Page last updated: 2024-08-07 10:17:42

Phospholipid hydroperoxide glutathione peroxidase

A phospholipid hydroperoxide glutathione peroxidase GPX4 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P36969]

Synonyms

PHGPx;
EC 1.11.1.12;
Glutathione peroxidase 4;
GPx-4;
GSHPx-4

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's1 (100.00)2.80

Compounds (4)

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
2-chloro-N-heptyl-N-(3-methylphenyl)acetamideHomo sapiens (human)EC5015.170022
N-(1,3-benzodioxol-5-yl)-2-chloro-N-[(2-prop-2-enoxyphenyl)methyl]acetamideHomo sapiens (human)EC5017.300022
ML162Homo sapiens (human)EC501.114022
ML-210Homo sapiens (human)EC5016.522022

Enables

This protein enables 5 target(s):

TargetCategoryDefinition
glutathione peroxidase activitymolecular functionCatalysis of the reaction: 2 glutathione + hydrogen peroxide = oxidized glutathione + 2 H2O. [EC:1.11.1.9, PMID:36771108]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
selenium bindingmolecular functionBinding to a selenium (Se) ion. [GOC:ai]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
phospholipid-hydroperoxide glutathione peroxidase activitymolecular functionCatalysis of the reaction: a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O. [PMID:3978121, PMID:8617728, RHEA:19057]

Located In

This protein is located in 4 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
nuclear envelopecellular componentThe double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]

Involved In

This protein is involved in 11 target(s):

TargetCategoryDefinition
chromatin organizationbiological processThe assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. [PMID:20404130]
phospholipid metabolic processbiological processThe chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester. [ISBN:0198506732]
response to oxidative stressbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:jl, PMID:12115731]
spermatogenesisbiological processThe developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa. [GOC:jid, ISBN:9780878933846, PMID:28073824, PMID:30990821]
arachidonic acid metabolic processbiological processThe chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. [ISBN:0198506732]
lipoxygenase pathwaybiological processThe chemical reactions and pathways by which an unsaturated fatty acid (such as arachidonic acid or linolenic acid) is converted to other compounds, and in which the first step is hydroperoxide formation catalyzed by lipoxygenase. [GOC:mah, PMID:17163881]
response to estradiolbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen. [GOC:mah, ISBN:0911910123]
long-chain fatty acid biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of a long-chain fatty acid. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons. [PMID:18390550]
protein polymerizationbiological processThe process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein. [GOC:ai]
cellular oxidant detoxificationbiological processAny process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide. [GOC:dos, GOC:vw]
negative regulation of ferroptosisbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of ferroptosis. [GOC:sp, PMID:24439385, PMID:25402683, PMID:29290465]