| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ATP6V1A | PDIA3 | ENSP00000273398 | ENSP00000300289 | ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells | protein disulfide isomerase family A, member 3 | 0.561 |
| ATP6V1A | PPIC | ENSP00000273398 | ENSP00000303057 | ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.642 |
| FKBP2 | P4HB | ENSP00000310935 | ENSP00000327801 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | 0.710 |
| FKBP2 | PDIA2 | ENSP00000310935 | ENSP00000219406 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | 0.752 |
| FKBP2 | PDIA3 | ENSP00000310935 | ENSP00000300289 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | protein disulfide isomerase family A, member 3 | 0.895 |
| FKBP2 | PDIA4 | ENSP00000310935 | ENSP00000286091 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | protein disulfide isomerase family A, member 4 | 0.819 |
| FKBP2 | PPIC | ENSP00000310935 | ENSP00000303057 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.710 |
| FKBP3 | PPIC | ENSP00000216330 | ENSP00000303057 | FK506 binding protein 3, 25kDa; FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.645 |
| LGALS3BP | PPIC | ENSP00000262776 | ENSP00000303057 | lectin, galactoside-binding, soluble, 3 binding protein; Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.657 |
| P4HB | FKBP2 | ENSP00000327801 | ENSP00000310935 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.710 |
| P4HB | PDIA2 | ENSP00000327801 | ENSP00000219406 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | 0.586 |
| P4HB | PDIA3 | ENSP00000327801 | ENSP00000300289 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | protein disulfide isomerase family A, member 3 | 0.822 |
| P4HB | PDIA4 | ENSP00000327801 | ENSP00000286091 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | protein disulfide isomerase family A, member 4 | 0.826 |
| P4HB | PPIC | ENSP00000327801 | ENSP00000303057 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.613 |
| PDIA2 | FKBP2 | ENSP00000219406 | ENSP00000310935 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.752 |
| PDIA2 | P4HB | ENSP00000219406 | ENSP00000327801 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | 0.586 |
| PDIA2 | PDIA3 | ENSP00000219406 | ENSP00000300289 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | protein disulfide isomerase family A, member 3 | 0.563 |
| PDIA2 | PDIA4 | ENSP00000219406 | ENSP00000286091 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | protein disulfide isomerase family A, member 4 | 0.560 |
| PDIA2 | PPIC | ENSP00000219406 | ENSP00000303057 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | peptidylprolyl isomerase C (cyclophilin C); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) | 0.605 |
| PDIA3 | ATP6V1A | ENSP00000300289 | ENSP00000273398 | protein disulfide isomerase family A, member 3 | ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells | 0.561 |
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