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Human Metabolome Database Version 2.5

 

Showing metabocard for Vitamin D3 (HMDB00876)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:19
Accession Number HMDB00876
Secondary Accession Numbers Not Available
Common Name Vitamin D3
Description Vitamin D3 is a steroid hormone that has long been known for its important role in regulating body levels of calcium and phosphorus, in mineralization of bone, and for the assimilation of Vitamin A. It is structurally similar to steroids such as testosterone, cholesterol, and cortisol (though vitamin D3 itself is a secosteroid).
Synonyms
  1. (+)-Vitamin D3
  2. (3beta,Z,7E)-9,10-Secocholesta-5,7,10(19)-trien-3-ol
  3. (5E,7E)-9,10-Secocholesta-5,7,10-trien-3-ol
  4. 3-beta,Z,7E-9,10-Secocholestr-5,7,10(19)-trien-3-ol
  5. 9,10-Secocholesta-5,7,10(19)-trien-3-beta-ol
  6. 9,10-Secocholesta-5,7,10(19)-trien-3-ol
  7. 9,10-secocholesta-5,7,10-trien-3-ol
  8. Arachitol
  9. CC
  10. Calciol
  11. Cholecalciferol
  12. Cholecalciferol D3
  13. Colecalciferol
  14. D3-Vigantol
  15. Delsterol
  16. Deparal
  17. Devaron
  18. Ebivit
  19. FeraCol
  20. Granuvit D3
  21. Micro-dee
  22. Oleovitamin D3
  23. Provitina
  24. Quintox
  25. Ricketon
  26. Trivitan
  27. Vi-De3
  28. VidDe-3-hydrosol
  29. Videkhol
  30. Vigantol
  31. Vigorsan
  32. Vitinc Dan-Dee-3
Chemical IUPAC Name 3-[2-[7a-methyl-1-(6-methylheptan-2-yl)-2,3,3a,5,6,7-hexahydro-1H-inden-4-ylidene]ethylidene]-4-methylidene-cyclohexan-1-ol
Chemical Formula C27H44O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Vitamin D3 derivatives
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
  • Essential vitamins
Application
Source
  • Exogenous
Average Molecular Weight 384.638
Monoisotopic Molecular Weight 384.339203
Isomeric SMILES CC(C)CCC[C@@H](C)[C@H]1CCC2[C@]1(C)CCCC2=C/C=C1/C[C@@H](O)CCC1=C
Canonical SMILES CC(C)CCCC(C)C1CCC2C1(C)CCCC2=CC=C1CC(O)CCC1=C
KEGG Compound ID C05443 Link Image
BioCyc ID VITAMIN_D_%7B3%7D Link Image
BiGG ID 2288999 Link Image
Wikipedia Link Vitamin D3 Link Image
NuGOwiki Link HMDB00876 Link Image
Metagene Link HMDB00876 Link Image
METLIN ID 222 Link Image
PubChem Compound 2735 Link Image
PubChem Substance 7767974 Link Image
ChEBI ID 28940 Link Image
CAS Registry Number 67-97-0
InChI Identifier InChI=1/C27H44O/c1-19(2)8-6-9-21(4)25-15-16-26-22(10-7-17-27(25,26)5)12-13-23-18-24(28)14-11-20(23)3/h12-13,19,21,24-26,28H,3,6-11,14-18H2,1-2,4-5H3/b22-12+,23-13-/t21-,24+,25-,26?,27-/m1/s1
Synthesis Reference Nemoto, Hideo; Kurobe, Hiroshi; Fukumoto, Keiichiro; Kametani, Tetsuji. A modified synthesis of the (+)-8a-phenylsulfonyl-des-AB-cholestane via an intramolecular nucleophilic attack to epoxide - a total synthesis of vitamin D3. Heterocycles (1985), 23(3),
Melting Point (Experimental) 84.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.31e-08 mg/mL [MEYLAN,WM et al. (1996)]; 3.80e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.98 [Predicted by ALOGPS]; 7.5 [Predicted by PubChem via XLOGP]; 10.24 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
Tissue Location
Tissue References
Fibroblasts
Gonads
Intestine
Keratinocyte
Kidney
Liver
Liver Parathyroid Gland
Placenta
Prostate
Skin
Spleen
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 0.0060 +/- 0.0042 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shepard RM, Horst RL, Hamstra AJ, DeLuca HF: Determination of vitamin D and its metabolites in plasma from normal and anephric man. Biochem J. 1979 Jul 15;182(1):55-69. [PubMed Link Image]
Biofluid Blood
Value 0.0681 +/- 0.01880 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal with high exposure to sun
Comments Not Available
References
  • Shepard RM, Horst RL, Hamstra AJ, DeLuca HF: Determination of vitamin D and its metabolites in plasma from normal and anephric man. Biochem J. 1979 Jul 15;182(1):55-69. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.0037 +/- 0.0016 uM
Age Adult:>18 yrs old
Sex Both
Condition Anephric patients
Comments Not Available
References
  • Shepard RM, Horst RL, Hamstra AJ, DeLuca HF: Determination of vitamin D and its metabolites in plasma from normal and anephric man. Biochem J. 1979 Jul 15;182(1):55-69. [PubMed Link Image]
Associated Disorders
Condition References
Anephric patients
  • Shepard RM, Horst RL, Hamstra AJ, DeLuca HF: Determination of vitamin D and its metabolites in plasma from normal and anephric man. Biochem J. 1979 Jul 15;182(1):55-69. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Rautureau M, Rambaud JC: Aqueous solubilisation of vitamin D3 in normal man. Gut. 1981 May;22(5):393-7. [PubMed Link Image]
  2. Shepard RM, Horst RL, Hamstra AJ, DeLuca HF: Determination of vitamin D and its metabolites in plasma from normal and anephric man. Biochem J. 1979 Jul 15;182(1):55-69. [PubMed Link Image]
  3. Osborne JE, Hutchinson PE: Vitamin D and systemic cancer: is this relevant to malignant melanoma? Br J Dermatol. 2002 Aug;147(2):197-213. [PubMed Link Image]
  4. Haddad JG, Jennings AS, Aw TC: Vitamin D uptake and metabolism by perfused rat liver: influences of carrier proteins. Endocrinology. 1988 Jul;123(1):498-504. [PubMed Link Image]
  5. Kida K, Goodman DS: Studies on the transport of vitamin D and of 25-hydroxyvitamin D in human plasma. J Lipid Res. 1976 Sep;17(5):485-90. [PubMed Link Image]
  6. Flanagan JN, Young MV, Persons KS, Wang L, Mathieu JS, Whitlatch LW, Holick MF, Chen TC: Vitamin D metabolism in human prostate cells: implications for prostate cancer chemoprevention by vitamin D. Anticancer Res. 2006 Jul-Aug;26(4A):2567-72. [PubMed Link Image]
  7. Lips P: Vitamin D deficiency and secondary hyperparathyroidism in the elderly: consequences for bone loss and fractures and therapeutic implications. Endocr Rev. 2001 Aug;22(4):477-501. [PubMed Link Image]
  8. Svendsen ML, Daneels G, Geysen J, Binderup L, Kragballe K: Proliferation and differentiation of cultured human keratinocytes is modulated by 1,25(OH)2D3 and synthetic vitamin D3 analogues in a cell density-, calcium- and serum-dependent manner. Pharmacol Toxicol. 1997 Jan;80(1):49-56. [PubMed Link Image]
