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UGT2B7 UGT2B7 CYP2S1 CYP2S1 CYP1A2 CYP1A2 UGT2B17 UGT2B17 CYP2A6 CYP2A6 UGT1A1 UGT1A1 CYP4A11 CYP4A11 CYP3A4 CYP3A4 UGT1A6 UGT1A6 CYP3A7 CYP3A7 CYP2C8 CYP2C8 CYP3A5 CYP3A5 UGT1A8 UGT1A8 CYP26A1 CYP26A1 ADH4 ADH4 DHRS4L2 DHRS4L2 UGT1A5 UGT1A5 UGT1A7 UGT1A7 UGT1A10 UGT1A10 UGT2B11 UGT2B11 ADH5 ADH5 AWAT2 AWAT2 PNPLA4 PNPLA4 RETSAT RETSAT RDH12 RDH12 DHRS3 DHRS3
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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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second shell of interactors
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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)
CYP26A1cytochrome P450, family 26, subfamily A, polypeptide 1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA (497 aa)
ADH4alcohol dehydrogenase 4 (class II), pi polypeptide (380 aa)
RDH12retinol dehydrogenase 12 (all-trans/9-cis/11-cis); Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments (316 aa)
RETSATretinol saturase (all-trans-retinol 13,14-reductase); Retinol saturase carrying out the saturation of the 13- 14 double bond of all-trans-retinol to produce all-trans-13,14- dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A (By similarity) (610 aa)
ADH5alcohol 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)
CYP2A6cytochrome P450, family 2, subfamily A, polypeptide 6 (494 aa)
UGT1A6UDP glucuronosyltransferase 1 family, polypeptide A6; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols (532 aa)
UGT2B7UDP glucuronosyltransferase 2 family, polypeptide B7; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (529 aa)
UGT1A1UDP glucuronosyltransferase 1 family, polypeptide A1; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4- methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone (533 aa)
CYP2S1cytochrome P450, family 2, subfamily S, polypeptide 1; Has a potential importance for extrahepatic xenobiotic metabolism (504 aa)
CYP4A11cytochrome P450, family 4, subfamily A, polypeptide 11; Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE) (519 aa)
UGT2B17UDP glucuronosyltransferase 2 family, polypeptide B17; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT) (530 aa)
DHRS4L2dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) (232 aa)
CYP3A7cytochrome P450, family 3, subfamily A, polypeptide 7; 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 (503 aa)
CYP3A4cytochrome 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)
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)
UGT1A10UDP glucuronosyltransferase 1 family, polypeptide A10; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 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)
UGT1A5UDP glucuronosyltransferase 1 family, polypeptide A5; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (534 aa)
UGT1A7UDP glucuronosyltransferase 1 family, polypeptide A7; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 aa)
UGT1A8UDP glucuronosyltransferase 1 family, polypeptide A8; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 aa)
DHRS3dehydrogenase/reductase (SDR family) member 3; Catalyzes the reduction of all-trans-retinal to all- trans-retinol in the presence of NADPH (302 aa)
PNPLA4patatin-like phospholipase domain containing 4; Lipid hydrolase (253 aa)
UGT2B11UDP glucuronosyltransferase 2 family, polypeptide B11; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (529 aa)
AWAT2acyl-CoA wax alcohol acyltransferase 2; Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA-retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo (333 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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