Harmonizome 3.0

glutathione S-transferase zeta 1

This gene is a member of the glutathione S-transferase (GSTs) super-family which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme catalyzes the conversion of maleylacetoacetate to fumarylacetoacatate, which is one of the steps in the phenylalanine/tyrosine degradation pathway. Deficiency of a similar gene in mouse causes oxidative stress. Several transcript variants of this gene encode multiple protein isoforms. [provided by RefSeq, Jul 2015]

glutathione S-transferase theta-4-like

glutathione S-transferase theta pseudogene 1

Predicted to enable glutathione transferase activity. Predicted to be involved in glutathione metabolic process. Predicted to be active in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

glutathione S-transferase theta pseudogene 2

glutathione S-transferase alpha 4

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-tranferase belonging to the alpha class. The alpha class genes, which are located in a cluster on chromosome 6, are highly related and encode enzymes with glutathione peroxidase activity that function in the detoxification of lipid peroxidation products. Reactive electrophiles produced by oxidative metabolism have been linked to a number of degenerative diseases including Parkinson's disease, Alzheimer's disease, cataract formation, and atherosclerosis. [provided by RefSeq, Jul 2008]

glutathione S-transferase alpha 5

The glutathione S-transferases (GST; EC 2.5.1.18) catalyze the conjugation of reduced glutathiones and a variety of electrophiles, including many known carcinogens and mutagens. The cytosolic GSTs belong to a large superfamily, with members located on different chromosomes. For additional information on GSTs, see GSTA1 (MIM 138359).[supplied by OMIM, Sep 2008]

glutathione S-transferase alpha 1

This gene encodes a member of a family of enzymes that function to add glutathione to target electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. This action is an important step in detoxification of these compounds. This subfamily of enzymes has a particular role in protecting cells from reactive oxygen species and the products of peroxidation. Polymorphisms in this gene influence the ability of individuals to metabolize different drugs. This gene is located in a cluster of similar genes and pseudogenes on chromosome 6. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2016]

glutathione S-transferase alpha 2

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-tranferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation. [provided by RefSeq, Jul 2008]

glutathione S-transferase alpha 3

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-tranferase belonging to the alpha class genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined. [provided by RefSeq, Jul 2008]

glutathione S-transferase mu 2 (muscle) pseudogene 1

glutathione S-transferase alpha 12, pseudogene

glutathione S-transferase pi 1 pseudogene 1

glutathione S-transferase alpha 8, pseudogene

glutathione S-transferase theta 2B (gene/pseudogene)

The protein encoded by this gene, glutathione S-transferase (GST) theta 2B (GSTT2B), is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: alpha, mu, pi, theta, and zeta. The theta class includes GSTT1, GSTT2, and GSTT2B. GSTT2 and GSTT2B are nearly identical to each other, and share 55% amino acid identity with GSTT1. All three genes may play a role in human carcinogenesis. The GSTT2B gene is a pseudogene in some populations. [provided by RefSeq, Sep 2015]

glutathione S-transferase mu 3 pseudogene 1

glutathione S-transferase theta 1 pseudogene

microsomal glutathione S-transferase 2

The MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, several of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. This gene encodes a protein which catalyzes the conjugation of leukotriene A4 and reduced glutathione to produce leukotriene C4. Alternatively spliced transcript variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Feb 2011]

microsomal glutathione S-transferase 3

This gene encodes a member of the MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) protein family. Members of this family are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. This gene encodes an enzyme which catalyzes the conjugation of leukotriene A4 and reduced glutathione to produce leukotriene C4. This enzyme also demonstrates glutathione-dependent peroxidase activity towards lipid hydroperoxides.[provided by RefSeq, May 2011]

microsomal glutathione S-transferase 1

The MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, two of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. Other family members, demonstrating glutathione S-transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the endoplasmic reticulum and outer mitochondrial membrane where it is thought to protect these membranes from oxidative stress. Several transcript variants, some non-protein coding and some protein coding, have been found for this gene. [provided by RefSeq, May 2012]

