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 |
| CAZ94176.1 | CAZ94177.1 | ZOBELLIA_103 | ZOBELLIA_104 | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.547 |
| CAZ94177.1 | CAZ94176.1 | ZOBELLIA_104 | ZOBELLIA_103 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | DEAD/DEAH RNA helicase; Protein that could be involved in ATP-dependent RNA unwinding in a variety of cellular processes, including ribosome assembly, protein synthesis, and RNA degradation; Contains a DEAD box; Belongs to the helicases superfamily II, DEAD/DEAH box RNA helicase family, DEAD box subfamily; Localized in the cytoplasm; Family membership. | 0.547 |
| CAZ94177.1 | CAZ94794.1 | ZOBELLIA_104 | ZOBELLIA_728 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Conserved hypothetical protein. | 0.514 |
| CAZ94177.1 | CAZ95898.1 | ZOBELLIA_104 | ZOBELLIA_1845 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Conserved hypothetical protein; Localized in the cytoplasm. | 0.596 |
| CAZ94794.1 | CAZ94177.1 | ZOBELLIA_728 | ZOBELLIA_104 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Conserved hypothetical protein. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.514 |
| CAZ95898.1 | CAZ94177.1 | ZOBELLIA_1845 | ZOBELLIA_104 | Conserved hypothetical protein; Localized in the cytoplasm. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.596 |