node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
COL11A2 | COL15A1 | ENSP00000363840 | ENSP00000364140 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | 0.912 |
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 | COL27A1 | ENSP00000363840 | ENSP00000348385 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(XXVII) chain; Plays a role during the calcification of cartilage and the transition of cartilage to bone; Belongs to the fibrillar collagen family | 0.921 |
COL11A2 | COL28A1 | ENSP00000363840 | ENSP00000382356 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(XXVIII) chain; May act as a cell-binding protein; Belongs to the VWA-containing collagen family | 0.915 |
COL11A2 | COL9A2 | ENSP00000363840 | ENSP00000361834 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-2(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans | 0.935 |
COL11A2 | COL9A3 | ENSP00000363840 | ENSP00000341640 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-3(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans | 0.932 |
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 | LEPREL1 | ENSP00000363840 | ENSP00000316881 | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase that catalyzes the post- translational formation of 3-hydroxyproline on collagens. Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4- hydroxyproline in the third position; Belongs to the leprecan family | 0.916 |
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 |
COL15A1 | COL11A2 | ENSP00000364140 | ENSP00000363840 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | 0.912 |
COL15A1 | COL1A1 | ENSP00000364140 | ENSP00000225964 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens | 0.939 |
COL15A1 | COL27A1 | ENSP00000364140 | ENSP00000348385 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-1(XXVII) chain; Plays a role during the calcification of cartilage and the transition of cartilage to bone; Belongs to the fibrillar collagen family | 0.917 |
COL15A1 | COL28A1 | ENSP00000364140 | ENSP00000382356 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-1(XXVIII) chain; May act as a cell-binding protein; Belongs to the VWA-containing collagen family | 0.911 |
COL15A1 | COL9A2 | ENSP00000364140 | ENSP00000361834 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-2(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans | 0.911 |
COL15A1 | COL9A3 | ENSP00000364140 | ENSP00000341640 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Collagen alpha-3(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans | 0.906 |
COL15A1 | CRTAP | ENSP00000364140 | ENSP00000323696 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family | 0.905 |
COL15A1 | LEPREL1 | ENSP00000364140 | ENSP00000316881 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase that catalyzes the post- translational formation of 3-hydroxyproline on collagens. Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4- hydroxyproline in the third position; Belongs to the leprecan family | 0.914 |
COL15A1 | P4HB | ENSP00000364140 | ENSP00000327801 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | 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 |
COL15A1 | PPIB | ENSP00000364140 | ENSP00000300026 | Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans | 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 | 0.901 |