glutathione S-transferase alpha 7, pseudogene

glutathione S-transferase pi 1

Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. This GST family member is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases. [provided by RefSeq, Jul 2008]

glutathione S-transferase omega 2

The protein encoded by this gene is an omega class glutathione S-transferase (GST). GSTs are involved in the metabolism of xenobiotics and carcinogens. Four transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jul 2010]

glutathione S-transferase omega 1

The protein encoded by this gene is an omega class glutathione S-transferase (GST) with glutathione-dependent thiol transferase and dehydroascorbate reductase activities. GSTs are involved in the metabolism of xenobiotics and carcinogens. The encoded protein acts as a homodimer and is found in the cytoplasm. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2010]

glutathione S-transferase mu 3 pseudogene 2

glutathione S-transferase theta 2 (gene/pseudogene)

The protein encoded by this gene, glutathione S-transferase (GST) theta 2 (GSTT2), is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: alpha, mu, pi, theta, and zeta. The theta class includes GSTT1, GSTT2, and GSTT2B. GSTT2 and GSTT2B are nearly identical to each other, and share 55% amino acid identity with GSTT1. All three genes may play a role in human carcinogenesis. The GSTT2 gene is a pseudogene in some populations. [provided by RefSeq, Sep 2015]

glutathione S-transferase theta-1-like

glutathione S-transferase alpha 11, pseudogene

glutathione S-transferase alpha 9, pseudogene

glutathione peroxidase pseudogene 2

glutathione peroxidase pseudogene 1

ChaC glutathione-specific gamma-glutamylcyclotransferase 1

This gene encodes a member of the gamma-glutamylcyclotransferase family of proteins. The encoded protein has been shown to promote neuronal differentiation by deglycination of the Notch receptor, which prevents receptor maturation and inhibits Notch signaling. This protein may also play a role in the unfolded protein response, and in regulation of glutathione levels and oxidative balance in the cell. Elevated expression of this gene may indicate increased risk of cancer recurrence among breast and ovarian cancer patients. [provided by RefSeq, Sep 2016]

glutathione S-transferase mu 1

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene. [provided by RefSeq, Jul 2008]

glutathione S-transferase mu 2 (muscle)

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. [provided by RefSeq, Jul 2008]

glutathione S-transferase mu 3 (brain)

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Mutations of this class mu gene have been linked with a slight increase in a number of cancers, likely due to exposure with environmental toxins. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2008]

glutathione S-transferase mu 4

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Diversification of these genes has occurred in regions encoding substrate-binding domains, as well as in tissue expression patterns, to accommodate an increasing number of foreign compounds. Multiple transcript variants, each encoding a distinct protein isoform, have been identified. [provided by RefSeq, Jul 2008]

glutathione S-transferase mu 5

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Diversification of these genes has occurred in regions encoding substrate-binding domains, as well as in tissue expression patterns, to accommodate an increasing number of foreign compounds. [provided by RefSeq, Jul 2008]

glutathione S-transferase omega 3, pseudogene

glutathione S-transferase theta-1-like

glutathione S-transferase mu 5 pseudogene 1

glutathione S-transferase, C-terminal domain containing

Located in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

glutathione synthetase

Glutathione is important for a variety of biological functions, including protection of cells from oxidative damage by free radicals, detoxification of xenobiotics, and membrane transport. The protein encoded by this gene functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in this gene are a cause of glutathione synthetase deficiency. [provided by RefSeq, Jul 2008]

glutathione reductase

This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found. [provided by RefSeq, Aug 2010]

glutathione S-transferase kappa 1

This gene encodes a member of the kappa class of the glutathione transferase superfamily of enzymes that function in cellular detoxification. The encoded protein is localized to the peroxisome and catalyzes the conjugation of glutathione to a wide range of hydrophobic substates facilitating the removal of these compounds from cells. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Jan 2009]

glutathione S-transferase alpha 5 pseudogene

glutathione S-transferase alpha 10, pseudogene

glutathione S-transferase theta 1

The protein encoded by this gene, glutathione S-transferase (GST) theta 1 (GSTT1), is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: alpha, mu, pi, theta, and zeta. The theta class includes GSTT1, GSTT2, and GSTT2B. GSTT1 and GSTT2/GSTT2B share 55% amino acid sequence identity and may play a role in human carcinogenesis. The GSTT1 gene is haplotype-specific and is absent from 38% of the population. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Sep 2015]

