node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ASNA1 | STATH | ENSP00000349887 | ENSP00000246895 | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.606 |
CST4 | HTN1 | ENSP00000217423 | ENSP00000246896 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | histatin 1; 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 | 0.649 |
CST4 | HTN3 | ENSP00000217423 | ENSP00000432561 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | histatin 3; 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 | 0.472 |
CST4 | MUC5B | ENSP00000217423 | ENSP00000436812 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | mucin 5B, oligomeric mucus/gel-forming | 0.499 |
CST4 | MUC7 | ENSP00000217423 | ENSP00000302021 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | mucin 7, secreted; May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili | 0.418 |
CST4 | STATH | ENSP00000217423 | ENSP00000246895 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.659 |
CTRC | RPL14 | ENSP00000365116 | ENSP00000345156 | chymotrypsin C (caldecrin); Has chymotrypsin-type protease activity and hypocalcemic activity | ribosomal protein L14 | 0.758 |
CTRC | STATH | ENSP00000365116 | ENSP00000246895 | chymotrypsin C (caldecrin); Has chymotrypsin-type protease activity and hypocalcemic activity | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.608 |
HTN1 | CST4 | ENSP00000246896 | ENSP00000217423 | histatin 1; 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 | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | 0.649 |
HTN1 | MUC5B | ENSP00000246896 | ENSP00000436812 | histatin 1; 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 | mucin 5B, oligomeric mucus/gel-forming | 0.719 |
HTN1 | MUC7 | ENSP00000246896 | ENSP00000302021 | histatin 1; 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 | mucin 7, secreted; May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili | 0.739 |
HTN1 | STATH | ENSP00000246896 | ENSP00000246895 | histatin 1; 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 | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.866 |
HTN3 | CST4 | ENSP00000432561 | ENSP00000217423 | histatin 3; 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 S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | 0.472 |
HTN3 | MUC7 | ENSP00000432561 | ENSP00000302021 | histatin 3; 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 | mucin 7, secreted; May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili | 0.740 |
HTN3 | STATH | ENSP00000432561 | ENSP00000246895 | histatin 3; 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 | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.583 |
MUC5B | CST4 | ENSP00000436812 | ENSP00000217423 | mucin 5B, oligomeric mucus/gel-forming | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | 0.499 |
MUC5B | HTN1 | ENSP00000436812 | ENSP00000246896 | mucin 5B, oligomeric mucus/gel-forming | histatin 1; 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 | 0.719 |
MUC5B | MUC7 | ENSP00000436812 | ENSP00000302021 | mucin 5B, oligomeric mucus/gel-forming | mucin 7, secreted; May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili | 0.981 |
MUC5B | STATH | ENSP00000436812 | ENSP00000246895 | mucin 5B, oligomeric mucus/gel-forming | statherin; Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface | 0.739 |
MUC7 | CST4 | ENSP00000302021 | ENSP00000217423 | mucin 7, secreted; May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili | cystatin S; This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively | 0.418 |