STRINGSTRING
Nxn Nxn Tmx1 Tmx1 Txndc15 Txndc15 Pdia5 Pdia5 Prdx5 Prdx5 Tmx3 Tmx3 Prdx3 Prdx3 P4hb P4hb Prdx4 Prdx4 Dnajc10 Dnajc10 Pdia3 Pdia3 Erp44 Erp44 Txn1 Txn1 Txndc12 Txndc12 Pdilt Pdilt Pdia2 Pdia2 Qsox1 Qsox1 Qsox2 Qsox2 Txndc11 Txndc11 Txndc5 Txndc5 Tmx4 Tmx4 Dnajc16 Dnajc16 Pdia6 Pdia6 Txndc2 Txndc2 Glrx3 Glrx3 Nhlrc2 Nhlrc2 Prdx6 Prdx6 Pdia4 Pdia4 Nme8 Nme8 Sco1 Sco1 Txndc8 Txndc8 Prdx2 Prdx2 Txn2 Txn2 Tmx2 Tmx2 Prdx1 Prdx1 Txndc16 Txndc16 Txndc9 Txndc9 Prdx6b Prdx6b Nme9 Nme9 Sco2 Sco2 Txnl1 Txnl1
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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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). Belongs to the nucleoredoxin family. (435 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. (278 aa)
Txndc15Thioredoxin domain-containing protein 15; Acts as a positive regulator of ciliary hedgehog signaling. Required for cilia biogenesis. (344 aa)
Pdia5Protein disulfide-isomerase A5. (517 aa)
Prdx5Peroxiredoxin-5, 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 and as sensor of hydrogen peroxide-mediated signaling events. (210 aa)
Tmx3Protein disulfide-isomerase TMX3; Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase (By similarity). (456 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. (257 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 [...] (509 aa)
Prdx4Peroxiredoxin-4; 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 and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF- kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity). (274 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)
Pdia3Protein disulfide-isomerase A3. (505 aa)
Erp44Endoplasmic reticulum resident protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum (By similarity). (406 aa)
Txn1Thioredoxin; 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 [...] (105 aa)
Txndc12Thioredoxin domain-containing protein 12; Possesses significant protein thiol-disulfide oxidase activity. (170 aa)
PdiltProtein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis. (588 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 (By similarity). (527 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. (748 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 (By similarity). (639 aa)
Txndc11Thioredoxin domain-containing protein 11; May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation (By similarity). (948 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. (417 aa)
Tmx4Thioredoxin-related transmembrane protein 4. (335 aa)
Dnajc16DnaJ homolog subfamily C member 16. (772 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 (By similarity). May also regulate the UPR via the EIF2AK3 UPR sensor (By similarity). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). Belongs to the protein disulfide isomerase family. (445 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. (550 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 (By similarity). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator. Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (By similarity). (337 aa)
Nhlrc2NHL repeat-containing protein 2; Required for normal embryonic development. (725 aa)
Prdx6Peroxiredoxin-6; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role [...] (224 aa)
Pdia4Protein disulfide-isomerase A4. (641 aa)
Nme8Thioredoxin domain-containing protein 3; Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds (By similarity). (586 aa)
Sco1Protein SCO1 homolog, mitochondrial; Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT- CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (By similarity). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 ; Belongs to the SCO1/2 family. (284 aa)
Txndc8Thioredoxin domain-containing protein 8; May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm (By similarity). (153 aa)
Prdx2Peroxiredoxin-2; 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 and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). (198 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)
Tmx2Thioredoxin-related transmembrane protein 2. (295 aa)
Prdx1Peroxiredoxin-1; 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 and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron diffe [...] (199 aa)
Txndc16Thioredoxin domain-containing protein 16. (820 aa)
Txndc9Thioredoxin domain-containing protein 9; Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. (226 aa)
Prdx6bPeroxiredoxin 6, related sequence 1. (224 aa)
Nme9NME/NM23 family member 9; Belongs to the NDK family. (329 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. Belongs to the SCO1/2 family. (255 aa)
Txnl1Thioredoxin-like protein 1; Active thioredoxin with a redox potential of about -250 mV. (289 aa)
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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