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1alpha,25-dihydroxyvitamin D2 + O2 + [reduced NADPH-hemoprotein reductase] + H+
1alpha,25,26-trihydroxyvitamin D2 + [oxidized NADPHhemoprotein reductase] + H2O
-
-
-
?
1alpha,25-dihydroxyvitamin D3 + O2 + [reduced NADPH-hemoprotein reductase] + H+
1alpha,25,26-trihydroxyvitamin D3 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
1alpha-hydroxy-vitamin D2 + O2 + [reduced NADPH-hemoprotein reductase] + H+
1alpha,25-dihydroxy-vitamin D2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
1alpha-hydroxy-vitamin D3 + O2 + [reduced NADPH-hemoprotein reductase] + H+
1alpha,25-dihydroxy-vitamin D3 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
1alpha-hydroxycholecalciferol + O2 + NADPH + H+
1alpha,25-dihydroxycholecalciferol + NADP+ + H2O
-
-
-
-
?
1alpha-hydroxyvitamin D2 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D2 + NADP+ + H2O
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxy-vitamin D3 + NADP+ + H2O
-
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
25-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyitamin D3 + NADP+ + H2O
-
additional product: 24,25-dihydroxyvitamin D3
-
?
bufuralol + O2 + NADPH + H+
1'-hydroxybufuralol + NADP+ + H2O
-
-
-
-
?
calciferol + O2 + [reduced NADPH-hemoprotein reductase]
25-hydroxy-vitamin D2 + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme CYP2R1 hydroxylates vitamin D2 at position C-25 position
-
-
?
calciferol + O2 + [reduced NADPH-hemoprotein reductase]
25-hydroxyergocalciferol + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme CYP2R1 hydroxylates vitamin D2 at position C-25 position
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
cholecalciferol + O2 + NADPH + H+
25-hydroxycholecalciferol + NADP+ + H2O
-
at about 20% of the rate with 1alpha-hydroxycholecalciferol
-
-
?
ebastin + O2 + NADPH + H+
? + NADP+ + H2O
histamine H1-recepter antagonist
-
-
?
tolterodine + O2 + NADPH + H+
? + NADP+ + H2O
-
-
-
-
?
vitamin D2 + O2 + NADPH + H+
25-hydroxy-vitamin D2 + NADP+ + H2O
-
-
-
-
?
vitamin D2 + O2 + NADPH + H+
25-hydroxyvitamin D2 + NADP+ + H2O
vitamin D3 + O2 + NADPH + H+
1alpha, 25-dihydroxy-vitamin D3 + NADP+ + H2O
vitamin D3 + O2 + NADPH + H+
25-hydroxy-vitamin D3 + NADP+ + H2O
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
additional information
?
-
1alpha-hydroxyvitamin D2 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D2 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D2 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D2 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
1alpha,25-dihydroxyvitamin D3 + NADP+ + H2O
-
-
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme CYP2R1 hydroxylates vitamin D3 at position C-25 position
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme CYP2R1 hydroxylates vitamin D3 at position C-25 position
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
the microsomal enzyme CYP2R1 catalyzes C-25 hydroxylation of vitamin D3 to an active vitamin D receptor ligand in the liver and other organs
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
calciol i.e. cholecalciferol i.e. vitamin D3. Calcidiol i.e. 25-hydroxyvitamin D3
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
calciol + O2 + [reduced NADPH-hemoprotein reductase]
calcidiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
vitamin D2 + O2 + NADPH + H+
25-hydroxyvitamin D2 + NADP+ + H2O
-
-
-
?
vitamin D2 + O2 + NADPH + H+
25-hydroxyvitamin D2 + NADP+ + H2O
-
-
-
?
vitamin D2 + O2 + NADPH + H+
25-hydroxyvitamin D2 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
1alpha, 25-dihydroxy-vitamin D3 + NADP+ + H2O
-
major products are 25-hydroxy-vitamin D3 and 1alpha, 25-dihydroxy-vitamin D3, plus minor amounts of 26-hydroxy-vitamin D3
-
?
