| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| COL1A2 | FAP | ENSP00000297268 | ENSP00000188790 | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | 0.630 |
| COL1A2 | FN1 | ENSP00000297268 | ENSP00000346839 | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | Fibronectin type III domain containing; Endogenous ligands | 0.893 |
| COL1A2 | LOX | ENSP00000297268 | ENSP00000231004 | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | Protein-lysine 6-oxidase; Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity); Belongs to the lysyl oxidase family | 0.766 |
| COL1A2 | POSTN | ENSP00000297268 | ENSP00000369071 | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | Periostin; Induces cell attachment and spreading and plays a role in cell adhesion. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity); Gla domain containing | 0.872 |
| DPP7 | FAP | ENSP00000360635 | ENSP00000188790 | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides; DASH family | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | 0.745 |
| DPP7 | PREP | ENSP00000360635 | ENSP00000358106 | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides; DASH family | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family | 0.721 |
| FAP | COL1A2 | ENSP00000188790 | ENSP00000297268 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | 0.630 |
| FAP | DPP7 | ENSP00000188790 | ENSP00000360635 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides; DASH family | 0.745 |
| FAP | FN1 | ENSP00000188790 | ENSP00000346839 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Fibronectin type III domain containing; Endogenous ligands | 0.741 |
| FAP | GCG | ENSP00000188790 | ENSP00000387662 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Glucagon; Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life; Belongs to the glucagon family | 0.779 |
| FAP | GIP | ENSP00000188790 | ENSP00000350005 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Gastric inhibitory polypeptide; Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion; Endogenous ligands | 0.712 |
| FAP | LOX | ENSP00000188790 | ENSP00000231004 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Protein-lysine 6-oxidase; Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity); Belongs to the lysyl oxidase family | 0.632 |
| FAP | NAGLU | ENSP00000188790 | ENSP00000225927 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Alpha-N-acetylglucosaminidase; Involved in the degradation of heparan sulfate | 0.620 |
| FAP | POSTN | ENSP00000188790 | ENSP00000369071 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Periostin; Induces cell attachment and spreading and plays a role in cell adhesion. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity); Gla domain containing | 0.668 |
| FAP | PREP | ENSP00000188790 | ENSP00000358106 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family | 0.718 |
| FAP | PYY | ENSP00000188790 | ENSP00000353198 | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | Peptide YY; This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility; Endogenous ligands | 0.663 |
| FN1 | COL1A2 | ENSP00000346839 | ENSP00000297268 | Fibronectin type III domain containing; Endogenous ligands | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | 0.893 |
| FN1 | FAP | ENSP00000346839 | ENSP00000188790 | Fibronectin type III domain containing; Endogenous ligands | Prolyl endopeptidase FAP; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenasci [...] | 0.741 |
| FN1 | LOX | ENSP00000346839 | ENSP00000231004 | Fibronectin type III domain containing; Endogenous ligands | Protein-lysine 6-oxidase; Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity); Belongs to the lysyl oxidase family | 0.898 |
| FN1 | POSTN | ENSP00000346839 | ENSP00000369071 | Fibronectin type III domain containing; Endogenous ligands | Periostin; Induces cell attachment and spreading and plays a role in cell adhesion. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity); Gla domain containing | 0.863 |