glutathione peroxidase 1

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. Other studies indicate that H2O2 is also essential for growth-factor mediated signal transduction, mitochondrial function, and maintenance of thiol redox-balance; therefore, by limiting H2O2 accumulation, glutathione peroxidases are also involved in modulating these processes. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme is the most abundant, is ubiquitously expressed and localized in the cytoplasm, and whose preferred substrate is hydrogen peroxide. It is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. This gene contains an in-frame GCG trinucleotide repeat in the coding region, and three alleles with 4, 5 or 6 repeats have been found in the human population. The allele with 4 GCG repeats has been significantly associated with breast cancer risk in premenopausal women. Alternatively spliced transcript variants have been found for this gene. Pseudogenes of this locus have been identified on chromosomes X and 21. [provided by RefSeq, Aug 2017]

glutathione S-transferase alpha 6, pseudogene

glutathione peroxidase 3

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme is secreted, and is abundantly found in plasma. Downregulation of expression of this gene by promoter hypermethylation has been observed in a wide spectrum of human malignancies, including thyroid cancer, hepatocellular carcinoma and chronic myeloid leukemia. This isozyme is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2016]

glutathione peroxidase 2

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme is predominantly expressed in the gastrointestinal tract (also in liver in human), is localized in the cytoplasm, and whose preferred substrate is hydrogen peroxide. Overexpression of this gene is associated with increased differentiation and proliferation in colorectal cancer. This isozyme is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2016]

glutathione peroxidase 5

This gene belongs to the glutathione peroxidase family. It is specifically expressed in the epididymis in the mammalian male reproductive tract, and is androgen-regulated. Unlike several other characterized glutathione peroxidases, this enzyme is not a selenoprotein, lacking the selenocysteine residue. Thus, it is selenium-independent, and has been proposed to play a role in protecting the membranes of spermatozoa from the damaging effects of lipid peroxidation and/or preventing premature acrosome reaction. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Oct 2016]

glutathione peroxidase 4

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of hydrogen peroxide, organic hydroperoxides and lipid hydroperoxides, and thereby protect cells against oxidative damage. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme has a high preference for lipid hydroperoxides and protects cells against membrane lipid peroxidation and cell death. It is also required for normal sperm development; thus, it has been identified as a 'moonlighting' protein because of its ability to serve dual functions as a peroxidase, as well as a structural protein in mature spermatozoa. Mutations in this gene are associated with Sedaghatian type of spondylometaphyseal dysplasia (SMDS). This isozyme is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Transcript variants resulting from alternative splicing or use of alternate promoters have been described to encode isoforms with different subcellular localization. [provided by RefSeq, Dec 2018]

glutathione peroxidase 7

Enables catalase activity. Predicted to be involved in cellular response to oxidative stress. Located in endoplasmic reticulum. Implicated in Barrett's adenocarcinoma and Barrett's esophagus. [provided by Alliance of Genome Resources, Mar 2025]

glutathione peroxidase 6

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of hydrogen peroxide, organic hydroperoxides and lipid hydroperoxides, and thereby protect cells against oxidative damage. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. Expression of this gene has been observed in embryos and olfactory epithelium; however, the exact function of this gene is not known. This isozyme is a selenoprotein in humans, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. The orthologs of this gene in mouse and rat (and some other species) contain a cysteine (Cys) residue in place of the Sec residue, and their corresponding mRNAs lack SECIS element. [provided by RefSeq, Jul 2017]

glutathione peroxidase 8 (putative)

