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 |
| BDEG_20523 | BDEG_21123 | A0A177W8A6 | A0A177WBE2 | Nfu_N domain-containing protein. | Aconitate hydratase, mitochondrial; Belongs to the aconitase/IPM isomerase family. | 0.681 |
| BDEG_20523 | BDEG_21381 | A0A177W8A6 | A0A177WB83 | Nfu_N domain-containing protein. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.524 |
| BDEG_20523 | BDEG_22327 | A0A177W8A6 | A0A177WE43 | Nfu_N domain-containing protein. | CN hydrolase domain-containing protein. | 0.468 |
| BDEG_20523 | BDEG_26245 | A0A177W8A6 | A0A177WRV6 | Nfu_N domain-containing protein. | Uncharacterized protein; Belongs to the BolA/IbaG family. | 0.618 |
| BDEG_20523 | BDEG_26885 | A0A177W8A6 | A0A177WUF7 | Nfu_N domain-containing protein. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.639 |
| BDEG_20708 | BDEG_26885 | A0A177W9W9 | A0A177WUF7 | Uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.613 |
| BDEG_21123 | BDEG_20523 | A0A177WBE2 | A0A177W8A6 | Aconitate hydratase, mitochondrial; Belongs to the aconitase/IPM isomerase family. | Nfu_N domain-containing protein. | 0.681 |
| BDEG_21123 | BDEG_26885 | A0A177WBE2 | A0A177WUF7 | Aconitate hydratase, mitochondrial; Belongs to the aconitase/IPM isomerase family. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.576 |
| BDEG_21381 | BDEG_20523 | A0A177WB83 | A0A177W8A6 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Nfu_N domain-containing protein. | 0.524 |
| BDEG_21381 | BDEG_21472 | A0A177WB83 | A0A177WCK1 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | 0.989 |
| BDEG_21381 | BDEG_22327 | A0A177WB83 | A0A177WE43 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | CN hydrolase domain-containing protein. | 0.792 |
| BDEG_21381 | BDEG_26063 | A0A177WB83 | A0A177WRB6 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | BPL/LPL catalytic domain-containing protein. | 0.885 |
| BDEG_21381 | BDEG_26885 | A0A177WB83 | A0A177WUF7 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.991 |
| BDEG_21381 | BDEG_27154 | A0A177WB83 | A0A177WUS6 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Lactamase_B domain-containing protein. | 0.459 |
| BDEG_21472 | BDEG_21381 | A0A177WCK1 | A0A177WB83 | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.989 |
| BDEG_21472 | BDEG_26063 | A0A177WCK1 | A0A177WRB6 | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | BPL/LPL catalytic domain-containing protein. | 0.973 |
| BDEG_21472 | BDEG_26885 | A0A177WCK1 | A0A177WUF7 | Glycine cleavage system H protein; The H protein shuttles the methylamine group of glycine from the P protein to the T protein; Belongs to the GcvH family. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.988 |
| BDEG_22327 | BDEG_20523 | A0A177WE43 | A0A177W8A6 | CN hydrolase domain-containing protein. | Nfu_N domain-containing protein. | 0.468 |
| BDEG_22327 | BDEG_21381 | A0A177WE43 | A0A177WB83 | CN hydrolase domain-containing protein. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.792 |
| BDEG_22327 | BDEG_26885 | A0A177WE43 | A0A177WUF7 | CN hydrolase domain-containing protein. | Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.803 |
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