node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABCA4 | LRAT | ENSP00000359245 | ENSP00000337224 | ATP-binding cassette, sub-family A (ABC1), member 4; In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans- retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removi [...] | 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 [...] | 0.471 |
ABCA4 | RDH12 | ENSP00000359245 | ENSP00000267502 | ATP-binding cassette, sub-family A (ABC1), member 4; In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans- retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removi [...] | 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 | 0.970 |
ALDH1A1 | BCMO1 | ENSP00000297785 | ENSP00000258168 | 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) | 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 | 0.925 |
ALDH1A1 | CYP26A1 | ENSP00000297785 | ENSP00000224356 | 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) | 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 | 0.963 |
ALDH1A1 | RDH12 | ENSP00000297785 | ENSP00000267502 | 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) | 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 | 0.930 |
ALDH1A1 | UBC | ENSP00000297785 | ENSP00000344818 | 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) | ubiquitin C | 0.705 |
ALDH1A2 | BCMO1 | ENSP00000249750 | ENSP00000258168 | 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) | 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 | 0.923 |
ALDH1A2 | CYP26A1 | ENSP00000249750 | ENSP00000224356 | 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) | 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 | 0.982 |
ALDH1A2 | RDH12 | ENSP00000249750 | ENSP00000267502 | 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) | 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 | 0.930 |
ALDH1A2 | UBC | ENSP00000249750 | ENSP00000344818 | 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) | ubiquitin C | 0.795 |
AOX1 | BCMO1 | ENSP00000363832 | ENSP00000258168 | aldehyde oxidase 1 | 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 | 0.906 |
AOX1 | CYP26A1 | ENSP00000363832 | ENSP00000224356 | aldehyde oxidase 1 | 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 | 0.906 |
AOX1 | RDH12 | ENSP00000363832 | ENSP00000267502 | aldehyde oxidase 1 | 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 | 0.910 |
AWAT2 | CYP26A1 | ENSP00000421172 | ENSP00000224356 | acyl-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 | 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 | 0.905 |
AWAT2 | RDH12 | ENSP00000421172 | ENSP00000267502 | acyl-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 | 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 | 0.905 |
AWAT2 | RETSAT | ENSP00000421172 | ENSP00000295802 | acyl-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 | 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) | 0.900 |
BCMO1 | ALDH1A1 | ENSP00000258168 | ENSP00000297785 | 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 | 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) | 0.925 |
BCMO1 | ALDH1A2 | ENSP00000258168 | ENSP00000249750 | 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 | 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) | 0.923 |
BCMO1 | AOX1 | ENSP00000258168 | ENSP00000363832 | 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 | aldehyde oxidase 1 | 0.906 |
BCMO1 | RDH12 | ENSP00000258168 | ENSP00000267502 | 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 | 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 | 0.941 |