  9. Yetgin S, Yalcin SS: The effect of vitamin D3 on CD34 progenitor cells in vitamin D deficiency rickets. Turk J Pediatr. 2004 Apr-Jun;46(2):164-6. [PubMed Link Image]
  10. Astecker N, Reddy GS, Herzig G, Vorisek G, Schuster I: 1alpha,25-Dihydroxy-3-epi-vitamin D3 a physiological metabolite of 1alpha,25-dihydroxyvitamin D3: its production and metabolism in primary human keratinocytes. Mol Cell Endocrinol. 2000 Dec 22;170(1-2):91-101. [PubMed Link Image]
  11. Murao N, Ohishi N, Nabuchi Y, Ishigai M, Kawanishi T, Aso Y: The determination of 2beta-(3-hydroxypropoxy)-1alpha,25-dihydroxy vitamin D3 (ED-71) in human serum by high-performance liquid chromatography-electrospray tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Sep 5;823(2):61-8. Epub 2004 Nov 19. [PubMed Link Image]
  12. Lippens S, Kockx M, Denecker G, Knaapen M, Verheyen A, Christiaen R, Tschachler E, Vandenabeele P, Declercq W: Vitamin D3 induces caspase-14 expression in psoriatic lesions and enhances caspase-14 processing in organotypic skin cultures. Am J Pathol. 2004 Sep;165(3):833-41. [PubMed Link Image]
  13. Bjorkhem I, Holmberg I, Kristiansen T, Pedersen JI: Assay of 1,25-dihydroxy vitamin D3 by isotope dilution--mass fragmentography. Clin Chem. 1979 Apr;25(4):584-8. [PubMed Link Image]
  14. Matsuoka LY, McConnachie P, Wortsman J, Holick MF: Immunological responses to ultraviolet light B radiation in Black individuals. Life Sci. 1999;64(17):1563-9. [PubMed Link Image]
  15. Zimber A, Chedeville A, Abita JP, Barbu V, Gespach C: Functional interactions between bile acids, all-trans retinoic acid, and 1,25-dihydroxy-vitamin D3 on monocytic differentiation and myeloblastin gene down-regulation in HL60 and THP-1 human leukemia cells. Cancer Res. 2000 Feb 1;60(3):672-8. [PubMed Link Image]
  16. Baggio B, Budakovic A, Nassuato MA, Vezzoli G, Manzato E, Luisetto G, Zaninotto M: Plasma phospholipid arachidonic acid content and calcium metabolism in idiopathic calcium nephrolithiasis. Kidney Int. 2000 Sep;58(3):1278-84. [PubMed Link Image]
  17. MacLaughlin J, Holick MF: Aging decreases the capacity of human skin to produce vitamin D3. J Clin Invest. 1985 Oct;76(4):1536-8. [PubMed Link Image]
  18. Lee YF, Young WJ, Lin WJ, Shyr CR, Chang C: Differential regulation of direct repeat 3 vitamin D3 and direct repeat 4 thyroid hormone signaling pathways by the human TR4 orphan receptor. J Biol Chem. 1999 Jun 4;274(23):16198-205. [PubMed Link Image]
  19. Okano T, Kuroda E, Nakao H, Kodama S, Matsuo T, Nakamichi Y, Nakajima K, Hirao N, Kobayashi T: Lack of evidence for existence of vitamin D and 25-hydroxyvitamin D sulfates in human breast and cow's milk. J Nutr Sci Vitaminol (Tokyo). 1986 Oct;32(5):449-62. [PubMed Link Image]
  20. Mata-Granados JM, Caballo-Lopez A, Luque de Castro MD, Quesada JM: Automated method for the determination of vitamin D3 hydroxymetabolites in serum. Anal Bioanal Chem. 2003 Sep;377(2):287-92. Epub 2003 Jul 9. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Nuclear receptor coactivator 3
  2. Sterol 26-hydroxylase, mitochondrial
  3. 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
  4. Vitamin D3 receptor
  5. 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
  6. Vitamin D 25-hydroxylase
  7. Transcription initiation factor TFIID subunit 4
  8. Nuclear receptor coactivator 6
  9. cDNA FLJ51539, highly similar to Vitamin D3 receptor
Enzyme 1 [top]
Enzyme 1 ID 5255
Enzyme 1 Name Nuclear receptor coactivator 3
Enzyme 1 Synonyms
  1. NCoA-3
  2. ACTR
  3. Amplified in breast cancer 1 protein
  4. AIB-1
  5. CBP-interacting protein
  6. pCIP
  7. Class E basic helix-loop-helix protein 42
  8. bHLHe42
  9. Receptor-associated coactivator 3
  10. RAC-3
  11. Steroid receptor coactivator protein 3
  12. SRC-3
  13. Thyroid hormone receptor activator molecule 1
  14. TRAM-1
Enzyme 1 Gene Name NCOA3
Enzyme 1 Protein Sequence >Nuclear receptor coactivator 3
MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDID
NFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQA
LDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNG
VSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGE
DLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRC
IQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDR
HGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLA
DPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNI
MISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLST
LSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKE
SSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVS
SSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGN
VVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQE
KDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLK
SSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGS
SMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPT
LPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQV
SHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPE
LVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMN
QMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTA
GGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQ
QQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQ
PDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQ
FAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC
Enzyme 1 Number of Residues 1424
Enzyme 1 Molecular Weight 155292.5
Enzyme 1 Theoretical pI 7.51
Enzyme 1 GO Classification
Function
  • binding
  • hormone receptor binding
  • molecular transducer activity
  • nuclear hormone receptor binding
  • protein binding
  • receptor binding
  • signal transducer activity
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transcription regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 1 General Function Involved in transcription coactivator activity
Enzyme 1 Specific Function Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit. Interacts with PSMB9
