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PCYOX1L PCYOX1L TMX2 TMX2 TXNRD1 TXNRD1 DLD DLD TXN2 TXN2 TXNL1 TXNL1 PDIA2 PDIA2 GSR GSR TMX4 TMX4 MSRB1 MSRB1 QSOX2 QSOX2 MSRB3 MSRB3 ERO1B ERO1B GSTO2 GSTO2 NXN NXN ENOX2 ENOX2 GLRX5 GLRX5 P4HB P4HB PDIA5 PDIA5 MSRA MSRA STAB1 STAB1 TXNDC2 TXNDC2 PDIA3 PDIA3 TMX3 TMX3 PRDX3 PRDX3 CHCHD4 CHCHD4 GLRX2 GLRX2 QSOX1 QSOX1 GLRX3 GLRX3 GSTO1 GSTO1 TXNDC12 TXNDC12 PGK1 PGK1 TXN TXN MSRB2 MSRB2 TXNDC5 TXNDC5 GLRX GLRX SRXN1 SRXN1 STAB2 STAB2 SUOX SUOX ERO1A ERO1A GRXCR1 GRXCR1 TXNRD2 TXNRD2 IFI30 IFI30 PDIA6 PDIA6 PCYOX1 PCYOX1 TMX1 TMX1 SELENBP1 SELENBP1 SELENOT SELENOT TXNRD3 TXNRD3 CCS CCS SCO2 SCO2 H3BNX3_HUMAN H3BNX3_HUMAN SQOR SQOR PDIA4 PDIA4 GFER GFER TXNDC17 TXNDC17 SESN2 SESN2 ENOX1 ENOX1 DNAJC10 DNAJC10 SUMF1 SUMF1
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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experimentally determined
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PCYOX1LPrenylcysteine oxidase-like; Probable oxidoreductase. (494 aa)
TMX2Thioredoxin related transmembrane protein 2. (296 aa)
TXNRD1Thioredoxin 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. (649 aa)
DLDDihydrolipoyl dehydrogenase, mitochondrial; Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched- chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2- oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KA [...] (509 aa)
TXN2Thioredoxin, mitochondrial; Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity; Belongs to the thioredoxin family. (166 aa)
TXNL1Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV. (289 aa)
PDIA2Protein disulfide-isomerase A2; 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. (525 aa)
GSRGlutathione reductase, mitochondrial; Maintains high levels of reduced glutathione in the cytosol. (522 aa)
TMX4Thioredoxin related transmembrane protein 4. (349 aa)
MSRB1Methionine-R-sulfoxide reductase B1; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to a [...] (116 aa)
QSOX2Sulfhydryl oxidase 2; Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosis. (698 aa)
MSRB3Methionine-R-sulfoxide reductase B3; Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. Isoform 2 is essential for hearing. (192 aa)
ERO1BERO1-like protein beta; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive o [...] (467 aa)
GSTO2Glutathione S-transferase omega-2; Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). Belongs to the GST superfamily. Omega family. (243 aa)
NXNNucleoredoxin; Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A) (By similarity). Belongs to the nucleoredoxin family. (435 aa)
ENOX2Protein disulfide-thiol oxidoreductase; May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock. (610 aa)
GLRX5Glutaredoxin-related protein 5, mitochondrial; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters. Involved in protein lipoylation, acting in the pathway that provides an iron-sulfur cluster to lipoate synthase. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron- sulfur protein ACO1. May protect cells against apoptosis due to reactive oxygen species and oxidative stress (By similarity). (157 aa)
P4HBProtein disulfide-isomerase; 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 other chape [...] (508 aa)
PDIA5Protein disulfide-isomerase A5; Protein disulfide isomerase family A member 5. (519 aa)
MSRAMitochondrial peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. (235 aa)
STAB1Stabilin-1; Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system. (2570 aa)
TXNDC2Thioredoxin domain-containing protein 2; Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase. (553 aa)
PDIA3Protein disulfide-isomerase A3; Protein disulfide isomerase family A member 3; Belongs to the protein disulfide isomerase family. (505 aa)
TMX3Protein disulfide-isomerase TMX3; Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. (454 aa)
PRDX3Thioredoxin-dependent peroxide reductase, mitochondrial; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. (256 aa)
CHCHD4Mitochondrial intermembrane space import and assembly protein 40; Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes. Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Required for the import of COA7 in the IMS. Precursor proteins to be imported into the IMS are translo [...] (155 aa)
