| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | SDR16C5 | ENSP00000297785 | ENSP00000307607 | 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) | 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 | 0.934 |
| 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 | SDR16C5 | ENSP00000249750 | ENSP00000307607 | 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) | 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 | 0.935 |
| 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 | SDR16C5 | ENSP00000363832 | ENSP00000307607 | aldehyde oxidase 1 | 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 | 0.910 |
| 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 |
| AWAT2 | SDR16C5 | ENSP00000421172 | ENSP00000307607 | 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 | 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 | 0.905 |
| 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 | SDR16C5 | ENSP00000258168 | ENSP00000307607 | 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 | 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 | 0.926 |
| CHCHD7 | PLAG1 | ENSP00000306425 | ENSP00000325546 | coiled-coil-helix-coiled-coil-helix domain containing 7 | pleiomorphic adenoma gene 1; Transcription factor whose activation results in up- regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation- when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hep [...] | 0.782 |
| CHCHD7 | SDR16C5 | ENSP00000306425 | ENSP00000307607 | coiled-coil-helix-coiled-coil-helix domain containing 7 | 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 | 0.697 |
| LRAT | RETSAT | ENSP00000337224 | ENSP00000295802 | 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 [...] | 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) | 0.922 |
| LRAT | SDR16C5 | ENSP00000337224 | ENSP00000307607 | 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 [...] | 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 | 0.912 |
| PLAG1 | CHCHD7 | ENSP00000325546 | ENSP00000306425 | pleiomorphic adenoma gene 1; Transcription factor whose activation results in up- regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation- when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hep [...] | coiled-coil-helix-coiled-coil-helix domain containing 7 | 0.782 |
| PLAG1 | SDR16C5 | ENSP00000325546 | ENSP00000307607 | pleiomorphic adenoma gene 1; Transcription factor whose activation results in up- regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation- when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hep [...] | 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 | 0.602 |
| PNPLA4 | RETSAT | ENSP00000370430 | ENSP00000295802 | patatin-like phospholipase domain containing 4; Lipid hydrolase | 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 |
| PNPLA4 | SDR16C5 | ENSP00000370430 | ENSP00000307607 | patatin-like phospholipase domain containing 4; Lipid hydrolase | 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 | 0.900 |
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