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DUOX1 DUOX1 DUOX2 DUOX2 NOX5 NOX5 SOD3 SOD3 CCDC73 CCDC73 HEPHL1 HEPHL1 NOX4 NOX4 SLC11A2 SLC11A2 NOX1 NOX1 CYBB CYBB FXN FXN
"HEPHL1" - hephaestin-like 1 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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protein homology
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[Homology]
Score
HEPHL1hephaestin-like 1; May function as a ferroxidase and may be involved in copper transport and homeostasis (By similarity) (1159 aa)    
Predicted Functional Partners:
FXN
frataxin; Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown usin [...] (210 aa)
            score_image   0.645
SLC11A2
solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2 (590 aa)
        score_image   score_image   0.643
CCDC73
coiled-coil domain containing 73 (1079 aa)
            score_image   0.561
SOD3
superoxide dismutase 3, extracellular; Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen (240 aa)
        score_image   score_image   0.516
DUOX2
dual oxidase 2; Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain (1548 aa)
      score_image score_image   score_image   0.512
NOX5
NADPH oxidase, EF-hand calcium binding domain 5 (765 aa)
      score_image score_image   score_image   0.512
CYBB
cytochrome b-245, beta polypeptide; Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc (570 aa)
      score_image score_image   score_image   0.512
NOX1
NADPH oxidase 1; NOH-1S is a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain (564 aa)
      score_image score_image   score_image   0.512
DUOX1
dual oxidase 1; Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain (1551 aa)
      score_image score_image   score_image   0.512
NOX4
NADPH oxidase 4; Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 4 displa [...] (578 aa)
      score_image score_image   score_image   0.512
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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