node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
COL11A2 | COL1A1 | ENSP00000363840 | ENSP00000225964 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | 0.916 |
COL11A2 | COL1A2 | ENSP00000363840 | ENSP00000297268 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | 0.928 |
COL11A2 | COL3A1 | ENSP00000363840 | ENSP00000304408 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(III) chain; Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 | 0.914 |
COL11A2 | COL5A1 | ENSP00000363840 | ENSP00000360882 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin; Collagens | 0.904 |
COL11A2 | COL5A2 | ENSP00000363840 | ENSP00000364000 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue- specific matrices (By similarity) | 0.919 |
COL11A2 | CRTAP | ENSP00000363840 | ENSP00000323696 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family | 0.919 |
COL11A2 | LEPRE1 | ENSP00000363840 | ENSP00000236040 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Prolyl 3-hydroxylase 1; Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts | 0.942 |
COL11A2 | P4HB | ENSP00000363840 | ENSP00000327801 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.902 |
COL11A2 | PPIB | ENSP00000363840 | ENSP00000300026 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases | 0.900 |
COL11A2 | SERPINH1 | ENSP00000363840 | ENSP00000434412 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen; Serpin peptidase inhibitors | 0.904 |
COL1A1 | COL11A2 | ENSP00000225964 | ENSP00000363840 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | 0.916 |
COL1A1 | COL1A2 | ENSP00000225964 | ENSP00000297268 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family | 0.999 |
COL1A1 | COL3A1 | ENSP00000225964 | ENSP00000304408 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Collagen alpha-1(III) chain; Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 | 0.994 |
COL1A1 | COL5A1 | ENSP00000225964 | ENSP00000360882 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Collagen alpha-1(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin; Collagens | 0.986 |
COL1A1 | COL5A2 | ENSP00000225964 | ENSP00000364000 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue- specific matrices (By similarity) | 0.994 |
COL1A1 | CRTAP | ENSP00000225964 | ENSP00000323696 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family | 0.975 |
COL1A1 | LEPRE1 | ENSP00000225964 | ENSP00000236040 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Prolyl 3-hydroxylase 1; Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts | 0.968 |
COL1A1 | P4HB | ENSP00000225964 | ENSP00000327801 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] | 0.952 |
COL1A1 | PPIB | ENSP00000225964 | ENSP00000300026 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases | 0.952 |
COL1A1 | SERPINH1 | ENSP00000225964 | ENSP00000434412 | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen; Serpin peptidase inhibitors | 0.973 |