| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BACE1 | FURIN | ENSP00000318585 | ENSP00000483552 | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | 0.859 |
| BACE1 | ITM2B | ENSP00000318585 | ENSP00000497221 | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | 0.714 |
| BACE1 | ITM2C | ENSP00000318585 | ENSP00000322730 | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | 0.613 |
| BACE1 | PCSK7 | ENSP00000318585 | ENSP00000325917 | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | Proprotein convertase subtilisin/kexin type 7; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. | 0.490 |
| FURIN | BACE1 | ENSP00000483552 | ENSP00000318585 | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | 0.859 |
| FURIN | ITM2B | ENSP00000483552 | ENSP00000497221 | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | 0.400 |
| FURIN | ITM2C | ENSP00000483552 | ENSP00000322730 | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | 0.597 |
| FURIN | PCSK7 | ENSP00000483552 | ENSP00000325917 | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | Proprotein convertase subtilisin/kexin type 7; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. | 0.913 |
| ITM2B | BACE1 | ENSP00000497221 | ENSP00000318585 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | 0.714 |
| ITM2B | FURIN | ENSP00000497221 | ENSP00000483552 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | 0.400 |
| ITM2B | ITM2C | ENSP00000497221 | ENSP00000322730 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | 0.555 |
| ITM2B | LMBR1L | ENSP00000497221 | ENSP00000267102 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Protein LMBR1L; Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta- catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis. Belongs to the LIMR family. | 0.459 |
| ITM2B | NRBP1 | ENSP00000497221 | ENSP00000369192 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Nuclear receptor-binding protein; May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. | 0.597 |
| ITM2B | PCSK7 | ENSP00000497221 | ENSP00000325917 | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | Proprotein convertase subtilisin/kexin type 7; Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway. | 0.432 |
| ITM2C | BACE1 | ENSP00000322730 | ENSP00000318585 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Beta-secretase 1; Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves CHL1 (By similarity). | 0.613 |
| ITM2C | FURIN | ENSP00000322730 | ENSP00000483552 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. | 0.597 |
| ITM2C | ITM2B | ENSP00000322730 | ENSP00000497221 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Integral membrane protein 2B; Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites. Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers; Belongs to the ITM2 family. | 0.555 |
| ITM2C | KNDC1 | ENSP00000322730 | ENSP00000304437 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Kinase non-catalytic C-lobe domain-containing protein 1; RAS-Guanine nucleotide exchange factor (GEF) that controls the negative regulation of neuronal dendrite growth by mediating a signaling pathway linking RAS and MAP2 (By similarity). May be involved in cellular senescence. | 0.544 |
| ITM2C | LMBR1L | ENSP00000322730 | ENSP00000267102 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Protein LMBR1L; Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta- catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis. Belongs to the LIMR family. | 0.485 |
| ITM2C | MVB12B | ENSP00000322730 | ENSP00000354772 | Integral membrane protein 2C; Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). | Multivesicular body subunit 12B; Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. | 0.616 |
