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HMOX1 | heme oxygenase (decycling) 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed (288 aa) | |||
HMOX2 | heme oxygenase (decycling) 2; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter (316 aa) | |||
ORM1 | orosomucoid 1; Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction (201 aa) | |||
BLVRB | biliverdin reductase B (flavin reductase (NADPH)); Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin (206 aa) | |||
BLVRA | biliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor (296 aa) | |||
FLAD1 | FAD1 flavin adenine dinucleotide synthetase homolog (S. cerevisiae); Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme (587 aa) | |||
UGT1A6 | UDP glucuronosyltransferase 1 family, polypeptide A6; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols (532 aa) | |||
UGT2B7 | UDP glucuronosyltransferase 2 family, polypeptide B7; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (529 aa) | |||
UGT1A1 | UDP glucuronosyltransferase 1 family, polypeptide A1; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4- methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone (533 aa) | |||
UGT2B4 | UDP glucuronosyltransferase 2 family, polypeptide B4; UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4- nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is capable of 6 alpha-hydroxyglucuronidation of hyodeoxycholic acid (528 aa) | |||
UGT2B17 | UDP glucuronosyltransferase 2 family, polypeptide B17; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT) (530 aa) | |||
UGT1A10 | UDP glucuronosyltransferase 1 family, polypeptide A10; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 aa) | |||
UBC | ubiquitin C (685 aa) | |||
UGT1A9 | UDP glucuronosyltransferase 1 family, polypeptide A9; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols (530 aa) | |||
ENPP3 | ectonucleotide pyrophosphatase/phosphodiesterase 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity) (875 aa) | |||
ENPP1 | ectonucleotide pyrophosphatase/phosphodiesterase 1; By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. In vitro, has a broad specificity, hydrolyzing other nucleoside 5’ triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3’,5’-cAMP to AMP. May also be involved in the regu [...] (925 aa) | |||
UGT1A4 | UDP glucuronosyltransferase 1 family, polypeptide A4; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate (534 aa) | |||
UGT1A5 | UDP glucuronosyltransferase 1 family, polypeptide A5; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (534 aa) | |||
UGT1A7 | UDP glucuronosyltransferase 1 family, polypeptide A7; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 aa) | |||
UGT1A8 | UDP glucuronosyltransferase 1 family, polypeptide A8; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (530 aa) | |||
GMDS | GDP-mannose 4,6-dehydratase; Catalyzes the conversion of GDP-D-mannose to GDP-4- dehydro-6-deoxy-D-mannose (372 aa) | |||
SUMO1 | SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae); Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. [...] (101 aa) | |||
RPL31 | ribosomal protein L31 (128 aa) | |||
UGT2B11 | UDP glucuronosyltransferase 2 family, polypeptide B11; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (529 aa) | |||
UGT2A1 | UDP glucuronosyltransferase 2 family, polypeptide A1, complex locus; UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium (536 aa) | |||
UGT1A3 | UDP glucuronosyltransferase 1 family, polypeptide A3; UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (534 aa) |