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 |
| CAZ95249.1 | dppA1 | ZOBELLIA_1192 | ZOBELLIA_1190 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.544 |
| CAZ95249.1 | dtpT | ZOBELLIA_1192 | ZOBELLIA_1189 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.435 |
| CAZ95249.1 | mvaA | ZOBELLIA_1192 | ZOBELLIA_1191 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.964 |
| CAZ96783.1 | dppA1 | ZOBELLIA_2633 | ZOBELLIA_1190 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.533 |
| CAZ96783.1 | dtpT | ZOBELLIA_2633 | ZOBELLIA_1189 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.441 |
| dppA1 | CAZ95249.1 | ZOBELLIA_1190 | ZOBELLIA_1192 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 0.544 |
| dppA1 | CAZ96783.1 | ZOBELLIA_1190 | ZOBELLIA_2633 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.533 |
| dppA1 | dtpT | ZOBELLIA_1190 | ZOBELLIA_1189 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.642 |
| dppA1 | mvaA | ZOBELLIA_1190 | ZOBELLIA_1191 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.551 |
| dtpT | CAZ95249.1 | ZOBELLIA_1189 | ZOBELLIA_1192 | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 0.435 |
| dtpT | CAZ96783.1 | ZOBELLIA_1189 | ZOBELLIA_2633 | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.441 |
| dtpT | dppA1 | ZOBELLIA_1189 | ZOBELLIA_1190 | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.642 |
| dtpT | mvaA | ZOBELLIA_1189 | ZOBELLIA_1191 | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.406 |
| mvaA | CAZ95249.1 | ZOBELLIA_1191 | ZOBELLIA_1192 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 0.964 |
| mvaA | dppA1 | ZOBELLIA_1191 | ZOBELLIA_1190 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.551 |
| mvaA | dtpT | ZOBELLIA_1191 | ZOBELLIA_1189 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Di-/tripeptide transporter; DtpT a membrane permease responsible for the intake of di- or tri-peptides with the concomitant uptake of a proton. Features twelve transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.406 |