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 32307126 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9Y6Q9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name NCOA3_HUMAN Link Image
Enzyme 1 PDB ID 1KBH Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >4275 bp
ATGAGTGGATTAGGAGAAAACTTGGATCCACTGGCCAGTGATTCACGAAAACGCAAATTG
CCATGTGATACTCCAGGACAAGGTCTTACCTGCAGTGGTGAAAAACGGAGACGGGAGCAG
GAAAGTAAATATATTGAAGAATTGGCTGAGCTGATATCTGCCAATCTTAGTGATATTGAC
AATTTCAATGTCAAACCAGATAAATGTGCGATTTTAAAGGAAACAGTAAGACAGATACGT
CAAATAAAAGAGCAAGGAAAAACTATTTCCAATGATGATGATGTTCAAAAAGCCGATGTA
TCTTCTACAGGGCAGGGAGTTATTGATAAAGACTCCTTAGGACCGCTTTTACTTCAGGCA
TTGGATGGTTTCCTATTTGTGGTGAATCGAGACGGAAACATTGTATTTGTATCAGAAAAT
GTCACACAATACCTGCAATATAAGCAAGAGGACCTGGTTAACACAAGTGTTTACAATATC
TTACATGAAGAAGACAGAAAGGATTTTCTTAAGAATTTACCAAAATCTACAGTTAATGGA
GTTTCCTGGACAAATGAGACCCAAAGACAAAAAAGCCATACATTTAATTGCCGTATGTTG
ATGAAAACACCACATGATATTCTGGAAGACATAAACGCCAGTCCTGAAATGCGCCAGAGA
TATGAAACAATGCAGTGCTTTGCCCTGTCTCAGCCACGAGCTATGATGGAGGAAGGGGAA
GATTTGCAATCTTGTATGATCTGTGTGGCACGCCGCATTACTACAGGAGAAAGAACATTT
CCATCAAACCCTGAGAGCTTTATTACCAGACATGATCTTTCAGGAAAGGTTGTCAATATA
GATACAAATTCACTGAGATCCTCCATGAGGCCTGGCTTTGAAGATATAATCCGAAGGTGT
ATTCAGAGATTTTTTAGTCTAAATGATGGGCAGTCATGGTCCCAGAAACGTCACTATCAA
GAAGCTTATCTTAATGGCCATGCAGAAACCCCAGTATATCGATTCTCGTTGGCTGATGGA
ACTATAGTGACTGCACAGACAAAAAGCAAACTCTTCCGAAATCCTGTAACAAATGATCGA
CATGGCTTTGTCTCAACCCACTTCCTTCAGAGAGAACAGAATGGATATAGACCAAACCCA
AATCCTGTTGGACAAGGGATTAGACCACCTATGGCTGGATGCAACAGTTCGGTAGGCGGC
ATGAGTATGTCGCCAAACCAAGGCTTACAGATGCCGAGCAGCAGGGCCTATGGCTTGGCA
GACCCTAGCACCACAGGGCAGATGAGTGGAGCTAGGTATGGGGGTTCCAGTAACATAGCT
TCATTGACCCCTGGGCCAGGCATGCAATCACCATCTTCCTACCAGAACAACAACTATGGG
CTCAACATGAGTAGCCCCCCACATGGGAGTCCTGGTCTTGCCCCAAACCAGCAGAATATC
ATGATTTCTCCTCGTAATCGTGGGAGTCCAAAGATAGCCTCACATCAGTTTTCTCCTGTT
GCAGGTGTGCACTCTCCCATGGCATCTTCTGGCAATACTGGGAACCACAGCTTTTCCAGC
AGCTCTCTCAGTGCCCTGCAAGCCATCAGTGAAGGTGTGGGGACTTCCCTTTTATCTACT
CTGTCATCACCAGGCCCCAAATTGGATAACTCTCCCAATATGAATATTACCCAACCAAGT
AAAGTAAGCAATCAGGATTCCAAGAGTCCTCTGGGCTTTTATTGCGACCAAAATCCAGTG
GAGAGTTCAATGTGTCAGTCAAATAGCAGAGATCACCTCAGTGACAAAGAAAGTAAGGAG
AGCAGTGTTGAGGGGGCAGAGAATCAAAGGGGTCCTTTGGAAAGCAAAGGTCATAAAAAA
TTACTGCAGTTACTTACCTGTTCTTCTGATGACCGGGGTCATTCCTCCTTGACCAACTCC
CCCCTAGATTCAAGTTGTAAAGAATCTTCTGTTAGTGTCACCAGCCCCTCTGGAGTCTCC
TCCTCTACATCTGGAGGAGTATCCTCTACATCCAATATGCATGGGTCACTGTTACAAGAG
AAGCACCGGATTTTGCACAAGTTGCTGCAGAATGGGAATTCACCAGCTGAGGTAGCCAAG
ATTACTGCAGAAGCCACTGGGAAAGACACCAGCAGTATAACTTCTTGTGGGGACGGAAAT
GTTGTCAAGCAGGAGCAGCTAAGTCCTAAGAAGAAGGAGAATAATGCACTTCTTAGATAC
CTGCTGGACAGGGATGATCCTAGTGATGCACTCTCTAAAGAACTACAGCCCCAAGTGGAA
GGAGTGGATAATAAAATGAGTCAGTGCACCAGCTCCACCATTCCTAGCTCAAGTCAAGAG
AAAGACCCTAAAATTAAGACAGAGACAAGTGAAGAGGGATCTGGAGACTTGGATAATCTA
GATGCTATTCTTGGTGATCTGACTAGTTCTGACTTTTACAATAATTCCATATCCTCAAAT
GGTAGTCATCTGGGGACTAAGCAACAGGTGTTTCAAGGAACTAATTCTCTGGGTTTGAAA
AGTTCACAGTCTGTGCAGTCTATTCGTCCTCCATATAACCGAGCAGTGTCTCTGGATAGC
CCTGTTTCTGTTGGCTCAAGTCCTCCAGTAAAAAATATCAGTGCTTTCCCCATGTTACCA
AAGCAACCCATGTTGGGTGGGAATCCAAGAATGATGGATAGTCAGGAAAATTATGGCTCA
AGTATGGGTGGGCCAAACCGAAATGTGACTGTGACTCAGACTCCTTCCTCAGGAGACTGG
GGCTTACCAAACTCAAAGGCCGGCAGAATGGAACCTATGAATTCAAACTCCATGGGAAGA
CCAGGAGGAGATTATAATACTTCTTTACCCAGACCTGCACTGGGTGGCTCTATTCCCACA
TTGCCTCTTCGGTCTAATAGCATACCAGGTGCGAGACCAGTATTGCAACAGCAGCAGCAG
ATGCTTCAAATGAGGCCTGGTGAAATCCCCATGGGAATGGGGGCTAATCCCTATGGCCAA
GCAGCAGCATCTAACCAACTGGGTTCCTGGCCCGATGGCATGTTGTCCATGGAACAAGTT
TCTCATGGCACTCAAAATAGGCCTCTTCTTAGGAATTCCCTGGATGATCTTGTTGGGCCA
CCTTCCAACCTGGAAGGCCAGAGTGACGAAAGAGCATTATTGGACCAGCTGCACACTCTT
CTCAGCAACACAGATGCCACAGGCCTGGAAGAAATTGACAGAGCTTTGGGCATTCCTGAA
CTTGTCAATCAGGGACAGGCATTAGAGCCCAAACAGGATGCTTTCCAAGGCCAAGAAGCA
GCAGTAATGATGGATCAGAAGGCAGGATTATATGGACAGACATACCCAGCACAGGGGCCT
CCAATGCAAGGAGGCTTTCATCTTCAGGGACAATCACCATCTTTTAACTCTATGATGAAT
CAGATGAACCAGCAAGGCAATTTTCCTCTCCAAGGAATGCACCCACGAGCCAACATCATG
AGACCCCGGACAAACACCCCCAAGCAACTTAGAATGCAGCTTCAGCAGAGGCTGCAGGGC
CAGCAGTTTTTGAATCAGAGCCGACAGGCACTTGAATTGAAAATGGAAAACCCTACTGCT
GGTGGTGCTGCGGTGATGAGGCCTATGATGCAGCCCCAGGTGAGCTCCCAGCAGGGTTTT
CTTAATGCTCAAATGGTCGCCCAACGCAGCAGAGAGCTGCTAAGTCATCACTTCCGACAA
CAGAGGGTGGCTATGATGATGCAGCAGCAGCAGCAGCAGCAACAGCAGCAGCAGCAGCAG
CAGCAGCAGCAACAGCAACAGCAACAGCAACAGCAGCAACAGCAGCAAACCCAGGCCTTC
AGCCCACCTCCTAATGTGACTGCTTCCCCCAGCATGGATGGGCTTTTGGCAGGACCCACA
ATGCCACAAGCTCCTCCGCAACAGTTTCCATATCAACCAAATTATGGAATGGGACAACAA
CCAGATCCAGCCTTTGGTCGAGTGTCTAGTCCTCCCAATGCAATGATGTCGTCAAGAATG
GGTCCCTCCCAGAATCCCATGATGCAACACCCGCAGGCTGCATCCATCTATCAGTCCTCA
GAAATGAAGGGCTGGCCATCAGGAAATTTGGCCAGGAACAGCTCCTTTTCCCAGCAGCAG
TTTGCCCACCAGGGGAATCCTGCAGTGTATAGTATGGTGCACATGAATGGCAGCAGTGGT
CACATGGGACAGATGAACATGAACCCCATGCCCATGTCTGGCATGCCTATGGGTCCTGAT
CAGAAATACTGCTGA
Enzyme 1 GenBank Gene ID NM_181659.2 Link Image
Enzyme 1 GeneCard ID NCOA3 Link Image
Enzyme 1 GenAtlas ID NCOA3 Link Image
Enzyme 1 HGNC ID HGNC:7670 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 20q12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [PubMed Link Image]
  2. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed Link Image]
  3. Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS: AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science. 1997 Aug 15;277(5328):965-8. [PubMed Link Image]
  4. Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed Link Image]
  5. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Shirazi SK, Bober MA, Coetzee GA: Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene). Clin Genet. 1998 Jul;54(1):102-3. [PubMed Link Image]
  8. Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell. 1999 Sep 3;98(5):675-86. [PubMed Link Image]
  9. Werbajh S, Nojek I, Lanz R, Costas MA: RAC-3 is a NF-kappa B coactivator. FEBS Lett. 2000 Nov 24;485(2-3):195-9. [PubMed Link Image]
  10. Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Mol Cell Biol. 2002 May;22(10):3549-61. [PubMed Link Image]
  11. Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK: BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. Mol Cell Biol. 2003 Sep;23(17):6210-20. [PubMed Link Image]
