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 |
| CAZ94331.1 | CAZ97344.1 | ZOBELLIA_258 | ZOBELLIA_3206 | Kelch repeats protein; Contains a N-terminal domain of unknown function and a C-terminal domain displaying three Kelch repeats. The kelch motif forms a beta sheet and several of these sheets associate to form a beta propeller structure; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.420 |
| CAZ97343.1 | CAZ97344.1 | ZOBELLIA_3205 | ZOBELLIA_3206 | Conserved hypothetical protein; Localized in the cytoplasm. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.401 |
| CAZ97344.1 | CAZ94331.1 | ZOBELLIA_3206 | ZOBELLIA_258 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | Kelch repeats protein; Contains a N-terminal domain of unknown function and a C-terminal domain displaying three Kelch repeats. The kelch motif forms a beta sheet and several of these sheets associate to form a beta propeller structure; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.420 |
| CAZ97344.1 | CAZ97343.1 | ZOBELLIA_3206 | ZOBELLIA_3205 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.401 |
| CAZ97344.1 | arcB | ZOBELLIA_3206 | ZOBELLIA_4271 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.507 |
| CAZ97344.1 | iyd | ZOBELLIA_3206 | ZOBELLIA_4305 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | Iodotyrosine dehalogenase catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Uses FMN and NADPH as cofactors. Belongs to the nitroreductase family. Localized in the cytoplasm; Hypothetical protein. | 0.421 |
| CAZ97344.1 | nglA | ZOBELLIA_3206 | ZOBELLIA_1027 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | Alpha-N-acetylglucosaminidase, family GH89; Alpha-N-acetylglucosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. It belongs to the family 89 of the glycoside hydrolases. In human, this enzyme is involved in the degradation of heparan sulfate. Signal peptide cleaved between the residues 20 and 21. Localized in the periplasmic space; High confidence in function and specificity. | 0.514 |
| arcB | CAZ97344.1 | ZOBELLIA_4271 | ZOBELLIA_3206 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.507 |
| iyd | CAZ97344.1 | ZOBELLIA_4305 | ZOBELLIA_3206 | Iodotyrosine dehalogenase catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Uses FMN and NADPH as cofactors. Belongs to the nitroreductase family. Localized in the cytoplasm; Hypothetical protein. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.421 |
| nglA | CAZ97344.1 | ZOBELLIA_1027 | ZOBELLIA_3206 | Alpha-N-acetylglucosaminidase, family GH89; Alpha-N-acetylglucosaminidase catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. It belongs to the family 89 of the glycoside hydrolases. In human, this enzyme is involved in the degradation of heparan sulfate. Signal peptide cleaved between the residues 20 and 21. Localized in the periplasmic space; High confidence in function and specificity. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.514 |