• Version:
  • 11.0 [archived version]
STRINGSTRING
GSS GSS GSTM3 GSTM3 GSTA4 GSTA4 SOD2 SOD2 CAT CAT GPX8 GPX8 ALOX5 ALOX5 SOD3 SOD3 SOD1 SOD1 P4HB P4HB ERO1L ERO1L
"GPX8" - Glutathione peroxidase 8 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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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[Homology]
Score
GPX8Glutathione peroxidase 8; Belongs to the glutathione peroxidase family (209 aa)    
Predicted Functional Partners:
SOD1
Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (154 aa)
   
 
  0.973
SOD2
Superoxide dismutase [Mn], mitochondrial; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (222 aa)
     
 
  0.971
SOD3
Extracellular superoxide dismutase [Cu-Zn]; Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen (240 aa)
   
 
  0.957
ERO1L
ERO1-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)
     
  0.952
GSS
Glutathione synthetase; Belongs to the eukaryotic GSH synthase family (474 aa)
     
 
  0.945
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)
     
  0.941
ALOX5
Arachidonate 5-lipoxygenase; Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes; Belongs to the lipoxygenase family (674 aa)
         
  0.909
GSTM3
Glutathione S-transferase Mu 3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers; Belongs to the GST superfamily. Mu family (225 aa)
     
 
  0.876
CAT
Catalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells; Belongs to the catalase family (527 aa)
     
 
  0.870
GSTA4
Glutathione S-transferase A4; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE); Soluble glutathione S-transferases (222 aa)
     
 
  0.866
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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