vitamin D3 + O2 + NADPH + H+
1alpha, 25-dihydroxy-vitamin D3 + NADP+ + H2O
-
major products are 25-hydroxy-vitamin D3 and 1alpha, 25-dihydroxy-vitamin D3, plus minor amounts of 26-hydroxy-vitamin D3
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxy-vitamin D3 + NADP+ + H2O
-
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxy-vitamin D3 + NADP+ + H2O
-
major products are 25-hydroxy-vitamin D3 and 1alpha, 25-dihydroxy-vitamin D3, plus minor amounts of 26-hydroxy-vitamin D3. Data indicate that Vdh first hydroxylates the C-25 position of vitamion D3 and subsequently hydroxylates the C1alpha position of 25-hydroxy-vitamin D3
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxy-vitamin D3 + NADP+ + H2O
-
major products are 25-hydroxy-vitamin D3 and 1alpha, 25-dihydroxy-vitamin D3, plus minor amounts of 26-hydroxy-vitamin D3. Data indicate that Vdh first hydroxylates the C-25 position of vitamion D3 and subsequently hydroxylates the C1alpha position of 25-hydroxy-vitamin D3
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
-
-
?
vitamin D3 + O2 + NADPH + H+
25-hydroxyvitamin D3 + NADP+ + H2O
-
-
plus some 26-hydroxyvitamin D3
-
?
additional information
?
-
-
CYP2R1 shows no detectable 1alpha-hydroxylation activity
-
-
?
additional information
?
-
no substrates: 25-hydroxyvitamin D3, cholesterol, 7-dehydrocholesterol
-
-
?
additional information
?
-
no substrate: testosterone
-
-
?
additional information
?
-
-
no substrates: benzphetamine, 7-ethoxycoumarin, and benzo[a]pyrene
-
-
?
additional information
?
-
the descending order of 25-hydroxylation by CYP2C11 is 1-hydroxyvitamin D3, 1-hydroxyvitamin D2, vitamin D, vitamin D3. 24-Hydroxylation of 1alpha-hydroxyvitamin D3 is very low and does not occur with 1-alpha-hydroxyvitamin D2
-
-
?
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malfunction
compared with noncarriers, carriers of 4 risk alleles of rs10741657 have lowest concentrations and smallest increases in 25-hydroxy-vitamin D concentrations after 4 UVB treatments and largest decreases in 25-hydroxy-vitamin D concentrations after 6-months of consumption of vitamin D3fortified bread and milk. Common genetic variants rs10741657 and rs10766197 in vitamin D25-hydroxylase (CYP2R1) predict 25-hydroxy-vitamin D concentrations
malfunction
enzyme-deficient Cyp2r1-/- mice show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
malfunction
-
enzyme-deficient Cyp2r1-/- mice show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
-
metabolism
the cross talk from the bone to the testis of the vitamin D 25-hydroxylase CYP2R1 involves osteocalcin, which is produced by the osteoblasts and stimulates the production of testosterone by the Leydig cells through its putative receptor GPRC6A, a cation-sensing G-protein-coupled receptor. Action of osteocalcin on CYP2R1 expression and 25-hydroxyvitamin D production in a mouse Leydig cell line MA-10
metabolism
the microsomal enzyme CYP2R1 catalyzes C-25 hydroxylation of vitamin D3 to an active vitamin D receptor ligand in the liver and other organs
physiological function
expression of CYP2R1 in HEK 293 cells leads to the transcriptional activation of the vitamin D receptor when either vitamin D2 or D3 is added to the medium. Co-expression of CYP2R1 with vitamin D 1-hydroxylase CYP27B1 elicits additive activation of vitamin D3, whereas co-expression with vitamin D 24-hydroxylase CYP24A1 causes inactivation
physiological function
in male rats, hypophysectomy reduces body weight by 40% and liver weight by 50%. 25-Hydroxylase activity is reduced by 64%, 24-hydroxylase activity is reduced by 52%, and hepatic microsomal CYP2C11 mRNA is decreased by 73% compared with the values of sham-operated animals
physiological function
-
the absence of either of the two key hydroxylases, i.e., 25-hydroxylase and 1alpha-hydroxylase, neither inhibits nor enhances the development of experimental autoimmune encephalomyelitis in a mice model
