| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACACA | ALDH1A1 | ENSP00000344789 | ENSP00000297785 | acetyl-CoA carboxylase alpha | 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) | 0.636 |
| ACACA | ALDH1A2 | ENSP00000344789 | ENSP00000249750 | acetyl-CoA carboxylase alpha | 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) | 0.632 |
| ACACA | DHRS4L2 | ENSP00000344789 | ENSP00000334801 | acetyl-CoA carboxylase alpha | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) | 0.581 |
| ALDH1A1 | ACACA | ENSP00000297785 | ENSP00000344789 | 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) | acetyl-CoA carboxylase alpha | 0.636 |
| 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 | DHRS4L2 | ENSP00000297785 | ENSP00000334801 | 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) | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) | 0.925 |
| ALDH1A2 | ACACA | ENSP00000249750 | ENSP00000344789 | 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) | acetyl-CoA carboxylase alpha | 0.632 |
| 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 | DHRS4L2 | ENSP00000249750 | ENSP00000334801 | 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) | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) | 0.925 |
| 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 | DHRS4L2 | ENSP00000363832 | ENSP00000334801 | aldehyde oxidase 1 | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) | 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 | DHRS4L2 | ENSP00000421172 | ENSP00000334801 | 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 | dehydrogenase/reductase (SDR family) member 4 like 2; Probable oxidoreductase (By similarity) | 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 |
Share
