node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAPN7 | CAPNS1 | ENSP00000253693 | ENSP00000246533 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Calpain small subunit 1; Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; EF-hand domain containing | 0.967 |
CAPN7 | CAPNS2 | ENSP00000253693 | ENSP00000400882 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Calpain small subunit 2; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity; EF-hand domain containing | 0.944 |
CAPN7 | CASP3 | ENSP00000253693 | ENSP00000311032 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Caspase-3; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | 0.670 |
CAPN7 | CAST | ENSP00000253693 | ENSP00000379157 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 0.939 |
CAPN7 | CHMP4B | ENSP00000253693 | ENSP00000217402 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Charged multivesicular body protein 4b; Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential functio [...] | 0.763 |
CAPN7 | CTSB | ENSP00000253693 | ENSP00000345672 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins | 0.665 |
CAPN7 | IST1 | ENSP00000253693 | ENSP00000438399 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | IST1 homolog; ESCRT-III-like protein involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex- IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Regulates early endosomal tubulation together wi [...] | 0.767 |
CAPN7 | OXNAD1 | ENSP00000253693 | ENSP00000285083 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Oxidoreductase NAD-binding domain-containing protein 1; Oxidoreductase NAD binding domain containing 1 | 0.800 |
CAPN7 | TSG101 | ENSP00000253693 | ENSP00000251968 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Tumor susceptibility gene 101 protein; Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding [...] | 0.770 |
CAPN7 | XIRP1 | ENSP00000253693 | ENSP00000343140 | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | Xin actin-binding repeat-containing protein 1; Protects actin filaments from depolymerization; Belongs to the Xin family | 0.750 |
CAPNS1 | CAPN7 | ENSP00000246533 | ENSP00000253693 | Calpain small subunit 1; Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; EF-hand domain containing | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | 0.967 |
CAPNS1 | CAPNS2 | ENSP00000246533 | ENSP00000400882 | Calpain small subunit 1; Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; EF-hand domain containing | Calpain small subunit 2; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity; EF-hand domain containing | 0.920 |
CAPNS1 | CAST | ENSP00000246533 | ENSP00000379157 | Calpain small subunit 1; Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; EF-hand domain containing | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 0.982 |
CAPNS2 | CAPN7 | ENSP00000400882 | ENSP00000253693 | Calpain small subunit 2; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity; EF-hand domain containing | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | 0.944 |
CAPNS2 | CAPNS1 | ENSP00000400882 | ENSP00000246533 | Calpain small subunit 2; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity; EF-hand domain containing | Calpain small subunit 1; Regulatory subunit of the calcium-regulated non- lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; EF-hand domain containing | 0.920 |
CAPNS2 | CAST | ENSP00000400882 | ENSP00000379157 | Calpain small subunit 2; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity; EF-hand domain containing | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 0.980 |
CASP3 | CAPN7 | ENSP00000311032 | ENSP00000253693 | Caspase-3; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | 0.670 |
CASP3 | CAST | ENSP00000311032 | ENSP00000379157 | Caspase-3; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 0.775 |
CASP3 | CTSB | ENSP00000311032 | ENSP00000345672 | Caspase-3; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | Cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins | 0.631 |
CAST | CAPN7 | ENSP00000379157 | ENSP00000253693 | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | Calpain-7; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family | 0.939 |