  12. Kino T, Ichijo T, Chrousos GP: FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors. J Steroid Biochem Mol Biol. 2004 Dec;92(5):357-63. Epub 2004 Dec 19. [PubMed Link Image]
  13. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  14. Zhang H, Sun L, Liang J, Yu W, Zhang Y, Wang Y, Chen Y, Li R, Sun X, Shang Y: The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 2006 Sep 20;25(18):4223-33. Epub 2006 Sep 7. [PubMed Link Image]
  15. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  16. Zou JX, Revenko AS, Li LB, Gemo AT, Chen HW: ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification. Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):18067-72. Epub 2007 Nov 12. [PubMed Link Image]
  17. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  18. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  19. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  20. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6325
Enzyme 2 Name Sterol 26-hydroxylase, mitochondrial
Enzyme 2 Synonyms
  1. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
  2. Cytochrome P-450C27/25
  3. Cytochrome P450 27
  4. Sterol 27-hydroxylase
  5. Vitamin D(3) 25-hydroxylase
Enzyme 2 Gene Name CYP27A1
Enzyme 2 Protein Sequence >Sterol 26-hydroxylase, mitochondrial
MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEI
PRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQ
EGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNE
VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTF
VRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAA
GPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEA
LHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK
NTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRR
IAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC
Enzyme 2 Number of Residues 531
Enzyme 2 Molecular Weight 60234.3
Enzyme 2 Theoretical pI 9.16
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 2 General Function Involved in monooxygenase activity
Enzyme 2 Specific Function Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta- cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3- 25-hydroxylase activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O [RN:R04807]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q02318 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CP27A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1596 bp
ATGGCTGCGCTGGGCTGCGCGAGGCTGAGGTGGGCGCTGCGAGGGGCCGGCCGTGGCCTC
TGCCCCCACGGGGCCAGAGCCAAGGCCGCGATCCCTGCCGCCCTCCCCTCGGACAAGGCC
ACCGGAGCTCCCGGAGCCGGGCCTGGTGTCCGGCGGCGGCAACGGAGCTTAGAGGAGATT
CCACGTCTAGGACAGCTGCGCTTCTTCTTTCAGCTGTTCGTTCAAGGCTATGCCCTGCAA
CTGCACCAGTTACAGGTGCTTTACAAGGCCAAGTACGGTCCAATGTGGATGTCCTACTTA
GGGCCTCAGATGCACGTGAACCTGGCCAGTGCCCCGCTCTTGGAGCAAGTGATGCGGCAA
GAGGGAAAGTACCCAGTACGGAACGACATGGAGCTATGGAAGGAGCACCGGGACCAGCAC
GACCTGACCTATGGGCCGTTCACCACGGAAGGACACCACTGGTACCAGCTGCGCCAGGCT
CTGAACCAGCGGTTGCTGAAGCCAGCGGAAGCAGCGCTCTATACGGATGCTTTCAATGAG
GTGATTGATGACTTTATGACTCGACTGGACCAGCTGCGGGCAGAGAGTGCTTCGGGGAAC
CAGGTGTCGGACATGGCTCAACTCTTCTACTACTTTGCCTTGGAAGCTATTTGCTACATC
CTGTTCGAGAAACGCATTGGCTGCCTGCAGCGATCCATCCCCGAGGACACCGTGACCTTC
GTCAGATCCATCGGGTTAATGTTCCAGAACTCACTCTATGCCACCTTCCTCCCCAAGTGG
ACTCGCCCCGTGCTGCCTTTCTGGAAGCGATACCTGGATGGTTGGAATGCCATCTTTTCC
TTTGGGAAGAAGCTGATTGATGAGAAGCTCGAAGATATGGAGGCCCAACTGCAGGCAGCA
GGGCCAGATGGCATCCAGGTGTCTGGCTACCTGCACTTCTTACTGGCCAGTGGACAGCTC
AGTCCTCGGGAGGCCATGGGCAGCCTGCCTGAGCTGCTCATGGCTGGAGTGGACACGACA
TCCAACACGCTGACATGGGCCCTGTACCACCTCTCAAAGGACCCTGAGATCCAGGAGGCC
TTGCACGAGGAAGTGGTGGGTGTGGTGCCAGCCGGGCAAGTGCCCCAGCACAAGGACTTT
GCCCACATGCCGTTGCTCAAAGCTGTGCTTAAGGAGACTCTGCGTCTCTACCCTGTGGTC
CCCACAAACTCCCGGATCATAGAAAAGGAAATTGAAGTTGATGGCTTCCTCTTCCCCAAG
AACACCCAGTTTGTGTTCTGCCACTATGTGGTGTCCCGGGACCCCACTGCCTTCTCTGAG
CCTGAAAGCTTCCAGCCCCACCGCTGGCTGAGAAACAGCCAGCCTGCTACCCCCAGGATC
CAGCACCCATTTGGCTCTGTGCCCTTTGGCTATGGGGTCCGGGCCTGCCTGGGCCGCAGG
ATTGCAGAGCTGGAGATGCAGCTACTCCTCGCAAGGCTGATCCAGAAGTACAAGGTGGTC
CTGGCCCCGGAGACGGGGGAGTTGAAGAGTGTGGCCCGCATTGTCCTGGTTCCCAATAAG
AAAGTGGGCCTGCAGTTCCTGCAGAGACAGTGCTGA
Enzyme 2 GenBank Gene ID M62401 Link Image
Enzyme 2 GeneCard ID CYP27A1 Link Image
Enzyme 2 GenAtlas ID CYP27A1 Link Image
Enzyme 2 HGNC ID HGNC:2605 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q33-qter
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Cali JJ, Russell DW: Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem. 1991 Apr 25;266(12):7774-8. [PubMed Link Image]
  2. Guo YD, Strugnell S, Back DW, Jones G: Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8668-72. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Leitersdorf E, Reshef A, Meiner V, Levitzki R, Schwartz SP, Dann EJ, Berkman N, Cali JJ, Klapholz L, Berginer VM: Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin. J Clin Invest. 1993 Jun;91(6):2488-96. [PubMed Link Image]
  6. Cali JJ, Hsieh CL, Francke U, Russell DW: Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. J Biol Chem. 1991 Apr 25;266(12):7779-83. [PubMed Link Image]
  7. Kim KS, Kubota S, Kuriyama M, Fujiyama J, Bjorkhem I, Eggertsen G, Seyama Y: Identification of new mutations in sterol 27-hydroxylase gene in Japanese patients with cerebrotendinous xanthomatosis (CTX). J Lipid Res. 1994 Jun;35(6):1031-9. [PubMed Link Image]
  8. Chen W, Kubota S, Kim KS, Cheng J, Kuriyama M, Eggertsen G, Bjorkhem I, Seyama Y: Novel homozygous and compound heterozygous mutations of sterol 27-hydroxylase gene (CYP27) cause cerebrotendinous xanthomatosis in three Japanese patients from two unrelated families. J Lipid Res. 1997 May;38(5):870-9. [PubMed Link Image]
  9. Chen W, Kubota S, Ujike H, Ishihara T, Seyama Y: A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. Biochemistry. 1998 Oct 27;37(43):15050-6. [PubMed Link Image]
  10. Lamon-Fava S, Schaefer EJ, Garuti R, Salen G, Calandra S: Two novel mutations in the sterol 27-hydroxylase gene causing cerebrotendinous xanthomatosis. Clin Genet. 2002 Mar;61(3):185-91. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6331
Enzyme 3 Name 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Enzyme 3 Synonyms
  1. 25-OHD-1 alpha-hydroxylase
