Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | ADH1A | alcohol dehydrogenase 1A (class I), alpha polypeptide (375 aa) | ||
 | GSTA3 | glutathione S-transferase alpha 3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively (222 aa) | ||
 | GSR | glutathione reductase; Maintains high levels of reduced glutathione in the cytosol (522 aa) | ||
 | ALDH3A1 | aldehyde 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) | ||
 | GGT1 | gamma-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) | ||
 | GSTM5 | glutathione S-transferase mu 5; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (218 aa) | ||
 | ADH4 | alcohol dehydrogenase 4 (class II), pi polypeptide (380 aa) | ||
 | EPHX1 | epoxide hydrolase 1, microsomal (xenobiotic) (455 aa) | ||
 | GSTT2B | glutathione 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) | ||
 | ADH5 | alcohol dehydrogenase 5 (class III), chi polypeptide; Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (374 aa) | ||
 | CYP2S1 | cytochrome P450, family 2, subfamily S, polypeptide 1; Has a potential importance for extrahepatic xenobiotic metabolism (504 aa) | ||
 | GSTM1 | glutathione S-transferase mu 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (218 aa) | ||
 | ALDH1A3 | aldehyde 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) | ||
 | CYP2A13 | cytochrome 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) | ||
 | CYP2F1 | cytochrome 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) | ||
 | CYP3A4 | cytochrome P450, family 3, subfamily A, polypeptide 4; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1’-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2- exo-monooxygenase. The enzyme also hydroxylates etoposide (503 aa) | ||
 | GGT7 | gamma-glutamyltransferase 7; Cleaves glutathione conjugates (By similarity) (662 aa) | ||
 | CYP1A2 | cytochrome 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) | ||
 | GSTO2 | glutathione S-transferase omega 2; Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) (243 aa) | ||
 | GSTO1 | glutathione 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) | ||
 | GSTM4 | glutathione 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) | ||
 | TXNDC12 | thioredoxin domain containing 12 (endoplasmic reticulum); Possesses significant protein thiol-disulfide oxidase activity (172 aa) | ||
 | ADH6 | alcohol dehydrogenase 6 (class V) (375 aa) | ||
 | GPX1 | glutathione peroxidase 1; Protects the hemoglobin in erythrocytes from oxidative breakdown (203 aa) | ||
 | GSTA2 | glutathione S-transferase alpha 2; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (222 aa) | ||
 | ADH7 | alcohol 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
Other names: H. sapiens, Homo, Homo sapiens, human, man
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