| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGR2 | ANXA10 | ENSP00000391490 | ENSP00000352248 | Anterior gradient protein 2 homolog; Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion. | Annexin A10. | 0.674 |
| AGR2 | CTSE | ENSP00000391490 | ENSP00000350911 | Anterior gradient protein 2 homolog; Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion. | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | 0.615 |
| ANXA10 | AGR2 | ENSP00000352248 | ENSP00000391490 | Annexin A10. | Anterior gradient protein 2 homolog; Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion. | 0.674 |
| ANXA10 | CTSE | ENSP00000352248 | ENSP00000350911 | Annexin A10. | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | 0.573 |
| ANXA10 | VSIG1 | ENSP00000352248 | ENSP00000402219 | Annexin A10. | V-set and immunoglobulin domain containing 1. | 0.582 |
| CTSB | CTSC | ENSP00000345672 | ENSP00000227266 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | 0.498 |
| CTSB | CTSE | ENSP00000345672 | ENSP00000350911 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | 0.611 |
| CTSB | CTSS | ENSP00000345672 | ENSP00000357981 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. | 0.961 |
| CTSB | LAMP1 | ENSP00000345672 | ENSP00000333298 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Lysosome-associated membrane glycoprotein 1; Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis. | 0.891 |
| CTSB | LAMP2 | ENSP00000345672 | ENSP00000408411 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Lysosome-associated membrane glycoprotein 2; Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels o [...] | 0.792 |
| CTSB | MTMR9 | ENSP00000345672 | ENSP00000221086 | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | Myotubularin-related protein 9; Acts as an adapter for myotubularin-related phosphatases. Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5- bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols. Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3- phosphate. The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels. Stabilizes MTMR8 protein levels. Plays a role in the late stages of ma [...] | 0.492 |
| CTSC | CTSB | ENSP00000227266 | ENSP00000345672 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | 0.498 |
| CTSC | CTSE | ENSP00000227266 | ENSP00000350911 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | 0.582 |
| CTSC | CTSS | ENSP00000227266 | ENSP00000357981 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. | 0.543 |
| CTSC | LAMP1 | ENSP00000227266 | ENSP00000333298 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Lysosome-associated membrane glycoprotein 1; Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis. | 0.571 |
| CTSC | LAMP2 | ENSP00000227266 | ENSP00000408411 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Lysosome-associated membrane glycoprotein 2; Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels o [...] | 0.448 |
| CTSE | AGR2 | ENSP00000350911 | ENSP00000391490 | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | Anterior gradient protein 2 homolog; Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion. | 0.615 |
| CTSE | ANXA10 | ENSP00000350911 | ENSP00000352248 | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | Annexin A10. | 0.573 |
| CTSE | CTSB | ENSP00000350911 | ENSP00000345672 | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family. | 0.611 |
| CTSE | CTSC | ENSP00000350911 | ENSP00000227266 | Cathepsin E form II; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Belongs to the peptidase A1 family. | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | 0.582 |
