node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACVR1 | FKBP1C | ENSP00000263640 | ENSP00000359693 | Activin receptor type-1; On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity) | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | 0.796 |
ACVR1 | TGFBR1 | ENSP00000263640 | ENSP00000364133 | Activin receptor type-1; On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity) | TGF-beta receptor type-1; Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogen [...] | 0.513 |
ENSG00000243667 | FKBP1C | ENSP00000477980 | ENSP00000359693 | WD repeat-containing protein 92; Seems to act as a modulator of apoptosis; WD repeat domain containing | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | 0.753 |
ENSG00000243667 | PPIA | ENSP00000477980 | ENSP00000419425 | WD repeat-containing protein 92; Seems to act as a modulator of apoptosis; WD repeat domain containing | Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily | 0.452 |
ENSG00000243667 | PPIF | ENSP00000477980 | ENSP00000225174 | WD repeat-containing protein 92; Seems to act as a modulator of apoptosis; WD repeat domain containing | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 0.401 |
FKBP1C | ACVR1 | ENSP00000359693 | ENSP00000263640 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Activin receptor type-1; On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity) | 0.796 |
FKBP1C | ENSG00000243667 | ENSP00000359693 | ENSP00000477980 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | WD repeat-containing protein 92; Seems to act as a modulator of apoptosis; WD repeat domain containing | 0.753 |
FKBP1C | MTOR | ENSP00000359693 | ENSP00000354558 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Serine/threonine-protein kinase mTOR; Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF [...] | 0.899 |
FKBP1C | PIN1 | ENSP00000359693 | ENSP00000247970 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] | 0.763 |
FKBP1C | PPIA | ENSP00000359693 | ENSP00000419425 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily | 0.771 |
FKBP1C | PPIB | ENSP00000359693 | ENSP00000300026 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases | 0.797 |
FKBP1C | PPIF | ENSP00000359693 | ENSP00000225174 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 0.772 |
FKBP1C | PPP3R1 | ENSP00000359693 | ENSP00000234310 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Calcineurin subunit B type 1; Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity; EF-hand domain containing | 0.818 |
FKBP1C | RYR1 | ENSP00000359693 | ENSP00000352608 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | Ryanodine receptor 1; Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for nor [...] | 0.774 |
FKBP1C | TGFBR1 | ENSP00000359693 | ENSP00000364133 | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | TGF-beta receptor type-1; Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogen [...] | 0.817 |
MTOR | FKBP1C | ENSP00000354558 | ENSP00000359693 | Serine/threonine-protein kinase mTOR; Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF [...] | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | 0.899 |
PIN1 | FKBP1C | ENSP00000247970 | ENSP00000359693 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] | Peptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases | 0.763 |
PIN1 | PPIA | ENSP00000247970 | ENSP00000419425 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] | Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily | 0.756 |
PIN1 | PPIB | ENSP00000247970 | ENSP00000300026 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases | 0.467 |
PIN1 | PPIF | ENSP00000247970 | ENSP00000225174 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] | 0.658 |