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) | ||
 | 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) | ||
 | CYP2C9 | cytochrome P450, family 2, subfamily C, polypeptide 9; 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. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan (490 aa) | ||
 | EPHX1 | epoxide hydrolase 1, microsomal (xenobiotic) (455 aa) | ||
 | CYP2C18 | cytochrome 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) | ||
 | CYP2B6 | cytochrome P450, family 2, subfamily B, polypeptide 6; 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. Acts as a 1,4-cineole 2-exo-monooxygenase (491 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) | ||
 | GGT7 | gamma-glutamyltransferase 7; Cleaves glutathione conjugates (By similarity) (662 aa) | ||
 | UBC | ubiquitin C (685 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) | ||
 | GPX4 | glutathione peroxidase 4; Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity) (197 aa) | ||
 | MAPK8 | mitogen-activated protein kinase 8; Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JU [...] (427 aa) | ||
 | GPX6 | glutathione peroxidase 6 (olfactory) (221 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) | ||
 | GSTA4 | glutathione 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) | ||
 | CYP1A1 | cytochrome P450, family 1, subfamily A, polypeptide 1; 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 (512 aa) | ||
 | ADH6 | alcohol dehydrogenase 6 (class V) (375 aa) | ||
 | GSTP1 | glutathione S-transferase pi 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (210 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) | ||
 | GPX8 | glutathione peroxidase 8 (putative) (209 aa) | ||
 | GGT6 | gamma-glutamyltransferase 6; Cleaves glutathione conjugates (By similarity) (493 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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