| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A1bg | A2m | ENSMUSP00000094151 | ENSMUSP00000032203 | Alpha-1B-glycoprotein. | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | 0.714 |
| A1bg | Afm | ENSMUSP00000094151 | ENSMUSP00000108804 | Alpha-1B-glycoprotein. | Afamin; Functions as carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. Binds vitamin E. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the transport of vitamin E across the blood-brain barrier. | 0.914 |
| A1bg | Ahsg | ENSMUSP00000094151 | ENSMUSP00000023583 | Alpha-1B-glycoprotein. | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family. | 0.660 |
| A1bg | Apoh | ENSMUSP00000094151 | ENSMUSP00000000049 | Alpha-1B-glycoprotein. | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | 0.648 |
| A1bg | Gc | ENSMUSP00000094151 | ENSMUSP00000046636 | Alpha-1B-glycoprotein. | Vitamin D-binding protein; Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. | 0.745 |
| A1bg | Hp | ENSMUSP00000094151 | ENSMUSP00000074436 | Alpha-1B-glycoprotein. | Haptoglobin alpha chain; As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pat [...] | 0.708 |
| A1bg | Hpx | ENSMUSP00000094151 | ENSMUSP00000033185 | Alpha-1B-glycoprotein. | Hemopexin; Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. | 0.962 |
| A1bg | Itih4 | ENSMUSP00000094151 | ENSMUSP00000112798 | Alpha-1B-glycoprotein. | Inter alpha-trypsin inhibitor, heavy chain 4; Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. | 0.657 |
| A1bg | Kng1 | ENSMUSP00000094151 | ENSMUSP00000023589 | Alpha-1B-glycoprotein. | Kininogen-1 heavy chain; (1) Kininogens are inhibitors of thiol proteases; (2) HMW- kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of [...] | 0.711 |
| A1bg | Trf | ENSMUSP00000094151 | ENSMUSP00000035158 | Alpha-1B-glycoprotein. | Serotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. | 0.664 |
| A2m | A1bg | ENSMUSP00000032203 | ENSMUSP00000094151 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Alpha-1B-glycoprotein. | 0.714 |
| A2m | Ahsg | ENSMUSP00000032203 | ENSMUSP00000023583 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Alpha-2-HS-glycoprotein; Probably involved in differentiation; Belongs to the fetuin family. | 0.703 |
| A2m | Apoh | ENSMUSP00000032203 | ENSMUSP00000000049 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Beta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. | 0.457 |
| A2m | Gc | ENSMUSP00000032203 | ENSMUSP00000046636 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Vitamin D-binding protein; Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. | 0.508 |
| A2m | Hp | ENSMUSP00000032203 | ENSMUSP00000074436 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Haptoglobin alpha chain; As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pat [...] | 0.749 |
| A2m | Hpx | ENSMUSP00000032203 | ENSMUSP00000033185 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Hemopexin; Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. | 0.609 |
| A2m | Itih4 | ENSMUSP00000032203 | ENSMUSP00000112798 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Inter alpha-trypsin inhibitor, heavy chain 4; Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. | 0.424 |
| A2m | Kng1 | ENSMUSP00000032203 | ENSMUSP00000023589 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Kininogen-1 heavy chain; (1) Kininogens are inhibitors of thiol proteases; (2) HMW- kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of [...] | 0.423 |
| A2m | Trf | ENSMUSP00000032203 | ENSMUSP00000035158 | Alpha-2-macroglobulin-P; Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the [...] | Serotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. | 0.530 |
| Afm | A1bg | ENSMUSP00000108804 | ENSMUSP00000094151 | Afamin; Functions as carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. Binds vitamin E. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the transport of vitamin E across the blood-brain barrier. | Alpha-1B-glycoprotein. | 0.914 |