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PRDX3 PRDX3 GPX4 GPX4 TXN TXN GLRX2 GLRX2 TXNRD2 TXNRD2 TXN2 TXN2 GSR GSR GLRX5 GLRX5 GLRX3 GLRX3 PRDX6 PRDX6 GPX1 GPX1
"GLRX2" - glutaredoxin 2 in Homo sapiens
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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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protein of unknown 3D structure
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Predicted Interactions
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GLRX2glutaredoxin 2; 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 glutathionylation and degluta [...] (165 aa)    
Predicted Functional Partners:
GLRX5
glutaredoxin 5; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 (157 aa)
    score_image   score_image   score_image   0.958
GLRX3
glutaredoxin 3; Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). May play a role in regulating the function of the thioredoxin system. Does not posses any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (335 aa)
        score_image   score_image   0.933
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. 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 A [...] (105 aa)
      score_image score_image   score_image   0.894
GSR
glutathione reductase; Maintains high levels of reduced glutathione in the cytosol (522 aa)
      score_image     score_image   0.787
TXN2
thioredoxin 2; Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity (166 aa)
      score_image score_image   score_image   0.783
PRDX6
peroxiredoxin 6; Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury (224 aa)
      score_image score_image   score_image   0.766
PRDX3
peroxiredoxin 3; Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical- generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (256 aa)
      score_image score_image   score_image   0.716
TXNRD2
thioredoxin reductase 2 (524 aa)
      score_image     score_image   0.712
GPX4
glutathione peroxidase 4; Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity) (197 aa)
      score_image score_image   score_image   0.673
GPX1
glutathione peroxidase 1; Protects the hemoglobin in erythrocytes from oxidative breakdown (203 aa)
      score_image score_image   score_image   0.663
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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