node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A2M | KLK4 | ENSP00000323929 | ENSP00000326159 | 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 c [...] | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | 0.993 |
A2M | KNG1 | ENSP00000323929 | ENSP00000493985 | 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 c [...] | Low molecular weight growth-promoting factor; (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) [...] | 0.927 |
A2M | MMP20 | ENSP00000323929 | ENSP00000260228 | 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 c [...] | Matrix metalloproteinase-20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. | 0.575 |
A2M | SERPINA4 | ENSP00000323929 | ENSP00000451172 | 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 c [...] | Kallistatin; Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein. Belongs to the serpin family. | 0.408 |
A2M | SERPINC1 | ENSP00000323929 | ENSP00000356671 | 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 c [...] | Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. | 0.927 |
A2M | SERPING1 | ENSP00000323929 | ENSP00000278407 | 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 c [...] | 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. | 0.905 |
ACE | BDKRB2 | ENSP00000290866 | ENSP00000450482 | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily. | 0.917 |
ACE | KLK4 | ENSP00000290866 | ENSP00000326159 | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | 0.842 |
ACE | KNG1 | ENSP00000290866 | ENSP00000493985 | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | Low molecular weight growth-promoting factor; (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) [...] | 0.995 |
ACE | SERPINC1 | ENSP00000290866 | ENSP00000356671 | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. | 0.444 |
ACE | SERPING1 | ENSP00000290866 | ENSP00000278407 | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | 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. | 0.634 |
BDKRB2 | ACE | ENSP00000450482 | ENSP00000290866 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily. | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | 0.917 |
BDKRB2 | KLK4 | ENSP00000450482 | ENSP00000326159 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily. | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | 0.850 |
BDKRB2 | KNG1 | ENSP00000450482 | ENSP00000493985 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily. | Low molecular weight growth-promoting factor; (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) [...] | 0.999 |
BDKRB2 | SERPING1 | ENSP00000450482 | ENSP00000278407 | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 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. | 0.590 |
KLK4 | A2M | ENSP00000326159 | ENSP00000323929 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | 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 c [...] | 0.993 |
KLK4 | ACE | ENSP00000326159 | ENSP00000290866 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | Angiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. | 0.842 |
KLK4 | BDKRB2 | ENSP00000326159 | ENSP00000450482 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | B2 bradykinin receptor; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system; Belongs to the G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily. | 0.850 |
KLK4 | KNG1 | ENSP00000326159 | ENSP00000493985 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | Low molecular weight growth-promoting factor; (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) [...] | 0.997 |
KLK4 | MMP20 | ENSP00000326159 | ENSP00000260228 | Kallikrein-4; Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). | Matrix metalloproteinase-20; Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site. | 0.963 |