physiological function
CYP2R1 is a major, but not exclusive, contributor to 25-hydroxyvitamin D production in vivo. A second enzyme is another contributor to this important step in vitamin D activation
physiological function
CYP2R1 is a physiologically important vitamin D 25-hydroxylase. Vitamin D3 is initially converted to 25(OH)D3 in the liver, and then 25(OH)D 3 is converted to a functionally active form, namely 1alpha,25(OH)2D3, in the kidney. 1alpha,25(OH)2D3 plays essential roles in calcium and phosphate homeostasis, cell differentiation and immunology. Metabolic activation of vitamin D3 is performed by the hepatic vitamin D3 25-hydroxylase microsomal CYP2R1, and mitochondrial 1alpha-hydroxylase CYP27A1
physiological function
the microsomal vitamin D 25-hydroxylase plays an important role in converting dietary vitamin D to active metabolite, 25-(OH)D3. 1,25(OH)2D3 regulates CYP2R1 gene expression in oral squamous cell carcinoma tumor cells
physiological function
-
CYP2R1 is a major, but not exclusive, contributor to 25-hydroxyvitamin D production in vivo. A second enzyme is another contributor to this important step in vitamin D activation
-
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A326G
about 90% loss of activity with all substrates tested
L99P
-
mutation identified in a patient with low circulating levels of 25-hydroxyvitamin D and classic symptoms of vitamin D deficiency. This individual is homozygous for a transition mutation in exon 2 of the CYP2R1 gene on chromosome 11p15.2, leading to the substitution of a proline for an evolutionarily conserved leucine and eliminating vitamin D 25-hydroxylase enzyme activity
V391L
mutation converts the enzyme from a catabolic 1alpha,25-dihydroxyvitamin D3-24-hydroxylase into an anabolic 1alpha-hydroxy-vitamin-D3-25-hydroxylase, which forms the hormone, 1alpha,25-dihydroxyvitamin D3. Mutant enzyme retains its basal ability to catabolize 1alpha,25-dihydroxyvitamin D3 via C24 hydroxylation, and can also produce calcitroic acid
V391L/A326G
mutant enzyme continues to form 1alpha,25-dihydroxyvitamin D3 from 1alpha-hydroxyvitamin D3, but this initial product is diverted via the C23 hydroxylation pathway into the 26,23-lactone. About 40-60% of wild-type activity
E216A
2- to 3fold increase in hydroxylase activity
E384R
2- to 3fold increase in hydroxylase activity
T70R
2- to 3fold increase in hydroxylase activity
T70R/V156L/E216M/E384R
21fold increase in hydroxylase activity
T70R/V156S/E216A/E384R
7.9fold increase in hydroxylase activity
V156S
2- to 3fold increase in hydroxylase activity
E216A
-
2- to 3fold increase in hydroxylase activity
-
E384R
-
2- to 3fold increase in hydroxylase activity
-
T70R
-
2- to 3fold increase in hydroxylase activity
-
T70R/V156L/E216M/E384R
-
21fold increase in hydroxylase activity
-
V156S
-
2- to 3fold increase in hydroxylase activity
-
A241G/L243V/F244L/P245R/R246F
-
mutation in substrate recognition site 3, to the equivalent residues in CYP2D6, an enzyme not active in 25-hydroxylation. The 25-hydroxylase activity of the mutant is completely lost whereas the activity toward tolterodine remains virtually unaffected
additional information
construction of null mutant enzyme-deficient Cyp2r1-/- mice, that show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
additional information
-
construction of null mutant enzyme-deficient Cyp2r1-/- mice, that show greater than 50% reduction in serum 25-hydroxyvitamin D3 level, while the 1alpha,25-dihydroxyvitamin D3 level in the serum remains unchanged. A double knockout of Cyp2r1 and Cyp27a1, the enzyme responsible for the 1alpha-hydroxylation step, maintain a similar circulating level of 25-hydroxyvitamin D3 and 1alpha,25-dihydroxyvitamin D3
-
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Rahmaniyan, M.; Patrick, K.; Bell, N.H.
