| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| C4BPA | PRB1 | ENSP00000356037 | ENSP00000420826 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Basic salivary proline-rich protein 1; Proline rich protein BstNI subfamily 1. | 0.764 |
| C4BPA | PRB2 | ENSP00000356037 | ENSP00000374013 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Basic salivary proline-rich protein 2; Proline rich protein BstNI subfamily 2. | 0.692 |
| C4BPA | PRB3 | ENSP00000356037 | ENSP00000442626 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Basic salivary proline-rich protein 3; Acts as a receptor for the Gram-negative bacterium F.nucleatum. | 0.706 |
| C4BPA | PRB4 | ENSP00000356037 | ENSP00000279575 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Basic salivary proline-rich protein 4; Proline rich protein BstNI subfamily 4. | 0.729 |
| C4BPA | PRH1 | ENSP00000356037 | ENSP00000479168 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Proline rich protein HaeIII subfamily 1. | 0.725 |
| C4BPA | PRH2 | ENSP00000356037 | ENSP00000379682 | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | Salivary acidic proline-rich phosphoprotein 1/2; PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth. | 0.758 |
| CST5 | HTN3 | ENSP00000307132 | ENSP00000432561 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | His3-(20-30)-peptide; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. | 0.562 |
| CST5 | PRB1 | ENSP00000307132 | ENSP00000420826 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Basic salivary proline-rich protein 1; Proline rich protein BstNI subfamily 1. | 0.608 |
| CST5 | PRB2 | ENSP00000307132 | ENSP00000374013 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Basic salivary proline-rich protein 2; Proline rich protein BstNI subfamily 2. | 0.624 |
| CST5 | PRB3 | ENSP00000307132 | ENSP00000442626 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Basic salivary proline-rich protein 3; Acts as a receptor for the Gram-negative bacterium F.nucleatum. | 0.645 |
| CST5 | PRB4 | ENSP00000307132 | ENSP00000279575 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Basic salivary proline-rich protein 4; Proline rich protein BstNI subfamily 4. | 0.688 |
| CST5 | PRH1 | ENSP00000307132 | ENSP00000479168 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Proline rich protein HaeIII subfamily 1. | 0.698 |
| CST5 | SMR3B | ENSP00000307132 | ENSP00000481313 | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | Submaxillary gland androgen regulated protein 3B; Belongs to the PROL1/PROL3 family. | 0.577 |
| HTN3 | CST5 | ENSP00000432561 | ENSP00000307132 | His3-(20-30)-peptide; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | 0.562 |
| HTN3 | PRB2 | ENSP00000432561 | ENSP00000374013 | His3-(20-30)-peptide; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. | Basic salivary proline-rich protein 2; Proline rich protein BstNI subfamily 2. | 0.628 |
| HTN3 | PRB3 | ENSP00000432561 | ENSP00000442626 | His3-(20-30)-peptide; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. | Basic salivary proline-rich protein 3; Acts as a receptor for the Gram-negative bacterium F.nucleatum. | 0.605 |
| HTN3 | SMR3B | ENSP00000432561 | ENSP00000481313 | His3-(20-30)-peptide; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. | Submaxillary gland androgen regulated protein 3B; Belongs to the PROL1/PROL3 family. | 0.615 |
| PRB1 | C4BPA | ENSP00000420826 | ENSP00000356037 | Basic salivary proline-rich protein 1; Proline rich protein BstNI subfamily 1. | C4b-binding protein alpha chain; Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component. | 0.764 |
| PRB1 | CST5 | ENSP00000420826 | ENSP00000307132 | Basic salivary proline-rich protein 1; Proline rich protein BstNI subfamily 1. | Cystatin-D; Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B. | 0.608 |
| PRB1 | PRB2 | ENSP00000420826 | ENSP00000374013 | Basic salivary proline-rich protein 1; Proline rich protein BstNI subfamily 1. | Basic salivary proline-rich protein 2; Proline rich protein BstNI subfamily 2. | 0.993 |
