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ADH1A ADH1A ADH1B ADH1B SDR16C5 SDR16C5 RDH16 RDH16 ADH6 ADH6 DHRS4L2 DHRS4L2 CYP26A1 CYP26A1 ADH5 ADH5 RETSAT RETSAT HSD17B6 HSD17B6 DHRS9 DHRS9 PNPLA4 PNPLA4 DHRS3 DHRS3 ADH4 ADH4 ADH7 ADH7 RDH10 RDH10 RDH12 RDH12 RDH8 RDH8 EIF4B EIF4B RPE65 RPE65
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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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second shell of interactors
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RDH8retinol dehydrogenase 8 (all-trans); Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity (By similarity) (311 aa)
ADH1Aalcohol dehydrogenase 1A (class I), alpha polypeptide (375 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)
RDH10retinol dehydrogenase 10 (all-trans); Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (341 aa)
EIF4Beukaryotic translation initiation factor 4B; Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5’- terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F (611 aa)
RPE65retinal pigment epithelium-specific protein 65kDa; Plays important roles in the production of 11-cis retinal and in visual pigment regeneration. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis- retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT. The enzymatic activity is linearly dependent of th [...] (533 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)
ADH1Balcohol dehydrogenase 1B (class I), beta polypeptide (375 aa)
SDR16C5short chain dehydrogenase/reductase family 16C, member 5; Oxidoreductase with strong preference for NAD. Active in both the oxidative and reductive directions. Oxidizes all-trans- retinol in all-trans-retinaldehyde. No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH (309 aa)
DHRS9dehydrogenase/reductase (SDR family) member 9; 3-alpha-hydroxysteroid dehydrogenase that converts 3- alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH (319 aa)
HSD17B6hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse); NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3- alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is firs [...] (317 aa)
DHRS4L2dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) (232 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)
ADH6alcohol dehydrogenase 6 (class V) (375 aa)
RDH16retinol dehydrogenase 16 (all-trans); Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction (317 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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