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 |
KRH_12500 | KRH_14010 | KRH_12500 | KRH_14010 | Putative lipoate-protein ligase. | Hypothetical protein. | 0.900 |
KRH_12500 | KRH_14420 | KRH_12500 | KRH_14420 | Putative lipoate-protein ligase. | Dihydrolipoamide acyltransferase. | 0.583 |
KRH_12500 | gcvH | KRH_12500 | KRH_15100 | Putative lipoate-protein ligase. | Glycine cleavage system H-protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.910 |
KRH_12500 | lipA | KRH_12500 | KRH_14460 | Putative lipoate-protein ligase. | Lipoyl synthase; 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. | 0.936 |
KRH_12500 | lipB | KRH_12500 | KRH_14450 | Putative lipoate-protein ligase. | Lipoate-protein ligase B; 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. | 0.917 |
KRH_12500 | sucA | KRH_12500 | KRH_09450 | Putative lipoate-protein ligase. | 2-oxoglutarate dehydrogenase E1 component; Protein synonym:alpha-ketoglutarate dehydrogenase. | 0.873 |
KRH_14010 | KRH_12500 | KRH_14010 | KRH_12500 | Hypothetical protein. | Putative lipoate-protein ligase. | 0.900 |
KRH_14010 | KRH_14420 | KRH_14010 | KRH_14420 | Hypothetical protein. | Dihydrolipoamide acyltransferase. | 0.583 |
KRH_14010 | gcvH | KRH_14010 | KRH_15100 | Hypothetical protein. | Glycine cleavage system H-protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.859 |
KRH_14010 | lipA | KRH_14010 | KRH_14460 | Hypothetical protein. | Lipoyl synthase; 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. | 0.920 |
KRH_14010 | lipB | KRH_14010 | KRH_14450 | Hypothetical protein. | Lipoate-protein ligase B; 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. | 0.917 |
KRH_14010 | sucA | KRH_14010 | KRH_09450 | Hypothetical protein. | 2-oxoglutarate dehydrogenase E1 component; Protein synonym:alpha-ketoglutarate dehydrogenase. | 0.873 |
KRH_14420 | KRH_12500 | KRH_14420 | KRH_12500 | Dihydrolipoamide acyltransferase. | Putative lipoate-protein ligase. | 0.583 |
KRH_14420 | KRH_14010 | KRH_14420 | KRH_14010 | Dihydrolipoamide acyltransferase. | Hypothetical protein. | 0.583 |
KRH_14420 | gcvH | KRH_14420 | KRH_15100 | Dihydrolipoamide acyltransferase. | Glycine cleavage system H-protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.649 |
KRH_14420 | gcvP | KRH_14420 | KRH_05980 | Dihydrolipoamide acyltransferase. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.521 |
KRH_14420 | lipA | KRH_14420 | KRH_14460 | Dihydrolipoamide acyltransferase. | Lipoyl synthase; 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. | 0.569 |
KRH_14420 | lipB | KRH_14420 | KRH_14450 | Dihydrolipoamide acyltransferase. | Lipoate-protein ligase B; 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. | 0.607 |
KRH_14420 | sucA | KRH_14420 | KRH_09450 | Dihydrolipoamide acyltransferase. | 2-oxoglutarate dehydrogenase E1 component; Protein synonym:alpha-ketoglutarate dehydrogenase. | 0.995 |
KRH_14470 | lipA | KRH_14470 | KRH_14460 | Hypothetical membrane protein. | Lipoyl synthase; 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. | 0.567 |
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