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) | ||
 | RBP2 | retinol binding protein 2, cellular; Intracellular transport of retinol (134 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) | ||
 | ALDH1A2 | aldehyde dehydrogenase 1 family, member A2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity) (518 aa) | ||
 | BCMO1 | beta-carotene 15,15’-monooxygenase 1; Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15’-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed (547 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) | ||
 | 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) | ||
 | ALDH1A1 | aldehyde dehydrogenase 1 family, member A1; Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity) (501 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) | ||
 | AOX1 | aldehyde oxidase 1 (1338 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) | ||
 | MYC | v-myc myelocytomatosis viral oncogene homolog (avian); Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5’-CAC[GA]TG-3’. Seems to activate the transcription of growth-related genes (454 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) | ||
 | TEX13A | testis expressed 13A (409 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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