  2. 25-hydroxyvitamin D(3) 1-alpha-hydroxylase
  3. VD3 1A hydroxylase
  4. Calcidiol 1-monooxygenase
  5. Cytochrome P450 subfamily XXVIIB polypeptide 1
  6. Cytochrome P450C1 alpha
  7. Cytochrome P450VD1-alpha
  8. Cytochrome p450 27B1
Enzyme 3 Gene Name CYP27B1
Enzyme 3 Protein Sequence >25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSR
LHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCR
QRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPP
ALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPH
WLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFRE
ELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPS
ATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPA
QFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQP
EPGAAPVRPKTRTVLVPERSINLQFLDR
Enzyme 3 Number of Residues 508
Enzyme 3 Molecular Weight 56503.5
Enzyme 3 Theoretical pI 9.39
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in monooxygenase activity
Enzyme 3 Specific Function Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation
Enzyme 3 Pathways
Enzyme 3 Reactions
  • calcidiol + NADPH + H+ + O2 = calcitriol + NADP+ + H2O [RN:R03610]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID O15528 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CP27B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1527 bp
ATGACCCAGACCCTCAAGTACGCCTCCAGAGTGTTCCATCGCGTCCGCTGGGCGCCCGAG
TTGGGCGCCTCCCTAGGCTACCGAGAGTACCACTCAGCACGCCGGAGCTTGGCAGACATC
CCAGGCCCCTCTACGCCCAGCTTTCTGGCCGAACTTTTCTGCAAGGGGGGGCTGTCGAGG
CTACACGAGCTGCAGGTGCAGGGCGCCGCGCACTTCGGGCCGGTGTGGCTAGCCAGCTTT
GGGACAGTGCGCACCGTGTACGTGGCTGCCCCTGCACTCGTCGAGGAGCTGCTGCGACAG
GAGGGACCCCGGCCCGAGCGCTGCAGCTTCTCGCCCTGGACGGAGCACCGCCGCTGCCGC
CAGCGGGCTTGCGGACTGCTCACTGCGGAAGGCGAAGAATGGCAAAGGCTCCGCAGTCTC
CTGGCCCCGCTCCTCCTCCGGCCTCAAGCGGCCGCCCGCTACGCCGGAACCCTGAACAAC
GTAGTCTGCGACCTTGTGCGGCGTCTGAGGCGCCAGCGGGGACGTGGCACGGGGCCGCCC
GCCCTGGTTCGGGACGTGGCGGGGGAATTTTACAAGTTCGGACTGGAAGGCATCGCCGCG
GTTCTGCTCGGCTCGCGCTTGGGCTGCCTGGAGGCTCAAGTGCCACCCGACACGGAGACC
TTCATCCGCGCTGTGGGCTCGGTGTTTGTGTCCACGCTGTTGACCATGGCGATGCCCCAC
TGGCTGCGCCACCTTGTGCCTGGGCCCTGGGGCCGCCTCTGCCGAGACTGGGACCAGATG
TTTGCATTTGCTCAGAGGCACGTGGAGCGGCGAGAGGCAGAGGCAGCCATGAGGAACGGA
GGACAGCCCGAGAAGGACCTGGAGTCTGGGGCGCACCTGACCCACTTCCTGTTCCGGGAA
GAGTTGCCTGCCCAGTCCATCCTGGGAAATGTGACAGAGTTGCTATTGGCGGGAGTGGAC
ACGGTGTCCAACACGCTCTCTTGGGCTCTGTATGAGCTCTCCCGGCACCCCGAAGTCCAG
ACAGCACTCCACTCAGAGATCACAGCTGCCCTGAGCCCTGGCTCCAGTGCCTACCCCTCA
GCCACTGTTCTGTCCCAGCTGCCCCTGCTGAAGGCGGTGGTCAAGGAAGTGCTAAGACTG
TACCCTGTGGTACCTGGAAATTCTCGTGTCCCAGACAAAGACATTCATGTGGGTGACTAT
ATTATCCCCAAAAATACGCTGGTCACTCTGTGTCACTATGCCACTTCAAGGGACCCTGCC
CAGTTCCCAGAGCCAAATTCTTTTCGTCCAGCTCGCTGGCTGGGGGAGGGTCCCACCCCC
CACCCATTTGCATCTCTTCCCTTTGGCTTTGGCAAGCGCAGCTGTATGGGGAGACGCCTG
GCAGAGCTTGAATTGCAAATGGCTTTGGCCCAGATCCTAACACATTTTGAGGTGCAGCCT
GAGCCAGGTGCGGCCCCAGTTAGACCCAAGACCCGGACTGTCCTGGTACCTGAAAGGAGC
ATCAACCTACAGTTTTTGGACAGATAG
Enzyme 3 GenBank Gene ID AB005038 Link Image
Enzyme 3 GeneCard ID CYP27B1 Link Image
Enzyme 3 GenAtlas ID CYP27B1 Link Image
Enzyme 3 HGNC ID HGNC:2606 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 12q13.1-q13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Fu GK, Portale AA, Miller WL: Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. DNA Cell Biol. 1997 Dec;16(12):1499-507. [PubMed Link Image]
  2. Monkawa T, Yoshida T, Wakino S, Shinki T, Anazawa H, Deluca HF, Suda T, Hayashi M, Saruta T: Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase. Biochem Biophys Res Commun. 1997 Oct 20;239(2):527-33. [PubMed Link Image]
  3. Fu GK, Lin D, Zhang MY, Bikle DD, Shackleton CH, Miller WL, Portale AA: Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol Endocrinol. 1997 Dec;11(13):1961-70. [PubMed Link Image]
  4. Kitanaka S, Takeyama K, Murayama A, Sato T, Okumura K, Nogami M, Hasegawa Y, Niimi H, Yanagisawa J, Tanaka T, Kato S: Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets. N Engl J Med. 1998 Mar 5;338(10):653-61. [PubMed Link Image]
  5. Wang JT, Lin CJ, Burridge SM, Fu GK, Labuda M, Portale AA, Miller WL: Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families. Am J Hum Genet. 1998 Dec;63(6):1694-702. [PubMed Link Image]
  6. Smith SJ, Rucka AK, Berry JL, Davies M, Mylchreest S, Paterson CR, Heath DA, Tassabehji M, Read AP, Mee AP, Mawer EB: Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. J Bone Miner Res. 1999 May;14(5):730-9. [PubMed Link Image]
  7. Kitanaka S, Murayama A, Sakaki T, Inouye K, Seino Y, Fukumoto S, Shima M, Yukizane S, Takayanagi M, Niimi H, Takeyama K, Kato S: No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation. J Clin Endocrinol Metab. 1999 Nov;84(11):4111-7. [PubMed Link Image]
  8. Wang X, Zhang MY, Miller WL, Portale AA: Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro. J Clin Endocrinol Metab. 2002 Jun;87(6):2424-30. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7156
Enzyme 4 Name Vitamin D3 receptor
Enzyme 4 Synonyms
  1. VDR
  2. 1,25-dihydroxyvitamin D3 receptor
  3. Nuclear receptor subfamily 1 group I member 1
Enzyme 4 Gene Name VDR
Enzyme 4 Protein Sequence >Vitamin D3 receptor
MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTC
PFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSL
RPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSG
DSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQK
VIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDV
TKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLS
NTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLE
VFGNEIS
Enzyme 4 Number of Residues 427
Enzyme 4 Molecular Weight 48288.6
Enzyme 4 Theoretical pI 6.50
Enzyme 4 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 4 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 4 Specific Function Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Recruited to promoters via its interaction with the WINAC complex subunit BAZ1B/WSTF, which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 340203 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P11473 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name VDR_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1284 bp
