node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A2m | C1qbp | ENSRNOP00000019346 | ENSRNOP00000031020 | Alpha-2-macroglobulin; 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 co [...] | Complement component 1 Q subcomponent-binding protein, mitochondrial; Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a [...] | 0.554 |
A2m | F12 | ENSRNOP00000019346 | ENSRNOP00000061983 | Alpha-2-macroglobulin; 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 co [...] | Coagulation factor XIIa heavy chain; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). | 0.437 |
A2m | Klkb1 | ENSRNOP00000019346 | ENSRNOP00000019237 | Alpha-2-macroglobulin; 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 co [...] | Plasma kallikrein heavy chain; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. | 0.923 |
A2m | Kng1 | ENSRNOP00000019346 | ENSRNOP00000069578 | Alpha-2-macroglobulin; 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 co [...] | 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 [...] | 0.806 |
A2m | Plg | ENSRNOP00000019346 | ENSRNOP00000023370 | Alpha-2-macroglobulin; 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 co [...] | Plasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] | 0.677 |
A2m | Serping1 | ENSRNOP00000019346 | ENSRNOP00000009817 | Alpha-2-macroglobulin; 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 co [...] | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity). | 0.700 |
Bdkrb1 | Bdkrb2 | ENSRNOP00000005953 | ENSRNOP00000064990 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | 0.946 |
Bdkrb1 | F11 | ENSRNOP00000005953 | ENSRNOP00000073061 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | Coagulation factor XI; Belongs to the peptidase S1 family. | 0.402 |
Bdkrb1 | F12 | ENSRNOP00000005953 | ENSRNOP00000061983 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | Coagulation factor XIIa heavy chain; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). | 0.576 |
Bdkrb1 | Klkb1 | ENSRNOP00000005953 | ENSRNOP00000019237 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | Plasma kallikrein heavy chain; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. | 0.719 |
Bdkrb1 | Kng1 | ENSRNOP00000005953 | ENSRNOP00000069578 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | 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 [...] | 0.999 |
Bdkrb1 | Prcp | ENSRNOP00000005953 | ENSRNOP00000014271 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | Prolylcarboxypeptidase. | 0.439 |
Bdkrb1 | Serping1 | ENSRNOP00000005953 | ENSRNOP00000009817 | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity). | 0.541 |
Bdkrb2 | Bdkrb1 | ENSRNOP00000064990 | ENSRNOP00000005953 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily. | 0.946 |
Bdkrb2 | F11 | ENSRNOP00000064990 | ENSRNOP00000073061 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | Coagulation factor XI; Belongs to the peptidase S1 family. | 0.501 |
Bdkrb2 | F12 | ENSRNOP00000064990 | ENSRNOP00000061983 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | Coagulation factor XIIa heavy chain; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). | 0.603 |
Bdkrb2 | Klkb1 | ENSRNOP00000064990 | ENSRNOP00000019237 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | Plasma kallikrein heavy chain; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin. | 0.711 |
Bdkrb2 | Kng1 | ENSRNOP00000064990 | ENSRNOP00000069578 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | 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 [...] | 0.999 |
Bdkrb2 | Prcp | ENSRNOP00000064990 | ENSRNOP00000014271 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | Prolylcarboxypeptidase. | 0.473 |
Bdkrb2 | Serping1 | ENSRNOP00000064990 | ENSRNOP00000009817 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. | Plasma protease C1 inhibitor; Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (By similarity). | 0.571 |