Characterization of recombinant CYP2C11: a vitamin D 25-hydroxylase and 24-hydroxylase
Am. J. Physiol. Endocrinol. Metab.
288
E753-E760
2005
Rattus norvegicus (P08683)
brenda
Postlind, H.; Axen, E.; Bergman, T.; Wikvall, K.
Cloning, structure, and expression of a cDNA encoding vitamin D3 25-hydroxylase
Biochem. Biophys. Res. Commun.
241
491-497
1997
Sus scrofa
brenda
Hosseinpour, F.; Hidestrand, M.; Ingelman-Sundberg, M.; Wikvall, K.
The importance of residues in substrate recognition site 3 for the catalytic function of CYP2D25 (vitamin D 25-hydroxylase)
Biochem. Biophys. Res. Commun.
288
1059-1063
2001
Sus scrofa
brenda
Shinkyo, R.; Sakaki, T.; Kamakura, M.; Ohta, M.; Inouye, K.
Metabolism of vitamin D by human microsomal CYP2R1
Biochem. Biophys. Res. Commun.
324
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2004
Homo sapiens
brenda
Fujii, Y.; Kabumoto, H.; Nishimura, K.; Fujii, T.; Yanai, S.; Takeda, K.; Tamura, N.; Arisawa, A.; Tamura, T.
Purification, characterization, and directed evolution study of a vitamin D3 hydroxylase from Pseudonocardia autotrophica
Biochem. Biophys. Res. Commun.
385
170-175
2009
Pseudonocardia autotrophica (C4B644), Pseudonocardia autotrophica NBRC 12743 (C4B644)
brenda
Saarem, K.; Pedersen, J.I.
25-Hydroxylation of 1 alpha-hydroxyvitamin D-3 in rat and human liver
Biochim. Biophys. Acta
840
117-126
1985
Rattus norvegicus
brenda
Axen, E.
Purification from pig kidney of a microsomal cytochrome P450 catalyzing 1 alpha-hydroxylation of 25-hydroxyvitamin D3
FEBS Lett.
375
277-279
1995
Sus scrofa
brenda
Masumoto, O.; Ohyama, Y.; Okuda, K.
Purification and characterization of vitamin D 25-hydroxylase from rat liver mitochondria
J. Biol. Chem.
263
14256-14260
1988
Rattus norvegicus
brenda
Cheng, J.B.; Motola, D.L.; Mangelsdorf, D.J.; Russell, D.W.
De-orphanization of cytochrome P450 2R1: a microsomal vitamin D 25-hydroxilase
J. Biol. Chem.
278
38084-38093
2003
Mus musculus (Q6VVW9)
brenda
Yamasaki, T.; Izumi, S.; Ide, H.; Ohyama, Y.
Identification of a novel rat microsomal vitamin D3 25-hydroxylase
J. Biol. Chem.
279
22848-22856
2004
Rattus norvegicus (P51590)
brenda
Kaufmann, M.; Prosser, D.E.; Jones, G.
Bioengineering anabolic vitamin D-25-hydroxylase activity into the human vitamin D catabolic enzyme, cytochrome P450 CYP24A1, by a V391L mutation
J. Biol. Chem.
286
28729-28737
2011
Homo sapiens (Q07973), Homo sapiens
brenda
Strushkevich, N.; Usanov, S.A.; Plotnikov, A.N.; Jones, G.; Park, H.W.
Structural analysis of CYP2R1 in complex with vitamin D3
J. Mol. Biol.
380
95-106
2008
Homo sapiens (Q6VVX0)
brenda
Cheng, J.B.; Levine, M.A.; Bell, N.H.; Mangelsdorf, D.J.; Russell, D.W.
Genetic evidence that the human CYP2R1 enzyme is a key vitamin D 25-hydroxylase
Proc. Natl. Acad. Sci. USA
101
7711-7715
2004
Homo sapiens
brenda
Wang, Y.; Marling, S.J.; Zhu, J.G.; Severson, K.S.; DeLuca, H.F.