ATGGAGGCAATGGCGGCCAGCACTTCCCTGCCTGACCCTGGAGACTTTGACCGGAACGTG
CCCCGGATCTGTGGGGTGTGTGGAGACCGAGCCACTGGCTTTCACTTCAATGCTATGACC
TGTGAAGGCTGCAAAGGCTTCTTCAGGCGAAGCATGAAGCGGAAGGCACTATTCACCTGC
CCCTTCAACGGGGACTGCCGCATCACCAAGGACAACCGACGCCACTGCCAGGCCTGCCGG
CTCAAACGCTGTGTGGACATCGGCATGATGAAGGAGTTCATTCTGACAGATGAGGAAGTG
CAGAGGAAGCGGGAGATGATCCTGAAGCGGAAGGAGGAGGAGGCCTTGAAGGACAGTCTG
CGGCCCAAGCTGTCTGAGGAGCAGCAGCGCATCATTGCCATACTGCTGGACGCCCACCAT
AAGACCTACGACCCCACCTACTCCGACTTCTGCCAGTTCCGGCCTCCAGTTCGTGTGAAT
GATGGTGGAGGGAGCCATCCTTCCAGGCCCAACTCCAGACACACTCCCAGCTTCTCTGGG
GACTCCTCCTCCTCCTGCTCAGATCACTGTATCACCTCTTCAGACATGATGGACTCGTCC
AGCTTCTCCAATCTGGATCTGAGTGAAGAAGATTCAGATGACCCTTCTGTGACCCTAGAG
CTGTCCCAGCTCTCCATGCTGCCCCACCTGGCTGACCTGGTCAGTTACAGCATCCAAAAG
GTCATTGGCTTTGCTAAGATGATACCAGGATTCAGAGACCTCACCTCTGAGGACCAGATC
GTACTGCTGAAGTCAAGTGCCATTGAGGTCATCATGTTGCGCTCCAATGAGTCCTTCACC
ATGGACGACATGTCCTGGACCTGTGGCAACCAAGACTACAAGTACCGCGTCAGTGACGTG
ACCAAAGCCGGACACAGCCTGGAGCTGATTGAGCCCCTCATCAAGTTCCAGGTGGGACTG
AAGAAGCTGAACTTGCATGAGGAGGAGCATGTCCTGCTCATGGCCATCTGCATCGTCTCC
CCAGATCGTCCTGGGGTGCAGGACGCCGCGCTGATTGAGGCCATCCAGGACCGCCTGTCC
AACACACTGCAGACGTACATCCGCTGCCGCCACCCGCCCCCGGGCAGCCACCTGCTCTAT
GCCAAGATGATCCAGAAGCTAGCCGACCTGCGCAGCCTCAATGAGGAGCACTCCAAGCAG
TACCGCTGCCTCTCCTTCCAGCCTGAGTGCAGCATGAAGCTAACGCCCCTTGTGCTCGAA
GTGTTTGGCAATGAGATCTCCTGA
Enzyme 4 GenBank Gene ID J03258 Link Image
Enzyme 4 GeneCard ID VDR Link Image
Enzyme 4 GenAtlas ID VDR Link Image
Enzyme 4 HGNC ID HGNC:12679 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 12q13.11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Baker AR, McDonnell DP, Hughes M, Crisp TM, Mangelsdorf DJ, Haussler MR, Pike JW, Shine J, O'Malley BW: Cloning and expression of full-length cDNA encoding human vitamin D receptor. Proc Natl Acad Sci U S A. 1988 May;85(10):3294-8. [PubMed Link Image]
  2. Goto H, Chen KS, Prahl JM, DeLuca HF: A single receptor identical with that from intestine/T47D cells mediates the action of 1,25-dihydroxyvitamin D-3 in HL-60 cells. Biochim Biophys Acta. 1992 Aug 17;1132(1):103-8. [PubMed Link Image]
  3. Miyamoto K, Kesterson RA, Yamamoto H, Taketani Y, Nishiwaki E, Tatsumi S, Inoue Y, Morita K, Takeda E, Pike JW: Structural organization of the human vitamin D receptor chromosomal gene and its promoter. Mol Endocrinol. 1997 Jul;11(8):1165-79. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yu XP, Mocharla H, Hustmyer FG, Manolagas SC: Vitamin D receptor expression in human lymphocytes. Signal requirements and characterization by western blots and DNA sequencing. J Biol Chem. 1991 Apr 25;266(12):7588-95. [PubMed Link Image]
  7. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed Link Image]
  8. Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed Link Image]
  9. Fujiki R, Kim MS, Sasaki Y, Yoshimura K, Kitagawa H, Kato S: Ligand-induced transrepression by VDR through association of WSTF with acetylated histones. EMBO J. 2005 Nov 16;24(22):3881-94. Epub 2005 Oct 27. [PubMed Link Image]
  10. Rochel N, Wurtz JM, Mitschler A, Klaholz B, Moras D: The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand. Mol Cell. 2000 Jan;5(1):173-9. [PubMed Link Image]
  11. Tocchini-Valentini G, Rochel N, Wurtz JM, Mitschler A, Moras D: Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5491-6. [PubMed Link Image]
  12. Shaffer PL, Gewirth DT: Structural basis of VDR-DNA interactions on direct repeat response elements. EMBO J. 2002 May 1;21(9):2242-52. [PubMed Link Image]
  13. Tocchini-Valentini G, Rochel N, Wurtz JM, Moras D: Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification. J Med Chem. 2004 Apr 8;47(8):1956-61. [PubMed Link Image]
  14. Shaffer PL, Gewirth DT: Structural analysis of RXR-VDR interactions on DR3 DNA. J Steroid Biochem Mol Biol. 2004 May;89-90(1-5):215-9. [PubMed Link Image]
  15. Eelen G, Verlinden L, Rochel N, Claessens F, De Clercq P, Vandewalle M, Tocchini-Valentini G, Moras D, Bouillon R, Verstuyf A: Superagonistic action of 14-epi-analogs of 1,25-dihydroxyvitamin D explained by vitamin D receptor-coactivator interaction. Mol Pharmacol. 2005 May;67(5):1566-73. Epub 2005 Feb 22. [PubMed Link Image]
  16. Hourai S, Fujishima T, Kittaka A, Suhara Y, Takayama H, Rochel N, Moras D: Probing a water channel near the A-ring of receptor-bound 1 alpha,25-dihydroxyvitamin D3 with selected 2 alpha-substituted analogues. J Med Chem. 2006 Aug 24;49(17):5199-205. [PubMed Link Image]
  17. Hughes MR, Malloy PJ, Kieback DG, Kesterson RA, Pike JW, Feldman D, O'Malley BW: Point mutations in the human vitamin D receptor gene associated with hypocalcemic rickets. Science. 1988 Dec 23;242(4886):1702-5. [PubMed Link Image]
  18. Yagi H, Ozono K, Miyake H, Nagashima K, Kuroume T, Pike JW: A new point mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor in a kindred with hereditary 1,25-dihydroxyvitamin D-resistant rickets. J Clin Endocrinol Metab. 1993 Feb;76(2):509-12. [PubMed Link Image]
  19. Saijo T, Ito M, Takeda E, Huq AH, Naito E, Yokota I, Sone T, Pike JW, Kuroda Y: A unique mutation in the vitamin D receptor gene in three Japanese patients with vitamin D-dependent rickets type II: utility of single-strand conformation polymorphism analysis for heterozygous carrier detection. Am J Hum Genet. 1991 Sep;49(3):668-73. [PubMed Link Image]
  20. Sone T, Marx SJ, Liberman UA, Pike JW: A unique point mutation in the human vitamin D receptor chromosomal gene confers hereditary resistance to 1,25-dihydroxyvitamin D3. Mol Endocrinol. 1990 Apr;4(4):623-31. [PubMed Link Image]
  21. Malloy PJ, Weisman Y, Feldman D: Hereditary 1 alpha,25-dihydroxyvitamin D-resistant rickets resulting from a mutation in the vitamin D receptor deoxyribonucleic acid-binding domain. J Clin Endocrinol Metab. 1994 Feb;78(2):313-6. [PubMed Link Image]
  22. Kristjansson K, Rut AR, Hewison M, O'Riordan JL, Hughes MR: Two mutations in the hormone binding domain of the vitamin D receptor cause tissue resistance to 1,25 dihydroxyvitamin D3. J Clin Invest. 1993 Jul;92(1):12-6. [PubMed Link Image]