GLRX2Glutaredoxin-2, mitochondrial; Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylat [...] (165 aa)
QSOX1Sulfhydryl oxidase 1; Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration. (747 aa)
GLRX3Glutaredoxin-3; Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. (335 aa)
GSTO1Glutathione S-transferase omega-1; Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. (241 aa)
TXNDC12Thioredoxin domain-containing protein 12; Possesses significant protein thiol-disulfide oxidase activity. (172 aa)
PGK1Phosphoglycerate kinase 1; Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility. (417 aa)
TXNThioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S- nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates [...] (105 aa)
MSRB2Methionine-R-sulfoxide reductase B2, mitochondrial; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maint [...] (182 aa)
TXNDC5Thioredoxin domain-containing protein 5; Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). (432 aa)
GLRXGlutaredoxin-1; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins; Belongs to the glutaredoxin family. (106 aa)
SRXN1Sulfiredoxin-1; Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Belongs to the sulfiredoxin family. (137 aa)
STAB2190 kDa form stabilin-2; Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluid [...] (2551 aa)
SUOXSulfite oxidase, mitochondrial; Sulfite oxidase. (545 aa)
ERO1AERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] (468 aa)
GRXCR1Glutaredoxin domain-containing cysteine-rich protein 1; May play a role in actin filament architecture in developing stereocilia of sensory cells; Belongs to the GRXCR1 family. (290 aa)
TXNRD2Thioredoxin reductase 2, mitochondrial; Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis. Maintains thioredoxin in a reduced state. May play a role in redox- regulated cell signaling. (524 aa)
IFI30Gamma-interferon-inducible lysosomal thiol reductase; 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). (250 aa)
PDIA6Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. (492 aa)
PCYOX1Prenylcysteine oxidase 1; Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine. (505 aa)
TMX1Thioredoxin-related transmembrane protein 1; May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. (280 aa)
SELENBP1Methanethiol oxidase; Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria. Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). (514 aa)
SELENOTThioredoxin reductase-like selenoprotein T; Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress ans cell death. Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, con [...] (195 aa)
TXNRD3Thioredoxin reductase 3; Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity). (643 aa)
CCSCopper chaperone for superoxide dismutase; Delivers copper to copper zinc superoxide dismutase (SOD1); In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family. (274 aa)
SCO2Protein SCO2 homolog, mitochondrial; Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2. (266 aa)
H3BNX3_HUMANPyr_redox_2 domain-containing protein. (289 aa)
SQORSulfide:quinone oxidoreductase, mitochondrial; Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). Belongs to the SQRD family. (450 aa)
PDIA4Protein disulfide-isomerase A4; Protein disulfide isomerase family A member 4; Belongs to the protein disulfide isomerase family. (645 aa)
GFERFAD-linked sulfhydryl oxidase ALR; [Isoform 1]: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. (205 aa)
TXNDC17Thioredoxin 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. (123 aa)
SESN2Sestrin-2; Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1. May positively regulate the transcripti [...] (480 aa)
ENOX1Protein disulfide-thiol oxidoreductase; Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 24 minutes and play a role in control of the ultradian cellular biological clock. (643 aa)
DNAJC10DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] (793 aa)
SUMF1Formylglycine-generating enzyme; Oxidase that catalyzes the conversion of cysteine to 3- oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent. 3- oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. Known substrates include GALNS, ARSA, STS and ARSE. Belongs to the sulfatase-modifying factor family. (374 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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