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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ate1 | Ntan1 | FBpp0307617 | FBpp0291076 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). | protein-N-terminal asparagine amidohydrolase activity. It is involved in the biological process described with: positive regulation of DNA endoreduplication; ubiquitin-dependent protein catabolic process via the N-end rule pathway; negative regulation of glial cell proliferation; ubiquitin-dependent protein catabolic process. | 0.907 |
| Ate1 | Ubr1 | FBpp0307617 | FBpp0312009 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). | E3 ubiquitin-protein ligase UBR1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Belongs to the UBR1 family. | 0.941 |
| Ate1 | tun | FBpp0307617 | FBpp0300971 | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.749 |
| CG14969 | CG46280 | FBpp0072944 | FBpp0401443 | GH26007p. | RE12073p. | 0.648 |
| CG14969 | CG9547 | FBpp0072944 | FBpp0078893 | GH26007p. | GH06693p; glutaryl-CoA dehydrogenase activity; flavin adenine dinucleotide binding; fatty-acyl-CoA binding. It is involved in the biological process described with: fatty acid beta-oxidation using acyl-CoA dehydrogenase; lysine catabolic process; hydroxylysine catabolic process; fatty-acyl-CoA biosynthetic process; tryptophan metabolic process. | 0.613 |
| CG14969 | Tgt | FBpp0072944 | FBpp0077636 | GH26007p. | Queuine tRNA-ribosyltransferase catalytic subunit; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming [...] | 0.641 |
| CG14969 | tun | FBpp0072944 | FBpp0300971 | GH26007p. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.641 |
| CG46280 | CG14969 | FBpp0401443 | FBpp0072944 | RE12073p. | GH26007p. | 0.648 |
| CG46280 | Tgt | FBpp0401443 | FBpp0077636 | RE12073p. | Queuine tRNA-ribosyltransferase catalytic subunit; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming [...] | 0.429 |
| CG46280 | tun | FBpp0401443 | FBpp0300971 | RE12073p. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.650 |
| CG8060 | tun | FBpp0086322 | FBpp0300971 | Protein tyrosine kinase inhibitor activity. It is involved in the biological process described with: negative regulation of protein tyrosine kinase activity. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.636 |
| CG9288 | tun | FBpp0082297 | FBpp0300971 | Protein Abitram; May regulate actin polymerization. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.608 |
| CG9547 | CG14969 | FBpp0078893 | FBpp0072944 | GH06693p; glutaryl-CoA dehydrogenase activity; flavin adenine dinucleotide binding; fatty-acyl-CoA binding. It is involved in the biological process described with: fatty acid beta-oxidation using acyl-CoA dehydrogenase; lysine catabolic process; hydroxylysine catabolic process; fatty-acyl-CoA biosynthetic process; tryptophan metabolic process. | GH26007p. | 0.613 |
| CG9547 | Tgt | FBpp0078893 | FBpp0077636 | GH06693p; glutaryl-CoA dehydrogenase activity; flavin adenine dinucleotide binding; fatty-acyl-CoA binding. It is involved in the biological process described with: fatty acid beta-oxidation using acyl-CoA dehydrogenase; lysine catabolic process; hydroxylysine catabolic process; fatty-acyl-CoA biosynthetic process; tryptophan metabolic process. | Queuine tRNA-ribosyltransferase catalytic subunit; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming [...] | 0.646 |
| CG9547 | tun | FBpp0078893 | FBpp0300971 | GH06693p; glutaryl-CoA dehydrogenase activity; flavin adenine dinucleotide binding; fatty-acyl-CoA binding. It is involved in the biological process described with: fatty acid beta-oxidation using acyl-CoA dehydrogenase; lysine catabolic process; hydroxylysine catabolic process; fatty-acyl-CoA biosynthetic process; tryptophan metabolic process. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.637 |
| Ntan1 | Ate1 | FBpp0291076 | FBpp0307617 | protein-N-terminal asparagine amidohydrolase activity. It is involved in the biological process described with: positive regulation of DNA endoreduplication; ubiquitin-dependent protein catabolic process via the N-end rule pathway; negative regulation of glial cell proliferation; ubiquitin-dependent protein catabolic process. | Arginyl-tRNA--protein transferase 1; Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). | 0.907 |
| Ntan1 | Ubr1 | FBpp0291076 | FBpp0312009 | protein-N-terminal asparagine amidohydrolase activity. It is involved in the biological process described with: positive regulation of DNA endoreduplication; ubiquitin-dependent protein catabolic process via the N-end rule pathway; negative regulation of glial cell proliferation; ubiquitin-dependent protein catabolic process. | E3 ubiquitin-protein ligase UBR1; E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Belongs to the UBR1 family. | 0.806 |
| Ntan1 | tun | FBpp0291076 | FBpp0300971 | protein-N-terminal asparagine amidohydrolase activity. It is involved in the biological process described with: positive regulation of DNA endoreduplication; ubiquitin-dependent protein catabolic process via the N-end rule pathway; negative regulation of glial cell proliferation; ubiquitin-dependent protein catabolic process. | Protein N-terminal glutamine amidohydrolase; Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Belongs to the NTAQ1 family. | 0.945 |
| Tgt | CG14969 | FBpp0077636 | FBpp0072944 | Queuine tRNA-ribosyltransferase catalytic subunit; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming [...] | GH26007p. | 0.641 |
| Tgt | CG46280 | FBpp0077636 | FBpp0401443 | Queuine tRNA-ribosyltransferase catalytic subunit; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming [...] | RE12073p. | 0.429 |
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