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 |
| BLVRA | BLVRB | ENSPPYP00000019733 | ENSPPYP00000011187 | Biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. | BLVRB isoform 1. | 0.968 |
| BLVRA | HMOX1 | ENSPPYP00000019733 | ENSPPYP00000013121 | Biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.981 |
| BLVRA | HMOX2 | ENSPPYP00000019733 | ENSPPYP00000007986 | Biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. | HMOX2 isoform 7. | 0.971 |
| BLVRA | POR | ENSPPYP00000019733 | ENSPPYP00000019589 | Biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. | NADPH--cytochrome P450 reductase; This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5; In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. | 0.525 |
| BLVRB | BLVRA | ENSPPYP00000011187 | ENSPPYP00000019733 | BLVRB isoform 1. | Biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. | 0.968 |
| BLVRB | HMOX1 | ENSPPYP00000011187 | ENSPPYP00000013121 | BLVRB isoform 1. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.952 |
| BLVRB | HMOX2 | ENSPPYP00000011187 | ENSPPYP00000007986 | BLVRB isoform 1. | HMOX2 isoform 7. | 0.971 |
| COX10 | FECH | ENSPPYP00000008995 | ENSPPYP00000010312 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | 0.943 |
| COX10 | HCCS | ENSPPYP00000008995 | ENSPPYP00000022504 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | 0.954 |
| COX10 | HMOX1 | ENSPPYP00000008995 | ENSPPYP00000013121 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.908 |
| COX10 | HMOX2 | ENSPPYP00000008995 | ENSPPYP00000007986 | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. | HMOX2 isoform 7. | 0.908 |
| CP | FECH | ENSPPYP00000015875 | ENSPPYP00000010312 | Ceruloplasmin; Belongs to the multicopper oxidase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | 0.929 |
| CP | HEPH | ENSPPYP00000015875 | ENSPPYP00000022859 | Ceruloplasmin; Belongs to the multicopper oxidase family. | HEPH isoform 1; Belongs to the multicopper oxidase family. | 0.903 |
| CP | HMOX1 | ENSPPYP00000015875 | ENSPPYP00000013121 | Ceruloplasmin; Belongs to the multicopper oxidase family. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.920 |
| CP | HMOX2 | ENSPPYP00000015875 | ENSPPYP00000007986 | Ceruloplasmin; Belongs to the multicopper oxidase family. | HMOX2 isoform 7. | 0.915 |
| FECH | COX10 | ENSPPYP00000010312 | ENSPPYP00000008995 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. | 0.943 |
| FECH | CP | ENSPPYP00000010312 | ENSPPYP00000015875 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | Ceruloplasmin; Belongs to the multicopper oxidase family. | 0.929 |
| FECH | HCCS | ENSPPYP00000010312 | ENSPPYP00000022504 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | Cytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. | 0.919 |
| FECH | HEPH | ENSPPYP00000010312 | ENSPPYP00000022859 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | HEPH isoform 1; Belongs to the multicopper oxidase family. | 0.931 |
| FECH | HMOX1 | ENSPPYP00000010312 | ENSPPYP00000013121 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. | Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. | 0.935 |
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