Development of experimental autoimmune encephalomyelitis (EAE) in mice requires vitamin D and the vitamin D receptor
Proc. Natl. Acad. Sci. USA
109
8501-8504
2012
Mus musculus
brenda
Aiba, I.; Yamasaki, T.; Shinki, T.; Izumi, S.; Yamamoto, K.; Yamada, S.; Terato, H.; Ide, H.; Ohyama, Y.
Characterization of rat and human CYP2J enzymes as Vitamin D 25-hydroxylases
Steroids
71
849-856
2006
Homo sapiens (P51589), Homo sapiens, Rattus norvegicus (P51590)
brenda
Urbschat, A.; Paulus, P.; von Quernheim, Q.F.; Brueck, P.; Badenhoop, K.; Zeuzem, S.; Ramos-Lopez, E.
Vitamin D hydroxylases CYP2R1, CYP27B1 and CYP24A1 in renal cell carcinoma
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43
1282-1290
2013
Homo sapiens (Q6VVX0)
brenda
Foresta, C.; Strapazzon, G.; De Toni, L.; Perilli, L.; Di Mambro, A.; Muciaccia, B.; Sartori, L.; Selice, R.
Bone mineral density and testicular failure: evidence for a role of vitamin D 25-hydroxylase in human testis
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96
E646-E652
2011
Homo sapiens (Q6VVX0), Homo sapiens
brenda
Nissen, J.; Vogel, U.; Ravn-Haren, G.; Andersen, E.W.; Madsen, K.H.; Nex?, B.A.; Andersen, R.; Mejborn, H.; Bjerrum, P.J.; Rasmussen, L.B.; Wulf, H.C.
Common variants in CYP2R1 and GC genes are both determinants of serum 25-hydroxyvitamin D concentrations after UVB irradiation and after consumption of vitamin D3-fortified bread and milk during winter in Denmark
Am. J. Clin. Nutr.
101
218-227
2015
Homo sapiens (Q6VVX0)
brenda
Yasuda, K.; Endo, M.; Ikushiro, S.; Kamakura, M.; Ohta, M.; Sakaki, T.
UV-dependent production of 25-hydroxyvitamin D2 in the recombinant yeast cells expressing human CYP2R1
Biochem. Biophys. Res. Commun.
434
311-315
2013
Homo sapiens (Q6VVX0), Homo sapiens
brenda
De Toni, L.; De Filippis, V.; Tescari, S.; Ferigo, M.; Ferlin, A.; Scattolini, V.; Avogaro, A.; Vettor, R.; Foresta, C.
Uncarboxylated osteocalcin stimulates 25-hydroxy vitamin D production in Leydig cell line through a GPRC6a-dependent pathway
Endocrinology
155
4266-4274
2014
Mus musculus (Q6VVW9), Mus musculus
brenda
Sundaram, K.; Sambandam, Y.; Tsuruga, E.; Wagner, C.L.; Reddy, S.V.
1alpha,25-dihydroxyvitamin D3 modulates CYP2R1 gene expression in human oral squamous cell carcinoma tumor cells
Horm. Cancer
5
90-97
2014
Homo sapiens (Q6VVX0), Homo sapiens
brenda
Zhu, J.G.; Ochalek, J.T.; Kaufmann, M.; Jones, G.; Deluca, H.F.
CYP2R1 is a major, but not exclusive, contributor to 25-hydroxyvitamin D production in vivo
Proc. Natl. Acad. Sci. USA
110
15650-15655
2013
Mus musculus (Q6VVW9), Mus musculus C57BL/6 (Q6VVW9)
brenda
Ahn, J.; Yu, K.; Stolzenberg-Solomon, R.; Simon, K.C.; McCullough, M.L.; Gallicchio, L.; Jacobs, E.J.; Ascherio, A.; Helzlsouer, K.; Jacobs, K.B.; Li, Q.; Weinstein, S.J.; Purdue, M.; Virtamo, J.; Horst, R.; Wheeler, W.; Chanock, S.; Hunter, D.J.; Hayes, R.B.; Kraft, P.; Albanes, D.
Genome-wide association study of circulating vitamin D levels
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19
2739-2745
2010
Homo sapiens (Q6VVX0), Homo sapiens
brenda