| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| COL11A1 | COL12A1 | ENSP00000359114 | ENSP00000325146 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | 0.939 |
| COL11A1 | COL21A1 | ENSP00000359114 | ENSP00000244728 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen type XXI alpha 1 chain; Collagens | 0.924 |
| COL11A1 | COL24A1 | ENSP00000359114 | ENSP00000359603 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-1(XXIV) chain; May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development; Belongs to the fibrillar collagen family | 0.923 |
| COL11A1 | COL4A3 | ENSP00000359114 | ENSP00000379823 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-3(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen; Collagens | 0.920 |
| COL11A1 | COL4A4 | ENSP00000359114 | ENSP00000379866 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-4(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen | 0.923 |
| COL11A1 | COL4A5 | ENSP00000359114 | ENSP00000331902 | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | Collagen alpha-5(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen; Collagens | 0.925 |
| COL11A1 | COL5A1 | ENSP00000359114 | ENSP00000360882 | Collagen alpha-1(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 | 0.912 |
| COL11A1 | COL5A2 | ENSP00000359114 | ENSP00000364000 | Collagen alpha-1(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) | 0.949 |
| COL11A1 | CRTAP | ENSP00000359114 | ENSP00000323696 | Collagen alpha-1(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 | 0.920 |
| COL11A1 | LEPRE1 | ENSP00000359114 | ENSP00000236040 | Collagen alpha-1(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 | 0.930 |
| COL12A1 | COL11A1 | ENSP00000325146 | ENSP00000359114 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens | 0.939 |
| COL12A1 | COL21A1 | ENSP00000325146 | ENSP00000244728 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen type XXI alpha 1 chain; Collagens | 0.927 |
| COL12A1 | COL24A1 | ENSP00000325146 | ENSP00000359603 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen alpha-1(XXIV) chain; May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development; Belongs to the fibrillar collagen family | 0.919 |
| COL12A1 | COL4A3 | ENSP00000325146 | ENSP00000379823 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen alpha-3(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen; Collagens | 0.914 |
| COL12A1 | COL4A4 | ENSP00000325146 | ENSP00000379866 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen alpha-4(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen | 0.917 |
| COL12A1 | COL4A5 | ENSP00000325146 | ENSP00000331902 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Collagen alpha-5(IV) chain; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen; Collagens | 0.928 |
| COL12A1 | COL5A1 | ENSP00000325146 | ENSP00000360882 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | 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 | 0.952 |
| COL12A1 | COL5A2 | ENSP00000325146 | ENSP00000364000 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | 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) | 0.968 |
| COL12A1 | CRTAP | ENSP00000325146 | ENSP00000323696 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family | 0.910 |
| COL12A1 | LEPRE1 | ENSP00000325146 | ENSP00000236040 | Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family | 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 | 0.924 |
