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GLRX | GLRX isoform 1. (106 aa) | ||||
ENSPPYP00000016598 | annotation not available (104 aa) | ||||
GRXCR1 | GRXCR1 isoform 1. (231 aa) | ||||
STAB1 | STAB1 isoform 1. (2509 aa) | ||||
PDIA5 | Protein disulfide isomerase family A member 5. (519 aa) | ||||
TXNRD3 | TXNRD3 isoform 1. (569 aa) | ||||
DNAJC10 | DnaJ 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) | ||||
CR201_G0024663 | TXN2 isoform 1. (129 aa) | ||||
TXNRD2 | Thioredoxin reductase 2. (522 aa) | ||||
NXNL1 | NXNL1 isoform 1. (109 aa) | ||||
TMEM221 | Transmembrane protein 221 isoform X1. (129 aa) | ||||
CR201_G0002531 | TXNDC2 isoform 4. (478 aa) | ||||
P4HB | Protein 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) | ||||
TXNDC17 | 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 (By similarity); Belongs to the thioredoxin family. (123 aa) | ||||
NXN | NXN isoform 1. (390 aa) | ||||
GFER | Sulfhydryl oxidase. (81 aa) | ||||
PDIA2 | Protein 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 (By similarity); Belongs to the protein disulfide isomerase family. (521 aa) | ||||
PDIA3 | Protein disulfide-isomerase A3. (466 aa) | ||||
GLRX5 | GLRX5 isoform 2. (157 aa) | ||||
ERO1A | ERO1A isoform 1. (467 aa) | ||||
ENOX1 | ENOX1 isoform 1. (687 aa) | ||||
CR201_G0001249 | TXNRD1 isoform 17. (277 aa) | ||||
STAB2 | STAB2 isoform 1. (2293 aa) | ||||
CCS | Copper chaperone for superoxide dismutase. (274 aa) | ||||
GLRX3 | GLRX3 isoform 1. (335 aa) | ||||
TXNDC12 | Thioredoxin domain containing 12. (172 aa) | ||||
QSOX1 | Sulfhydryl 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. Belongs to the quiescin-sulfhydryl oxidase (QSOX) family. (607 aa) | ||||
GLRX2 | Glutaredoxin-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 [...] (161 aa) | ||||
ERO1B | ERO1B isoform 1. (394 aa) | ||||
SELENOT | Selenoprotein T; Belongs to the SelWTH family. Selenoprotein T subfamily. (137 aa) | ||||
TXNL1 | Thioredoxin like 1. (292 aa) | ||||
CHCHD4 | Coiled-coil-helix-coiled-coil-helix domain containing 4. (142 aa) | ||||
ENOX2 | Ecto-NOX disulfide-thiol exchanger 2. (610 aa) | ||||
QSOX2 | Sulfhydryl oxidase. (576 aa) | ||||
TXNDC8 | TXNDC8 isoform 3. (115 aa) | ||||
TXN | Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). 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 [...] (220 aa) | ||||
NXNL2 | Nucleoredoxin like 2. (156 aa) | ||||
GSR | Glutathione reductase; Maintains high levels of reduced glutathione in the cytosol. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (472 aa) | ||||
TXNDC5 | Thioredoxin domain-containing protein 5. (431 aa) | ||||
ENSPPYP00000018104 | annotation not available (312 aa) | ||||
GRXCR2 | Glutaredoxin and cysteine rich domain containing 2. (248 aa) |