GPX4 Back

glutathione peroxidase 4 (phospholipid hydroperoxidase)

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NCBI Description of GPX4

Glutathione peroxidase catalyzes the reduction of hydrogen peroxide, organic hydroperoxide, and lipid peroxides by reduced glutathione and functions in the protection of cells against oxidative damage. Human plasma glutathione peroxidase has been shown to be a selenium-containing enzyme and the UGA codon is translated into a selenocysteine. Through alternative splicing and transcription initiation, rat produces proteins that localize to the nucleus, mitochondrion, and cytoplasm. In humans, experimental evidence for alternative splicing exists; alternative transcription initiation and the cleavage sites of the mitochondrial and nuclear transit peptides need to be experimentally verified.

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Figure notes


• "Mouse over" a mutation to see details.
• Missense green saturation indicates evolutionary conservation of the mutated positions.
• Red hashes in protein strip are splice sites.
• Blue-white-red bars are log2 copy ratio distributions (–1 to +1) from Zack et al. (2013).


Legend

GPX4 is highly significantly mutated in
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GPX4 is significantly mutated in
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GPX4 is near significance in
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Click on a tumor type to see its full list of significant genes.

Data details


Mutation list for GPX4