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 |
| azo3617 | dnaJ1 | azo3617 | azo1062 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 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 [...] | 0.505 |
| azo3617 | dnaJ2 | azo3617 | azo1266 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 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. | 0.505 |
| azo3617 | ndk | azo3617 | azo0923 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.894 |
| azo3617 | ppiA | azo3617 | azo1057 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.805 |
| azo3617 | ppiB | azo3617 | azo1056 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.805 |
| azo3617 | yakC | azo3617 | azo2535 | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | Probable aldo-keto reductase. Homology to yakC of S.pombe of 43% (sprot|YAKC_SCHPO). Catalyze the reduction of 2-nitorbenzaldehyde, pyridine-2-aldehyde and 2-phthaladehyde. Pfam: Aldo/Keto reductase signal peptide no TMHs; Family membership. | 0.536 |
| dnaJ1 | azo3617 | azo1062 | azo3617 | 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 [...] | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.505 |
| dnaJ1 | ndk | azo1062 | azo0923 | 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 [...] | Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.829 |
| dnaJ1 | ppiA | azo1062 | azo1057 | 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 peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.827 |
| dnaJ1 | ppiB | azo1062 | azo1056 | 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 [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.827 |
| dnaJ1 | yakC | azo1062 | azo2535 | 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 aldo-keto reductase. Homology to yakC of S.pombe of 43% (sprot|YAKC_SCHPO). Catalyze the reduction of 2-nitorbenzaldehyde, pyridine-2-aldehyde and 2-phthaladehyde. Pfam: Aldo/Keto reductase signal peptide no TMHs; Family membership. | 0.534 |
| dnaJ2 | azo3617 | azo1266 | azo3617 | 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. | Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...] | 0.505 |
| dnaJ2 | ndk | azo1266 | azo0923 | 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. | Nucleoside-diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.829 |
| dnaJ2 | ppiA | azo1266 | azo1057 | 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. | Probable peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.827 |
| dnaJ2 | ppiB | azo1266 | azo1056 | 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. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.827 |
| dnaJ2 | yakC | azo1266 | azo2535 | 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. | Probable aldo-keto reductase. Homology to yakC of S.pombe of 43% (sprot|YAKC_SCHPO). Catalyze the reduction of 2-nitorbenzaldehyde, pyridine-2-aldehyde and 2-phthaladehyde. Pfam: Aldo/Keto reductase signal peptide no TMHs; Family membership. | 0.534 |
| ligC | ligI | azo2536 | azo2539 | Hypothetical oxidoreductase yrbE (EC 1.-.-.-). TREMBL:Q93PS4:90% identity; 93% similarity. This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyze the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and gala [...] | Probable 2-pyrone-4,6-dicarboxylate hydrolase. Homology to ligI of S. paucimobilis of 55% (tremble:O87170) Pfam: Amidohydrolase no signal peptide no TMHs; High confidence in function and specificity. | 0.967 |
| ligC | yafB | azo2536 | azo3631 | Hypothetical oxidoreductase yrbE (EC 1.-.-.-). TREMBL:Q93PS4:90% identity; 93% similarity. This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyze the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and gala [...] | 25-diketo-D-gluconic acid reductase B (EC 1.1.1.274) (25-DKG reductase B) (25-DKGR B) (25DKGR-B) (AKR5D). TREMBL:Q8Y090: 67% identity, 78% similarity. Catalyzes the reduction of 25-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG) (By similarity). subunit:monomer (by similarity). subcellular location:cytoplasmic (by similarity). 2-keto-l-gulonic acid is a key intermediate in the production of l-ascorbic acid (vitamin c). belongs to the aldo/keto reductase family InterPro:IPR001395; Aldo/ket_red. Pfam:PF00248; aldo_ket_red; 1. PRINTS PR00069; ALDKETRDTAS ribH: riboflavin sy [...] | 0.604 |
| ligC | yakC | azo2536 | azo2535 | Hypothetical oxidoreductase yrbE (EC 1.-.-.-). TREMBL:Q93PS4:90% identity; 93% similarity. This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyze the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and gala [...] | Probable aldo-keto reductase. Homology to yakC of S.pombe of 43% (sprot|YAKC_SCHPO). Catalyze the reduction of 2-nitorbenzaldehyde, pyridine-2-aldehyde and 2-phthaladehyde. Pfam: Aldo/Keto reductase signal peptide no TMHs; Family membership. | 0.795 |
| ligI | ligC | azo2539 | azo2536 | Probable 2-pyrone-4,6-dicarboxylate hydrolase. Homology to ligI of S. paucimobilis of 55% (tremble:O87170) Pfam: Amidohydrolase no signal peptide no TMHs; High confidence in function and specificity. | Hypothetical oxidoreductase yrbE (EC 1.-.-.-). TREMBL:Q93PS4:90% identity; 93% similarity. This group of enzymes utilise NADP or NAD, and is known as the GFO/IDH/MOCA family in Swiss-Prot. GFO is a glucose--fructose oxidoreductase, which converts D-glucose and D-fructose into D-gluconolactone and D-glucitol in the sorbitol-gluconate pathway. MOCA is a rhizopine catabolism protein which may catalyze the NADH-dependent dehydrogenase reaction involved in rhizopine catabolism. Other proteins belonging to this family include Gal80, a negative regulator for the expression of lactose and gala [...] | 0.967 |
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