| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| B2M | CTSS | ENSP00000452780 | ENSP00000357981 | beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity) | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | 0.932 |
| B2M | IFI30 | ENSP00000452780 | ENSP00000384886 | beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity) | interferon, gamma-inducible protein 30; Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II- restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity) | 0.925 |
| CD74 | CTSD | ENSP00000009530 | ENSP00000236671 | CD74 molecule, major histocompatibility complex, class II invariant chain | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | 0.912 |
| CD74 | CTSS | ENSP00000009530 | ENSP00000357981 | CD74 molecule, major histocompatibility complex, class II invariant chain | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | 0.988 |
| CD74 | LGMN | ENSP00000009530 | ENSP00000334052 | CD74 molecule, major histocompatibility complex, class II invariant chain | legumain; Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system | 0.915 |
| CTSD | CD74 | ENSP00000236671 | ENSP00000009530 | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | CD74 molecule, major histocompatibility complex, class II invariant chain | 0.912 |
| CTSD | CTSS | ENSP00000236671 | ENSP00000357981 | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | 0.988 |
| CTSD | IFI30 | ENSP00000236671 | ENSP00000384886 | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | interferon, gamma-inducible protein 30; Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II- restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity) | 0.926 |
| CTSD | LGMN | ENSP00000236671 | ENSP00000334052 | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | legumain; Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system | 0.503 |
| CTSS | B2M | ENSP00000357981 | ENSP00000452780 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity) | 0.932 |
| CTSS | CD74 | ENSP00000357981 | ENSP00000009530 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | CD74 molecule, major histocompatibility complex, class II invariant chain | 0.988 |
| CTSS | CTSD | ENSP00000357981 | ENSP00000236671 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | cathepsin D; Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease | 0.988 |
| CTSS | IFI30 | ENSP00000357981 | ENSP00000384886 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | interferon, gamma-inducible protein 30; Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II- restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity) | 0.942 |
| CTSS | LGMN | ENSP00000357981 | ENSP00000334052 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | legumain; Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system | 0.964 |
| CTSS | SERPINB4 | ENSP00000357981 | ENSP00000343445 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | serpin peptidase inhibitor, clade B (ovalbumin), member 4; May act as a protease inhibitor to modulate the host immune response against tumor cells | 0.954 |
| CTSS | TLR3 | ENSP00000357981 | ENSP00000296795 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | toll-like receptor 3; Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response | 0.927 |
| CTSS | TLR7 | ENSP00000357981 | ENSP00000370034 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | toll-like receptor 7; Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR7 is a nucleotide-sensing TLR which is activated by single-stranded RNA. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity) | 0.927 |
| CTSS | TLR9 | ENSP00000357981 | ENSP00000353874 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | toll-like receptor 9 | 0.933 |
| CTSS | UNC93B1 | ENSP00000357981 | ENSP00000227471 | cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N | unc-93 homolog B1 (C. elegans); Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B- cells removal | 0.937 |
| IFI30 | B2M | ENSP00000384886 | ENSP00000452780 | interferon, gamma-inducible protein 30; Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II- restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity) | beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity) | 0.925 |
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