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ALDH1A3 ALDH1A3 TXNDC12 TXNDC12 GPX2 GPX2 GPX7 GPX7 GGT1 GGT1 ADH7 ADH7 GSR GSR GSTT1 GSTT1 GSTO1 GSTO1 GGT5 GGT5 CYP2S1 CYP2S1 GSTA4 GSTA4 GSTT2B GSTT2B GSTM1 GSTM1 CYP2C18 CYP2C18 GSTM4 GSTM4 GSTA1 GSTA1 ALDH3A1 ALDH3A1 GSTA2 GSTA2 CYP2A13 CYP2A13 GPX1 GPX1 CYP3A5 CYP3A5 CYP2C8 CYP2C8 EPHX1 EPHX1 CYP1A2 CYP1A2 CYP2F1 CYP2F1
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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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some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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from curated databases
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Predicted Interactions
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GSRglutathione reductase; Maintains high levels of reduced glutathione in the cytosol (522 aa)
CYP3A5cytochrome P450, family 3, subfamily A, polypeptide 5; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics (502 aa)
ALDH3A1aldehyde dehydrogenase 3 family, member A1; ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes (453 aa)
GGT1gamma-glutamyltransferase 1; Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive (569 aa)
GSTT1glutathione S-transferase theta 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2- epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4- nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide (240 aa)
EPHX1epoxide hydrolase 1, microsomal (xenobiotic) (455 aa)
CYP2C18cytochrome P450, family 2, subfamily C, polypeptide 18; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics (490 aa)
GSTT2Bglutathione S-transferase theta 2B (gene/pseudogene); Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity (244 aa)
CYP2S1cytochrome P450, family 2, subfamily S, polypeptide 1; Has a potential importance for extrahepatic xenobiotic metabolism (504 aa)
GSTM1glutathione S-transferase mu 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (218 aa)
ALDH1A3aldehyde dehydrogenase 1 family, member A3; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system (By similarity) (512 aa)
CYP2A13cytochrome P450, family 2, subfamily A, polypeptide 13; Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N- dimethylaniline, 2’-methoxyacetophenone, N- nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4- (methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity (494 aa)
CYP2F1cytochrome P450, family 2, subfamily F, polypeptide 1; May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3- methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine (491 aa)
GSTA1glutathione S-transferase alpha 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (222 aa)
CYP1A2cytochrome P450, family 1, subfamily A, polypeptide 2; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic a [...] (516 aa)
GPX7glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks (187 aa)
GSTO1glutathione S-transferase omega 1; Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid (241 aa)
GSTM4glutathione S-transferase mu 4; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1- chloro-2,4-dinitrobenzene (218 aa)
GSTA4glutathione S-transferase alpha 4; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE) (222 aa)
CYP2C8cytochrome P450, family 2, subfamily C, polypeptide 8; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol) (490 aa)
TXNDC12thioredoxin domain containing 12 (endoplasmic reticulum); Possesses significant protein thiol-disulfide oxidase activity (172 aa)
GPX2glutathione peroxidase 2 (gastrointestinal); Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors (190 aa)
GGT5gamma-glutamyltransferase 5; Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4) (587 aa)
GPX1glutathione peroxidase 1; Protects the hemoglobin in erythrocytes from oxidative breakdown (203 aa)
GSTA2glutathione S-transferase alpha 2; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (222 aa)
ADH7alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide; Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism (394 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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