Enables peroxidase activity. Predicted to be involved in cellular response to oxidative stress. Predicted to be located in endoplasmic reticulum lumen. [provided by Alliance of Genome Resources, Mar 2025]

glutathione S-transferase theta 4

Predicted to enable glutathione transferase activity. Predicted to be involved in glutathione metabolic process. Predicted to be active in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione degradosome, DUG1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the mitochondrial degradosome cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the mitochondrial degradosome cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GO Cellular Component Annotations 2015

proteins localized to the mitochondrial degradosome cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Mitochondrial degradosome cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Bacterial degradosome cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Mitochondrial degradosome cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glutathione synthetase deficiency of erythrocytes, hemolytic anemia due to phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical Glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical N-ethylmaleimide-S-glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical S-ethyl glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical glutathione-BPDE conjugate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical S-(2,4-dinitrophenyl)glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical glutathione glycylethyl ester from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical gamma-glutamyl-glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical glutathione sulfinamide from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical 1-chloro-2,4-dinitrobenzene-glutathione conjugate from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical S-methyl glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical S-(4-nitrophenacyl)glutathione from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical Glutathione Disulfide from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical glutathione-C4 from the curated CTD Gene-Chemical Interactions dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glutathione synthetase deficiency from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glutathione Synthetase Deficiency of Erythrocytes, Hemolytic Anemia due to from the curated CTD Gene-Disease Associations dataset.

From DrugBank Drug Targets

interacting proteins for the Glutathione drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the Glutathione S-(2,4 Dinitrobenzene) drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-(N-Hydroxy-N-Iodophenylcarbamoyl)Glutathione drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the Oxidized Glutathione Disulfide drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-(N-Hydroxy-N-Bromophenylcarbamoyl)Glutathione drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-METHYL-GLUTATHIONE drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-Hydroxymethyl Glutathione drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the Glutathione Sulfonic Acid drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the GLUTATHIONE SULFINATE drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-(P-Nitrobenzyl)Glutathione drug from the curated DrugBank Drug Targets dataset.

From DrugBank Drug Targets

interacting proteins for the S-Benzyl-Glutathione drug from the curated DrugBank Drug Targets dataset.

From GAD Gene-Disease Associations

genes associated with the disease decreased glutathione production. in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term glutathione in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione derivative biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione transport biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione derivative metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione metabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the glutathione biosynthetic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione dehydrogenase (ascorbate) activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione disulfide oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the s-(hydroxymethyl)glutathione dehydrogenase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione synthase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the protein-disulfide reductase (glutathione) activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione-disulfide reductase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione transferase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phospholipid-hydroperoxide glutathione peroxidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione hydrolase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione peroxidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the glutathione binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(2-Chloroacetyl)glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the Oxidized glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(Hydroxymethyl)glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(1,2-Dichlorovinyl)glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the Glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the 2-Hydroxyestrone-4-S-glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(Formylmethyl)glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(2,2-Dichloro-1-hydroxy)ethyl glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the 4-Hydroxyestrone-2-S-glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the 2-Hydroxyestrone-1-S-glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the S-(PGJ2)-glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the Glutathione episulfonium ion metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HMDB Metabolites of Enzymes

interacting proteins for the 2-(S-Glutathionyl)acetyl glutathione metabolite from the curated HMDB Metabolites of Enzymes dataset.

From HPO Gene-Disease Associations

genes associated with the glutathione synthetase deficiency phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HumanCyc Pathways

proteins participating in the glutathione-mediated detoxification pathway from the HumanCyc Pathways dataset.

From HumanCyc Pathways

proteins participating in the glutathione biosynthesis pathway from the HumanCyc Pathways dataset.

From HumanCyc Pathways

proteins participating in the glutathione redox reactions I pathway from the HumanCyc Pathways dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione peroxidase Gpx7, putative protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin/glutathione reductase selenoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Membrane associated eicosanoid/glutathione metabolism-like domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione peroxidase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, Mu class protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione peroxidase active site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione synthase domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the HCCA isomerase/glutathione S-transferase kappa protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione synthase, N-terminal, eukaryotic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, alpha class protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione synthase, substrate-binding, eukaryotic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione synthase, alpha-helical, eukaryotic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione synthase, eukaryotic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, C-terminal-like protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione reductase, eukaryote/bacterial protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, Pi class protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Membrane-associated, eicosanoid/glutathione metabolism (MAPEG) protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione-dependent formaldehyde-activating enzyme/centromere protein V protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione peroxidase conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Glutathione S-transferase, omega-class protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From KEGG Pathways

