| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CDC37L1 | CLEC3B | ENSP00000371278 | ENSP00000296130 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | 0.900 |
| CDC37L1 | CTSW | ENSP00000371278 | ENSP00000311300 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins | 0.900 |
| CDC37L1 | ECM1 | ENSP00000371278 | ENSP00000358045 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Extracellular matrix protein 1; Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity | 0.900 |
| CDC37L1 | FAM3C | ENSP00000371278 | ENSP00000353025 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Protein FAM3C; May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition | 0.901 |
| CDC37L1 | ITIH3 | ENSP00000371278 | ENSP00000415769 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Inter-alpha-trypsin inhibitor heavy chain H3; May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes | 0.900 |
| CDC37L1 | LGALS3BP | ENSP00000371278 | ENSP00000262776 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Galectin-3-binding protein; Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells; BTB domain containing | 0.900 |
| CDC37L1 | RARRES2 | ENSP00000371278 | ENSP00000418009 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Retinoic acid receptor responder protein 2; Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an i [...] | 0.900 |
| CDC37L1 | SEPP1 | ENSP00000371278 | ENSP00000420939 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Selenoprotein P; Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis | 0.900 |
| CDC37L1 | SERPINA4 | ENSP00000371278 | ENSP00000450838 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Kallistatin; Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein; Belongs to the serpin family | 0.900 |
| CDC37L1 | TIMP3 | ENSP00000371278 | ENSP00000266085 | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | Metalloproteinase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 | 0.900 |
| CLEC3B | CDC37L1 | ENSP00000296130 | ENSP00000371278 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Hsp90 co-chaperone Cdc37-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 | 0.900 |
| CLEC3B | CTSW | ENSP00000296130 | ENSP00000311300 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins | 0.900 |
| CLEC3B | ECM1 | ENSP00000296130 | ENSP00000358045 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Extracellular matrix protein 1; Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity | 0.933 |
| CLEC3B | FAM3C | ENSP00000296130 | ENSP00000353025 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Protein FAM3C; May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition | 0.907 |
| CLEC3B | ITIH3 | ENSP00000296130 | ENSP00000415769 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Inter-alpha-trypsin inhibitor heavy chain H3; May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes | 0.904 |
| CLEC3B | LGALS3BP | ENSP00000296130 | ENSP00000262776 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Galectin-3-binding protein; Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells; BTB domain containing | 0.902 |
| CLEC3B | RARRES2 | ENSP00000296130 | ENSP00000418009 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Retinoic acid receptor responder protein 2; Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Its other ligands include G protein-coupled receptor 1 (GPR1) and chemokine receptor-like 2 (CCRL2). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an i [...] | 0.904 |
| CLEC3B | SEPP1 | ENSP00000296130 | ENSP00000420939 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Selenoprotein P; Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis | 0.933 |
| CLEC3B | SERPINA4 | ENSP00000296130 | ENSP00000450838 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Kallistatin; Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein; Belongs to the serpin family | 0.900 |
| CLEC3B | TIMP3 | ENSP00000296130 | ENSP00000266085 | Tetranectin; Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis; C-type lectin domain containing | Metalloproteinase inhibitor 3; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15 | 0.913 |
