node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CLEC7A | CST7 | ENSP00000302569 | ENSP00000420384 | C-type lectin domain family 7 member A; Lectin that functions as pattern receptor specific for beta- 1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity). Necessary for the TLR2- mediated inflammatory response and for TLR2-mediated activation of NF- kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does [...] | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | 0.686 |
CLEC7A | P2RY12 | ENSP00000302569 | ENSP00000307259 | C-type lectin domain family 7 member A; Lectin that functions as pattern receptor specific for beta- 1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity). Necessary for the TLR2- mediated inflammatory response and for TLR2-mediated activation of NF- kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does [...] | P2Y purinoceptor 12; Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation. | 0.656 |
CLEC7A | TMEM119 | ENSP00000302569 | ENSP00000376553 | C-type lectin domain family 7 member A; Lectin that functions as pattern receptor specific for beta- 1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity). Necessary for the TLR2- mediated inflammatory response and for TLR2-mediated activation of NF- kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does [...] | Transmembrane protein 119; Plays an important role in bone formation and normal bone mineralization. Promotes the differentiation of myoblasts into osteoblasts. May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway. Upregulates the expression of ATF4, a transcription factor which plays a central role in osteoblast differentiation. Essential for normal spermatogenesis and late testicular differentiation (By similarity). | 0.668 |
CLEC7A | TYROBP | ENSP00000302569 | ENSP00000262629 | C-type lectin domain family 7 member A; Lectin that functions as pattern receptor specific for beta- 1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity). Necessary for the TLR2- mediated inflammatory response and for TLR2-mediated activation of NF- kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does [...] | TYRO protein tyrosine kinase-binding protein; Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors. TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation. Also has an inhibitory role in some cells. Non-covalently associates with activating receptors of the CD300 family to mediate cell activation ; [...] | 0.704 |
CST7 | CLEC7A | ENSP00000420384 | ENSP00000302569 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | C-type lectin domain family 7 member A; Lectin that functions as pattern receptor specific for beta- 1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity). Necessary for the TLR2- mediated inflammatory response and for TLR2-mediated activation of NF- kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does [...] | 0.686 |
CST7 | CTSC | ENSP00000420384 | ENSP00000227266 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | 0.725 |
CST7 | CTSL | ENSP00000420384 | ENSP00000345344 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). | 0.941 |
CST7 | CTSW | ENSP00000420384 | ENSP00000311300 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Belongs to the peptidase C1 family. | 0.697 |
CST7 | GZMA | ENSP00000420384 | ENSP00000274306 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Granzyme A; Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA. Belongs to the peptidase S1 family. Granzym [...] | 0.718 |
CST7 | GZMH | ENSP00000420384 | ENSP00000216338 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Granzyme H; Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication. | 0.721 |
CST7 | NKG7 | ENSP00000420384 | ENSP00000221978 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Protein NKG7; Natural killer cell granule protein 7; Belongs to the PMP-22/EMP/MP20 family. | 0.900 |
CST7 | P2RY12 | ENSP00000420384 | ENSP00000307259 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | P2Y purinoceptor 12; Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation. | 0.700 |
CST7 | TMEM119 | ENSP00000420384 | ENSP00000376553 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | Transmembrane protein 119; Plays an important role in bone formation and normal bone mineralization. Promotes the differentiation of myoblasts into osteoblasts. May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway. Upregulates the expression of ATF4, a transcription factor which plays a central role in osteoblast differentiation. Essential for normal spermatogenesis and late testicular differentiation (By similarity). | 0.718 |
CST7 | TYROBP | ENSP00000420384 | ENSP00000262629 | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | TYRO protein tyrosine kinase-binding protein; Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors. TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation. Also has an inhibitory role in some cells. Non-covalently associates with activating receptors of the CD300 family to mediate cell activation ; [...] | 0.759 |
CTSC | CST7 | ENSP00000227266 | ENSP00000420384 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | 0.725 |
CTSC | CTSL | ENSP00000227266 | ENSP00000345344 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). | 0.445 |
CTSC | GZMA | ENSP00000227266 | ENSP00000274306 | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | Granzyme A; Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA. Belongs to the peptidase S1 family. Granzym [...] | 0.854 |
CTSL | CST7 | ENSP00000345344 | ENSP00000420384 | Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). | Cystatin-F; Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system. | 0.941 |
CTSL | CTSC | ENSP00000345344 | ENSP00000227266 | Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). | Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. | 0.445 |
CTSL | CTSW | ENSP00000345344 | ENSP00000311300 | Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). | Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Belongs to the peptidase C1 family. | 0.576 |