proteins participating in the glutathione metabolism pathway from the KEGG Pathways dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal glutathione peroxidase activity phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased glutathione peroxidase activity phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased glutathione level phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the abnormal glutathione level phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the hemolytic anemia due to glutathione peroxidase deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glutathione synthetase deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the hemolytic anemia due to glutathione synthetase deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the hemolytic anemia due to glutathione reductase deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term glutathione-transferase in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Defective GSS causes Glutathione synthetase deficiency (GSS deficiency) pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Glutathione conjugation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Glutathione synthesis and recycling pathway from the Reactome Pathways dataset.

From WikiPathways Pathways 2014

proteins participating in the Glutathione and one carbon metabolism(Mus musculus) pathway from the WikiPathways Pathways 2014 dataset.

From WikiPathways Pathways 2014

proteins participating in the Glutathione metabolism(Homo sapiens) pathway from the WikiPathways Pathways 2014 dataset.

From WikiPathways Pathways 2014

proteins participating in the Glutathione metabolism(Mus musculus) pathway from the WikiPathways Pathways 2014 dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glutathione Peroxidase Deficiency, Hemolytic Anemia Possibly Due To in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glutathione Synthetase Deficiency Of Erythrocytes, Hemolytic Anemia Due To in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione transport biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione derivative biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione biosynthetic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione deglycation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione import into mitochondrion biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the glutathione derivative metabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione transferase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ABC-type glutathione S-conjugate transporter activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione transmembrane transporter activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the protein-disulfide reductase (glutathione) activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the S-(hydroxymethyl)glutathione dehydrogenase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione hydrolase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione disulfide oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the deaminated glutathione amidase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the glutathione-dependent sulfide quinone oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased glutathione level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased glutathione peroxidase activity phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the increased circulating glutathione level phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MW Enzyme Metabolite Associations

interacting proteins for Glutathione metabolite from the MW Gene Metabolite Associations dataset.

From MW Enzyme Metabolite Associations

interacting proteins for Oxidized glutathione metabolite from the MW Gene Metabolite Associations dataset.

From MW Enzyme Metabolite Associations

interacting proteins for S-(Formylmethyl)glutathione metabolite from the MW Gene Metabolite Associations dataset.

From WikiPathways Pathways 2024

proteins participating in the Glutathione metabolism pathway from the WikiPathways Pathways 2024 dataset.

From WikiPathways Pathways 2024

proteins participating in the Gamma glutamyl cycle for the biosynthesis and degradation of glutathione including diseases pathway from the WikiPathways Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glutathione conjugation pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glutathione synthesis and recycling pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione transport biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione transmembrane transport biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione derivative biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione biosynthetic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione import into mitochondrion biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the cellular response to glutathione biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the glutathione derivative metabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of glutathione peroxidase activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the response to glutathione biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione transferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the ABC-type glutathione S-conjugate transporter activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione transmembrane transporter activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the protein-disulfide reductase (glutathione) activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione hydrolase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione disulfide oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the deaminated glutathione amidase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione specific gamma-glutamylcyclotransferase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the glutathione-dependent sulfide quinone oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glutathione synthetase deficiency from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores 2025

genes co-occuring with the disease Glutathione synthetase deficiency in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Glutathione hydrolase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Glutathione synthase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Inherited glutathione synthetase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glutathione synthetase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Hemolytic anemia due to glutathione reductase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Glutathione peroxidase in non-alcoholic fatty liver disease x mastiha supplementation interaction phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From KEGG Pathways 2026

proteins participating in the Glutathione metabolism pathway from the KEGG Pathways 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the GLUTATHIONE DISULFIDE drug from theDGIdb Drug Targets 2026 dataset.