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 |
| QY95_01080 | prfA | QY95_01080 | QY95_01083 | Threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | 0.459 |
| QY95_01080 | prmC | QY95_01080 | QY95_01082 | Threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.955 |
| QY95_03049 | prmC | QY95_03049 | QY95_01082 | Membrane protein YqhQ. | Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.912 |
| QY95_03106 | prmC | QY95_03106 | QY95_01082 | ASCH domain-containing protein. | Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.832 |
| atpA | atpC | QY95_01065 | QY95_01062 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
| atpA | atpD | QY95_01065 | QY95_01063 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
| atpA | atpE | QY95_01065 | QY95_01068 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpA | atpG | QY95_01065 | QY95_01064 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
| atpA | atpH | QY95_01065 | QY95_01066 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpA | prmC | QY95_01065 | QY95_01082 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.738 |
| atpC | atpA | QY95_01062 | QY95_01065 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
| atpC | atpD | QY95_01062 | QY95_01063 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
| atpC | atpE | QY95_01062 | QY95_01068 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpC | atpG | QY95_01062 | QY95_01064 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
| atpC | atpH | QY95_01062 | QY95_01066 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpC | prmC | QY95_01062 | QY95_01082 | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | Release factor glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.730 |
| atpD | atpA | QY95_01063 | QY95_01065 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
| atpD | atpC | QY95_01063 | QY95_01062 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
| atpD | atpE | QY95_01063 | QY95_01068 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpD | atpG | QY95_01063 | QY95_01064 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATP synthase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
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