node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADH1A | ALDH1A2 | ENSP00000209668 | ENSP00000249750 | alcohol dehydrogenase 1A (class I), alpha polypeptide | 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) | 0.939 |
ADH1A | CYP26A1 | ENSP00000209668 | ENSP00000224356 | alcohol dehydrogenase 1A (class I), alpha polypeptide | 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 | 0.944 |
ADH1B | ALDH1A2 | ENSP00000306606 | ENSP00000249750 | alcohol dehydrogenase 1B (class I), beta polypeptide | 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) | 0.941 |
ADH1B | CYP26A1 | ENSP00000306606 | ENSP00000224356 | alcohol dehydrogenase 1B (class I), beta polypeptide | 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 | 0.941 |
ADH4 | ADH7 | ENSP00000265512 | ENSP00000420269 | alcohol dehydrogenase 4 (class II), pi polypeptide | 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 | 0.591 |
ADH4 | ALDH1A2 | ENSP00000265512 | ENSP00000249750 | alcohol dehydrogenase 4 (class II), pi polypeptide | 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) | 0.944 |
ADH4 | CYP26A1 | ENSP00000265512 | ENSP00000224356 | alcohol dehydrogenase 4 (class II), pi polypeptide | 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 | 0.923 |
ADH4 | RDH10 | ENSP00000265512 | ENSP00000240285 | alcohol dehydrogenase 4 (class II), pi polypeptide | 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 | 0.436 |
ADH5 | ALDH1A2 | ENSP00000296412 | ENSP00000249750 | 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 | 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) | 0.946 |
ADH5 | CYP26A1 | ENSP00000296412 | ENSP00000224356 | 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 | 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 | 0.938 |
ADH5 | RDH10 | ENSP00000296412 | ENSP00000240285 | 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 | 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 | 0.439 |
ADH7 | ADH4 | ENSP00000420269 | ENSP00000265512 | 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 | alcohol dehydrogenase 4 (class II), pi polypeptide | 0.591 |
ADH7 | ALDH1A2 | ENSP00000420269 | ENSP00000249750 | 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 | 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) | 0.943 |
ADH7 | CYP26A1 | ENSP00000420269 | ENSP00000224356 | 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 | 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 | 0.929 |
ADH7 | RDH10 | ENSP00000420269 | ENSP00000240285 | 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 | 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 | 0.400 |
ALDH1A2 | ADH1A | ENSP00000249750 | ENSP00000209668 | 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) | alcohol dehydrogenase 1A (class I), alpha polypeptide | 0.939 |
ALDH1A2 | ADH1B | ENSP00000249750 | ENSP00000306606 | 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) | alcohol dehydrogenase 1B (class I), beta polypeptide | 0.941 |
ALDH1A2 | ADH4 | ENSP00000249750 | ENSP00000265512 | 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) | alcohol dehydrogenase 4 (class II), pi polypeptide | 0.944 |
ALDH1A2 | ADH5 | ENSP00000249750 | ENSP00000296412 | 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) | 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 | 0.946 |
ALDH1A2 | ADH7 | ENSP00000249750 | ENSP00000420269 | 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) | 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 | 0.943 |