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 |
| ank1 | azo1211 | azo1599 | azo1211 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.882 |
| ank1 | azo1598 | azo1599 | azo1598 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Putative deoxyribonuclease yabD (EC 3.1.21.-). InterPro: Uncharacterized protein family UPF0006. TIGR00010: deoxyribonuclease TatD family; Specificity unclear. | 0.800 |
| ank1 | azo3617 | azo1599 | azo3617 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 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 [...] | 0.918 |
| ank1 | fdh1B | azo1599 | azo3039 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity. | 0.898 |
| ank1 | gmk | azo1599 | azo3953 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | 0.800 |
| ank1 | hoxF | azo1599 | azo1412 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity. | 0.898 |
| ank1 | hrpA | azo1599 | azo0716 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | ATP-dependent helicase hrpA. Not yet known. InterPro: DEAD/DEAH box helicase; High confidence in function and specificity. | 0.883 |
| ank1 | petB | azo1599 | azo0961 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Ubiquinol-cytochrome c reductase cytochrome b protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.835 |
| ank1 | rpsC | azo1599 | azo3411 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family. | 0.852 |
| ank1 | sbcD | azo1599 | azo0199 | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | Exonuclease SbcD, putative; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family. | 0.872 |
| azo1211 | ank1 | azo1211 | azo1599 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.882 |
| azo1211 | azo3617 | azo1211 | azo3617 | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 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 [...] | 0.555 |
| azo1598 | ank1 | azo1598 | azo1599 | Putative deoxyribonuclease yabD (EC 3.1.21.-). InterPro: Uncharacterized protein family UPF0006. TIGR00010: deoxyribonuclease TatD family; Specificity unclear. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.800 |
| azo3617 | ank1 | azo3617 | azo1599 | 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 ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.918 |
| azo3617 | azo1211 | azo3617 | azo1211 | 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 [...] | Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs. | 0.555 |
| azo3617 | gmk | azo3617 | azo3953 | 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 [...] | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | 0.957 |
| fdh1B | ank1 | azo3039 | azo1599 | Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.898 |
| fdh1B | hoxF | azo3039 | azo1412 | Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity. | Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity. | 0.998 |
| fdh1B | petB | azo3039 | azo0961 | Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity. | Ubiquinol-cytochrome c reductase cytochrome b protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.938 |
| gmk | ank1 | azo3953 | azo1599 | Guanylate kinase; Essential for recycling GMP and indirectly, cGMP. | Putative ankyrin repeat harbouring exported protein; Hypothetical protein KIAA1223 (Fragment). TREMBL:Q8XYH0:35% identity; TREMBL:Q7VXC9:35% The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes.Each Ankyrin repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90 angle. The repeats stack together to form an L-shaped structure InterPro [...] | 0.800 |
page 1 of 2