Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but at higher resolution
... 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 |
PC1_1224 | mug | PC1_1224 | PC1_0547 | Deoxyribodipyrimidine photo-lyase; PFAM: DNA photolyase FAD-binding; DNA photolyase domain protein; KEGG: eca:ECA1349 deoxyribodipyrimidine photolyase. | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | 0.594 |
PC1_1974 | mug | PC1_1974 | PC1_0547 | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: eca:ECA2335 exonuclease III. | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | 0.740 |
PC1_1974 | polA | PC1_1974 | PC1_4227 | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: eca:ECA2335 exonuclease III. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.833 |
PC1_3479 | mug | PC1_3479 | PC1_0547 | PFAM: monooxygenase FAD-binding; KEGG: cvi:CV_1403 hypothetical protein. | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | 0.441 |
mug | PC1_1224 | PC1_0547 | PC1_1224 | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | Deoxyribodipyrimidine photo-lyase; PFAM: DNA photolyase FAD-binding; DNA photolyase domain protein; KEGG: eca:ECA1349 deoxyribodipyrimidine photolyase. | 0.594 |
mug | PC1_1974 | PC1_0547 | PC1_1974 | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: eca:ECA2335 exonuclease III. | 0.740 |
mug | PC1_3479 | PC1_0547 | PC1_3479 | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | PFAM: monooxygenase FAD-binding; KEGG: cvi:CV_1403 hypothetical protein. | 0.441 |
mug | polA | PC1_0547 | PC1_4227 | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.406 |
polA | PC1_1974 | PC1_4227 | PC1_1974 | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: eca:ECA2335 exonuclease III. | 0.833 |
polA | mug | PC1_4227 | PC1_0547 | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | Uracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. | 0.406 |