| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cp | Fech | ENSMUSP00000103964 | ENSMUSP00000157791 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | 0.923 |
| Cp | Fth1 | ENSMUSP00000103964 | ENSMUSP00000158539 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Ferritin heavy chain, N-terminally processed; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. | 0.914 |
| Cp | Ftl1 | ENSMUSP00000103964 | ENSMUSP00000092002 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Ferritin light chain 1; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney; Belongs to the ferritin family. | 0.892 |
| Cp | Ftmt | ENSMUSP00000103964 | ENSMUSP00000025388 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Ferritin, mitochondrial; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity); Belongs to the ferritin family. | 0.899 |
| Cp | Fxn | ENSMUSP00000103964 | ENSMUSP00000080081 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Frataxin intermediate form; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activity of ACO1 (By similarity); Belongs to the frataxin family. | 0.916 |
| Cp | Heph | ENSMUSP00000103964 | ENSMUSP00000033553 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Hephaestin; May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1. | 0.877 |
| Cp | Hephl1 | ENSMUSP00000103964 | ENSMUSP00000124518 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Ferroxidase HEPHL1; Is a copper-binding glycoprotein with ferroxidase activity. It oxidizes Fe(2+) to Fe(3+) without releasing radical oxygen species. May be involved in the regulation of intracellular iron content. | 0.877 |
| Cp | Hmox1 | ENSMUSP00000103964 | ENSMUSP00000005548 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | 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. | 0.932 |
| Cp | Hmox2 | ENSMUSP00000103964 | ENSMUSP00000004172 | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | Heme oxygenase 2; 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. | 0.884 |
| Fech | Cp | ENSMUSP00000157791 | ENSMUSP00000103964 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | 0.923 |
| Fech | Fth1 | ENSMUSP00000157791 | ENSMUSP00000158539 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Ferritin heavy chain, N-terminally processed; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. | 0.922 |
| Fech | Ftl1 | ENSMUSP00000157791 | ENSMUSP00000092002 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Ferritin light chain 1; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney; Belongs to the ferritin family. | 0.889 |
| Fech | Ftmt | ENSMUSP00000157791 | ENSMUSP00000025388 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Ferritin, mitochondrial; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity); Belongs to the ferritin family. | 0.925 |
| Fech | Fxn | ENSMUSP00000157791 | ENSMUSP00000080081 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Frataxin intermediate form; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activity of ACO1 (By similarity); Belongs to the frataxin family. | 0.992 |
| Fech | Heph | ENSMUSP00000157791 | ENSMUSP00000033553 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Hephaestin; May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1. | 0.916 |
| Fech | Hephl1 | ENSMUSP00000157791 | ENSMUSP00000124518 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Ferroxidase HEPHL1; Is a copper-binding glycoprotein with ferroxidase activity. It oxidizes Fe(2+) to Fe(3+) without releasing radical oxygen species. May be involved in the regulation of intracellular iron content. | 0.927 |
| Fech | Hmox1 | ENSMUSP00000157791 | ENSMUSP00000005548 | Ferrochelatase, mitochondrial; 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. | 0.955 |
| Fech | Hmox2 | ENSMUSP00000157791 | ENSMUSP00000004172 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Heme oxygenase 2; 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. | 0.947 |
| Fech | Ncoa4 | ENSMUSP00000157791 | ENSMUSP00000126071 | Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. | Nuclear receptor coactivator 4. | 0.597 |
| Fth1 | Cp | ENSMUSP00000158539 | ENSMUSP00000103964 | Ferritin heavy chain, N-terminally processed; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. | Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | 0.914 |