  23. Rut AR, Hewison M, Kristjansson K, Luisi B, Hughes MR, O'Riordan JL: Two mutations causing vitamin D resistant rickets: modelling on the basis of steroid hormone receptor DNA-binding domain crystal structures. Clin Endocrinol (Oxf). 1994 Nov;41(5):581-90. [PubMed Link Image]
  24. Lin NU, Malloy PJ, Sakati N, al-Ashwal A, Feldman D: A novel mutation in the deoxyribonucleic acid-binding domain of the vitamin D receptor causes hereditary 1,25-dihydroxyvitamin D-resistant rickets. J Clin Endocrinol Metab. 1996 Jul;81(7):2564-9. [PubMed Link Image]
  25. Whitfield GK, Selznick SH, Haussler CA, Hsieh JC, Galligan MA, Jurutka PW, Thompson PD, Lee SM, Zerwekh JE, Haussler MR: Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D3: point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partner. Mol Endocrinol. 1996 Dec;10(12):1617-31. [PubMed Link Image]
  26. Malloy PJ, Eccleshall TR, Gross C, Van Maldergem L, Bouillon R, Feldman D: Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness. J Clin Invest. 1997 Jan 15;99(2):297-304. [PubMed Link Image]
  27. Selvaraj P, Kurian SM, Chandra G, Reetha AM, Charles N, Narayanan PR: Vitamin D receptor gene variants of BsmI, ApaI, TaqI, and FokI polymorphisms in spinal tuberculosis. Clin Genet. 2004 Jan;65(1):73-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7159
Enzyme 5 Name 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
Enzyme 5 Synonyms
  1. 24-OHase
  2. Vitamin D(3) 24-hydroxylase
  3. Cytochrome P450 24A1
  4. Cytochrome P450-CC24
Enzyme 5 Gene Name CYP24A1
Enzyme 5 Protein Sequence >1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPG
PTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYR
TESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKIN
EVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIM
AIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSAD
FLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL
PENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQ
VLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIV
RKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR
Enzyme 5 Number of Residues 514
Enzyme 5 Molecular Weight 58874.7
Enzyme 5 Theoretical pI 8.99
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 5 General Function Involved in monooxygenase activity
Enzyme 5 Specific Function Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25- hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. It also shows 23- hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin D(3)-26,23-lactone as end product
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 7939322 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q07973 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CP24A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1545 bp
ATGAGCTCCCCCATCAGCAAGAGCCGCTCGCTTGCCGCCTTCCTGCAGCAGCTGCGCAGT
CCGAGGCAGCCCCCGAGACTGGTGACATCTACGGCGTACACGTCCCCTCAGCCGCGAGAG
GTGCCAGTCTGCCCGCTGACAGCTGGTGGCGAGACTCAGAACGCGGCCGCCCTGCCGGGC
CCCACCAGCTGGCCACTGCTGGGCAGCCTGCTGCAGATTCTCTGGAAAGGGGGTCTCAAG
AAACAGCACGACACCCTGGTGGAGTACCACAAGAAGTATGGCAAGATTTTCCGCATGAAG
TTGGGTTCCTTTGAGTCGGTGCACCTGGGCTCGCCATGCCTGCTGGAAGCGCTGTACCGC
ACCGAGAGCGCGTACCCGCAGCGGCTGGAGATCAAACCGTGGAAGGCCTATCGCGACTAC
CGCAAAGAAGGCTACGGGCTGCTGATCCTGGAAGGGGAAGACTGGCAGCGGGTCCGGAGT
GCCTTTCAAAAGAAACTAATGAAACCAGGGGAAGTGATGAAGCTGGACAACAAAATCAAT
GAGGTCTTGGCCGATTTTATGGGCAGAATAGATGAGCTCTGTGATGAAAGAGGCCACGTT
GAAGACTTGTACAGCGAACTGAACAAATGGTCGTTTGAAAGTATCTGCCTCGTGTTGTAT
GAGAAGAGATTTGGGCTTCTCCAGAAGAATGCAGGGGATGAAGCTGTGAACTTCATCATG
GCCATCAAAACAATGATGAGCACGTTTGGGAGGATGATGGTCACTCCAGTCGAGCTGCAC
AAGAGCCTCAACACCAAGGTCTGGCAGGACCACACTCTGGCCTGGGACACCATTTTCAAA
TCAGTCAAAGCTTGTATCGACAACCGGTTAGAGAAGTATTCTCAGCAGCCTAGTGCAGAT
TTCCTTTGTGACATTTATCACCAGAATCGGCTTTCAAAGAAAGAATTGTATGCTGCTGTC
ACAGAGCTCCAGCTGGCTGCGGTGGAAACGACAGCAAACAGTCTAATGTGGATTCTCTAC
AATTTATCCCGTAATCCCCAAGTGCAACAAAAGCTTCTTAAGGAAATTCAAAGTGTATTA
CCTGAGAATCAGGTGCCACGGGCAGAAGATTTGAGGAATATGCCGTATTTAAAAGCCTGT
CTGAAAGAATCTATGAGGCTTACGCCGAGTGTACCATTTACAACTCGGACTCTTGACAAG
GCAACAGTTCTGGGTGAATATGCTTTACCCAAAGGAACAGTGCTCATGCTAAATACCCAG
GTGTTGGGATCCAGTGAAGACAATTTTGAAGATTCAAGTCAGTTTAGACCTGAACGTTGG
CTTCAGGAGAAGGAAAAAATTAATCCTTTTGCGCATCTTCCATTTGGCGTTGGAAAAAGA
ATGTGCATTGGTCGCCGATTAGCAGAGCTTCAACTGCATTTGGCTCTTTGTTGGATTGTC
CGCAAATACGACATCCAGGCCACAGACAATGAGCCTGTTGAGATGCTACACTCAGGCACC
CTGGTGCCCAGCCGGGAACTCCCCATCGCGTTTTGCCAGCGATAA
Enzyme 5 GenBank Gene ID AL138805 Link Image
Enzyme 5 GeneCard ID CYP24A1 Link Image
Enzyme 5 GenAtlas ID CYP24A1 Link Image
Enzyme 5 HGNC ID HGNC:2602 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 20q13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Chen KS, Prahl JM, DeLuca HF: Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4543-7. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Chen KS, DeLuca HF: Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements. Biochim Biophys Acta. 1995 Jul 25;1263(1):1-9. [PubMed Link Image]
  4. Labuda M, Lemieux N, Tihy F, Prinster C, Glorieux FH: Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets. J Bone Miner Res. 1993 Nov;8(11):1397-406. [PubMed Link Image]
  5. Sakaki T, Kagawa N, Yamamoto K, Inouye K: Metabolism of vitamin D3 by cytochromes P450. Front Biosci. 2005 Jan 1;10:119-34. Print 2005 Jan 1. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8179
Enzyme 6 Name Vitamin D 25-hydroxylase
Enzyme 6 Synonyms
  1. Cytochrome P450 2R1
Enzyme 6 Gene Name CYP2R1
Enzyme 6 Protein Sequence >Vitamin D 25-hydroxylase
MWKLWRAEEGAAALGGALFLLLFALGVRQLLKQRRPMGFPPGPPGLPFIGNIYSLAASSE
LPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTK
MGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKSFESKILEETKFFNDAIETYKGRPFDFK
QLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPF
GKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENL
IFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPY
TEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVF
HPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPD
LKPRLGMTLQPQPYLICAERR
Enzyme 6 Number of Residues 501
