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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 | RDH8 | retinol 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) | ||
 | ADH1A | alcohol dehydrogenase 1A (class I), alpha polypeptide (375 aa) | ||
 | CYP26A1 | cytochrome 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) | ||
 | APOB | apolipoprotein B (including Ag(x) antigen) (4563 aa) | ||
 | APOA1 | apolipoprotein A-I; Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (267 aa) | ||
 | RDH10 | retinol 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) | ||
 | RDH5 | retinol dehydrogenase 5 (11-cis/9-cis); Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Also able to oxidize 9-cis-retinol and 13-cis-retinol, but not all- trans-retinol. Active in the presence of NAD as cofactor but not in the presence of NADP (318 aa) | ||
 | RPE65 | retinal 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) | ||
 | ADH4 | alcohol dehydrogenase 4 (class II), pi polypeptide (380 aa) | ||
 | RDH12 | retinol 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) | ||
 | RETSAT | retinol 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) | ||
 | 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) | ||
 | ADH1B | alcohol dehydrogenase 1B (class I), beta polypeptide (375 aa) | ||
 | SDR16C5 | short 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) | ||
 | DHRS9 | dehydrogenase/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) | ||
 | HSD17B6 | hydroxysteroid (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) | ||
 | DHRS4L2 | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) (232 aa) | ||
 | LRAT | lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase); Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chrom [...] (230 aa) | ||
 | APOA4 | apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons (396 aa) | ||
 | AKR1B10 | aldo-keto reductase family 1, member B10 (aldose reductase); Acts as all-trans-retinaldehyde reductase. Can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). May be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs (316 aa) | ||
 | APOA2 | apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism (100 aa) | ||
 | DHRS3 | dehydrogenase/reductase (SDR family) member 3; Catalyzes the reduction of all-trans-retinal to all- trans-retinol in the presence of NADPH (302 aa) | ||
 | RDH11 | retinol dehydrogenase 11 (all-trans/9-cis/11-cis); Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected (318 aa) | ||
 | ADH6 | alcohol dehydrogenase 6 (class V) (375 aa) | ||
 | RDH16 | retinol 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) | ||
 | 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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