node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FBN1 | FN1 | ENSP00000325527 | ENSP00000346839 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Fibronectin type III domain containing; Endogenous ligands | 0.989 |
FBN1 | FSTL1 | ENSP00000325527 | ENSP00000295633 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Follistatin-related protein 1; May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity); SPARC family | 0.958 |
FBN1 | IGFBP3 | ENSP00000325527 | ENSP00000370473 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Insulin-like growth factor-binding protein 3; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R | 0.923 |
FBN1 | IGFBP5 | ENSP00000325527 | ENSP00000233813 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Insulin-like growth factor-binding protein 5; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors | 0.919 |
FBN1 | LTBP1 | ENSP00000325527 | ENSP00000386043 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Latent-transforming growth factor beta-binding protein 1; May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extracellular matrix (ECM); Latent transforming growth factor beta binding proteins | 0.954 |
FBN1 | TGFB1 | ENSP00000325527 | ENSP00000221930 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Transforming growth factor beta-1; Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysi [...] | 0.881 |
FBN1 | TGFB2 | ENSP00000325527 | ENSP00000355896 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Transforming growth factor beta-2; TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth; Endogenous ligands | 0.614 |
FBN1 | TGFB3 | ENSP00000325527 | ENSP00000238682 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Transforming growth factor beta-3; Involved in embryogenesis and cell differentiation; Belongs to the TGF-beta family | 0.502 |
FBN1 | TIMP1 | ENSP00000325527 | ENSP00000218388 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Metalloproteinase inhibitor 1; Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it [...] | 0.939 |
FBN1 | VCAN | ENSP00000325527 | ENSP00000265077 | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | Versican core protein; May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid; C-type lectin domain containing | 0.983 |
FN1 | FBN1 | ENSP00000346839 | ENSP00000325527 | Fibronectin type III domain containing; Endogenous ligands | Fibrillin-1; Fibrillin-1- Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus w [...] | 0.989 |
FN1 | FSTL1 | ENSP00000346839 | ENSP00000295633 | Fibronectin type III domain containing; Endogenous ligands | Follistatin-related protein 1; May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity); SPARC family | 0.944 |
FN1 | IGFBP3 | ENSP00000346839 | ENSP00000370473 | Fibronectin type III domain containing; Endogenous ligands | Insulin-like growth factor-binding protein 3; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R | 0.984 |
FN1 | IGFBP5 | ENSP00000346839 | ENSP00000233813 | Fibronectin type III domain containing; Endogenous ligands | Insulin-like growth factor-binding protein 5; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors | 0.982 |
FN1 | LTBP1 | ENSP00000346839 | ENSP00000386043 | Fibronectin type III domain containing; Endogenous ligands | Latent-transforming growth factor beta-binding protein 1; May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extracellular matrix (ECM); Latent transforming growth factor beta binding proteins | 0.974 |
FN1 | TGFB1 | ENSP00000346839 | ENSP00000221930 | Fibronectin type III domain containing; Endogenous ligands | Transforming growth factor beta-1; Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysi [...] | 0.985 |
FN1 | TGFB2 | ENSP00000346839 | ENSP00000355896 | Fibronectin type III domain containing; Endogenous ligands | Transforming growth factor beta-2; TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth; Endogenous ligands | 0.976 |
FN1 | TGFB3 | ENSP00000346839 | ENSP00000238682 | Fibronectin type III domain containing; Endogenous ligands | Transforming growth factor beta-3; Involved in embryogenesis and cell differentiation; Belongs to the TGF-beta family | 0.967 |
FN1 | TIMP1 | ENSP00000346839 | ENSP00000218388 | Fibronectin type III domain containing; Endogenous ligands | Metalloproteinase inhibitor 1; Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it [...] | 0.972 |
FN1 | VCAN | ENSP00000346839 | ENSP00000265077 | Fibronectin type III domain containing; Endogenous ligands | Versican core protein; May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid; C-type lectin domain containing | 0.970 |