.1 | trxA-3 | ZOBELLIA_3486 | ZOBELLIA_3485 | Conserved hypothetical protein; Localized in the cytoplasm. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.525 |
| cbpA | dnaK | ZOBELLIA_3574 | ZOBELLIA_4708 | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.977 |
| cbpA | fusA | ZOBELLIA_3574 | ZOBELLIA_2508 | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...] | 0.712 |
| cbpA | grpE | ZOBELLIA_3574 | ZOBELLIA_2823 | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Co-chaperone HSP-70 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. Several rounds of [...] | 0.790 |
| cbpA | trxA-3 | ZOBELLIA_3574 | ZOBELLIA_3485 | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.605 |
| dnaJ | dnaK | ZOBELLIA_2824 | ZOBELLIA_4708 | Co-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 [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.985 |
| dnaJ | fusA | ZOBELLIA_2824 | ZOBELLIA_2508 | Co-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 [...] | Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...] | 0.745 |
| dnaJ | grpE | ZOBELLIA_2824 | ZOBELLIA_2823 | Co-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 [...] | Co-chaperone HSP-70 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. Several rounds of [...] | 0.987 |
| dnaJ | trxA-3 | ZOBELLIA_2824 | ZOBELLIA_3485 | Co-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 [...] | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.633 |
| dnaK | cbpA | ZOBELLIA_4708 | ZOBELLIA_3574 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.977 |
| dnaK | dnaJ | ZOBELLIA_4708 | ZOBELLIA_2824 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-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 [...] | 0.985 |
| dnaK | fusA | ZOBELLIA_4708 | ZOBELLIA_2508 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...] | 0.761 |
| dnaK | grpE | ZOBELLIA_4708 | ZOBELLIA_2823 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperone HSP-70 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. Several rounds of [...] | 0.994 |
| dnaK | trxA-3 | ZOBELLIA_4708 | ZOBELLIA_3485 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Thioredoxin is a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase; Localized in the cytoplasm; High confidence in function and specificity. | 0.570 |
| fusA | cbpA | ZOBELLIA_2508 | ZOBELLIA_3574 | Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...] | CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.712 |
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