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UROD UROD TXNDC5 TXNDC5 GPX4 GPX4 UBC UBC ERP44 ERP44 PRDX4 PRDX4 PDIA3 PDIA3 TXN TXN PRDX5 PRDX5 P4HB P4HB PDIA6 PDIA6
"PRDX4" - peroxiredoxin 4 in Homo sapiens
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protein of unknown 3D structure
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PRDX4peroxiredoxin 4; Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (271 aa)    
Predicted Functional Partners:
UBC
ubiquitin C (685 aa)
        score_image   score_image   0.971
ERP44
endoplasmic reticulum 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 ERO1L and ERO1LB in the endoplasmic reticulum (406 aa)
score_image       score_image   score_image   0.939
UROD
uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (367 aa)
      score_image     score_image   0.906
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   0.899
TXNDC5
thioredoxin domain containing 5 (endoplasmic reticulum); Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide- isomerase deficiency in yeast (By similarity) (432 aa)
score_image       score_image   score_image   0.899
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   score_image   0.898
PDIA3
protein disulfide isomerase family A, member 3 (505 aa)
score_image     score_image score_image   score_image   0.891
PRDX5
peroxiredoxin 5; Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling (214 aa)
      score_image score_image   score_image   0.877
PDIA6
protein disulfide isomerase family A, member 6; May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (440 aa)
score_image       score_image   score_image   0.848
P4HB
prolyl 4-hydroxylase, beta polypeptide; 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 [...] (508 aa)
score_image     score_image score_image   score_image   0.844
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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