node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SCAF4 | TXNDC17 | ENSP00000286835 | ENSP00000250101 | Splicing factor, arginine/serine-rich 15; May act to physically and functionally link transcription and pre-mRNA processing; Belongs to the splicing factor SR family | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | 0.745 |
TRPC7 | TXNDC17 | ENSP00000426070 | ENSP00000250101 | Short transient receptor potential channel 7; Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion; Transient receptor potential cation channels | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | 0.786 |
TXNDC17 | SCAF4 | ENSP00000250101 | ENSP00000286835 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Splicing factor, arginine/serine-rich 15; May act to physically and functionally link transcription and pre-mRNA processing; Belongs to the splicing factor SR family | 0.745 |
TXNDC17 | TRPC7 | ENSP00000250101 | ENSP00000426070 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Short transient receptor potential channel 7; Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) (By similarity). May also be activated by intracellular calcium store depletion; Transient receptor potential cation channels | 0.786 |
TXNDC17 | TXNL1 | ENSP00000250101 | ENSP00000217515 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | 0.929 |
TXNDC17 | TXNRD1 | ENSP00000250101 | ENSP00000434516 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing | 0.739 |
TXNDC17 | TYMS | ENSP00000250101 | ENSP00000315644 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Thymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway | 0.800 |
TXNDC17 | UBE2H | ENSP00000250101 | ENSP00000347836 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Ubiquitin-conjugating enzyme E2 H; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A; Ubiquitin conjugating enzymes E2 | 0.819 |
TXNDC17 | UBE2K | ENSP00000250101 | ENSP00000261427 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Ubiquitin-conjugating enzyme E2 K; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of ’Lys-48’-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam [...] | 0.814 |
TXNDC17 | USP5 | ENSP00000250101 | ENSP00000229268 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | Ubiquitin carboxyl-terminal hydrolase 5; Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored ’Lys-48’-linked polyubiquitin disassembly. Binds linear and ’Lys- 63’-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition; Ubiquitin specific peptidases | 0.807 |
TXNDC17 | WDR1 | ENSP00000250101 | ENSP00000427687 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | WD repeat-containing protein 1; Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Enhances cofilin-mediated actin severing (By similarity). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions. Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance (By similarity). Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape chan [...] | 0.816 |
TXNDC17 | WDR45B | ENSP00000250101 | ENSP00000376139 | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | WD repeat domain containing | 0.816 |
TXNL1 | TXNDC17 | ENSP00000217515 | ENSP00000250101 | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | 0.929 |
TXNL1 | TXNRD1 | ENSP00000217515 | ENSP00000434516 | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing | 0.700 |
TXNL1 | UBE2H | ENSP00000217515 | ENSP00000347836 | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | Ubiquitin-conjugating enzyme E2 H; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A; Ubiquitin conjugating enzymes E2 | 0.826 |
TXNL1 | USP5 | ENSP00000217515 | ENSP00000229268 | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | Ubiquitin carboxyl-terminal hydrolase 5; Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored ’Lys-48’-linked polyubiquitin disassembly. Binds linear and ’Lys- 63’-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition; Ubiquitin specific peptidases | 0.773 |
TXNRD1 | TXNDC17 | ENSP00000434516 | ENSP00000250101 | Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | 0.739 |
TXNRD1 | TXNL1 | ENSP00000434516 | ENSP00000217515 | Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing | Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV | 0.700 |
TXNRD1 | TYMS | ENSP00000434516 | ENSP00000315644 | Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing | Thymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway | 0.551 |
TYMS | TXNDC17 | ENSP00000315644 | ENSP00000250101 | Thymidylate synthase; Contributes to the de novo mitochondrial thymidylate biosynthesis pathway | Thioredoxin domain-containing protein 17; Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide; Belongs to the thioredoxin family | 0.800 |