Enzyme 6 Molecular Weight 57358.8
Enzyme 6 Theoretical pI 7.67
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 6 General Function Involved in monooxygenase activity
Enzyme 6 Specific Function Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3)
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O [RN:R04807]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 33591222 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q6VVX0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CP2R1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1506 bp
ATGTGGAAGCTTTGGAGAGCTGAAGAGGGCGCGGCGGCGCTCGGCGGCGCGCTCTTCCTG
CTGCTCTTCGCGCTAGGGGTCCGCCAGCTGCTGAAGCAGAGGCGGCCGATGGGCTTCCCC
CCGGGGCCGCCGGGGCTGCCATTTATCGGCAACATCTATTCCCTGGCAGCCTCATCCGAG
CTTCCCCATGTCTACATGAGAAAGCAGAGCCAGGTGTACGGAGAGATCTTCAGTTTAGAT
CTTGGAGGCATATCAACTGTGGTTCTAAATGGCTATGATGTAGTAAAGGAATGCCTTGTT
CATCAAAGCGAAATTTTTGCAGACAGACCATGCCTTCCTTTATTCATGAAGATGACAAAA
ATGGGAGGCTTACTCAATTCCAGATATGGCCGAGGATGGGTTGATCACAGACGATTAGCT
GTAAACAGTTTTCGATATTTTGGATATGGCCAAAAGTCTTTTGAATCTAAAATCTTGGAA
GAAACCAAATTTTTCAATGATGCTATTGAAACATACAAAGGTAGACCTTTTGACTTTAAA
CAGTTAATAACGAATGCTGTTTCAAACATAACCAATCTGATCATTTTTGGAGAACGATTC
ACTTATGAAGACACCGATTTTCAGCACATGATTGAGTTATTTAGTGAAAATGTGGAACTA
GCTGCCAGTGCCTCAGTCTTCTTGTATAATGCCTTTCCATGGATTGGCATCCTGCCTTTT
GGAAAACATCAACAGCTGTTTAGAAATGCAGCTGTAGTCTATGATTTTCTCTCCAGACTC
ATTGAAAAAGCTTCAGTCAACAGAAAGCCTCAGCTACCTCAGCATTTTGTTGATGCTTAT
TTAGATGAGATGGATCAAGGTAAAAATGACCCATCATCTACTTTCTCCAAAGAAAACCTA
ATTTTCTCAGTGGGTGAACTCATCATTGCTGGAACTGAAACTACAACCAATGTGCTACGG
TGGGCGATTCTTTTCATGGCCCTTTATCCTAATATTCAAGGACAAGTTCAGAAAGAGATT
GATTTAATTATGGGCCCTAATGGGAAGCCTTCTTGGGACGACAAATGCAAAATGCCTTAT
ACTGAGGCAGTTTTGCATGAAGTTTTAAGATTCTGTAATATAGTTCCATTAGGGATTTTC
CATGCAACCTCTGAAGATGCAGTTGTACGTGGTTATTCCATTCCTAAAGGCACAACAGTA
ATTACAAATCTTTATTCTGTACACTTTGATGAAAAGTACTGGAGAGACCCAGAAGTGTTC
CATCCTGAGCGATTTCTGGACAGCAGTGGATATTTTGCCAAGAAGGAAGCTTTGGTTCCT
TTTTCCCTAGGAAGAAGACATTGTCTTGGAGAACACTTGGCTCGGATGGAAATGTTCTTG
TTTTTTACAGCATTGCTTCAGAGGTTTCATTTGCATTTTCCACATGAACTAGTTCCAGAT
CTGAAGCCCAGGTTAGGCATGACATTGCAGCCCCAACCCTACCTCATCTGTGCTGAAAGA
CGCTGA
Enzyme 6 GenBank Gene ID AY323817 Link Image
Enzyme 6 GeneCard ID CYP2R1 Link Image
Enzyme 6 GenAtlas ID CYP2R1 Link Image
Enzyme 6 HGNC ID HGNC:20580 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 11p15.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Cheng JB, Motola DL, Mangelsdorf DJ, Russell DW: De-orphanization of cytochrome P450 2R1: a microsomal vitamin D 25-hydroxilase. J Biol Chem. 2003 Sep 26;278(39):38084-93. Epub 2003 Jul 16. [PubMed Link Image]
  2. Shinkyo R, Sakaki T, Kamakura M, Ohta M, Inouye K: Metabolism of vitamin D by human microsomal CYP2R1. Biochem Biophys Res Commun. 2004 Nov 5;324(1):451-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Strushkevich N, Usanov SA, Plotnikov AN, Jones G, Park HW: Structural analysis of CYP2R1 in complex with vitamin D3. J Mol Biol. 2008 Jun 27;380(1):95-106. Epub 2008 Apr 8. [PubMed Link Image]
  5. Cheng JB, Levine MA, Bell NH, Mangelsdorf DJ, Russell DW: Genetic evidence that the human CYP2R1 enzyme is a key vitamin D 25-hydroxylase. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7711-5. Epub 2004 May 5. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14986
Enzyme 7 Name Transcription initiation factor TFIID subunit 4
Enzyme 7 Synonyms
  1. RNA polymerase II TBP-associated factor subunit C
  2. TBP-associated factor 4
  3. Transcription initiation factor TFIID 130 kDa subunit
  4. TAF(II)130
  5. TAFII-130
  6. TAFII130
  7. Transcription initiation factor TFIID 135 kDa subunit
  8. TAF(II)135
  9. TAFII-135
  10. TAFII135
Enzyme 7 Gene Name TAF4
Enzyme 7 Protein Sequence >Transcription initiation factor TFIID subunit 4
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGN
HVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPA
PPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGP
GPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQT
PPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPP
AAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPGVKAESPKRVVQAAPPAAQT
LAASGPASTAASMVIGPTMQGALPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATT
SGIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAQA
HAQPQTTMAPRPATPTSAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPSATL
QRSPGVQPQLVLGGAAQTASLGTATAVQTGTPQRTVPGATTTSSAATETMENVKKCKNFL
STLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRS
LPALRQLTPDSAAFIQQSQQQPPPPTSQATTALTAVVLSSSVQRTAGKTAATVTSALQPP
VLSLTQPTQVGVGKQGQPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTP
QQIQLNPLQPVPVVKPAVLPGTKALSAVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASM
AGVNLSEESARILATNSELVGTLTRSCKDETFLLQAPLQRRILEIGKKHGITELHPDVVS
YVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDE
QEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKV
DCPGPGSGAEGSGPGSVVPGSSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLY
KAFLK
Enzyme 7 Number of Residues 1085
Enzyme 7 Molecular Weight 110113.3
Enzyme 7 Theoretical pI 10.64
Enzyme 7 GO Classification
Function
  • DNA binding
  • binding
  • nucleic acid binding
  • sequence-specific DNA binding transcription factor activity
  • transcription initiation factor activity
  • transcription regulator activity
Process
  • biological regulation
  • cellular component assembly
  • cellular component organization
  • cellular component organization or biogenesis
  • macromolecular complex assembly
  • protein complex assembly
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • transcription initiation
Component
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • nucleus
  • organelle
  • protein complex
  • transcription factor TFIID complex
  • transcription factor complex
Enzyme 7 General Function Involved in DNA binding
Enzyme 7 Specific Function Makes part of TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 56204142 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O00268 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name TAF4_HUMAN Link Image
Enzyme 7 PDB ID 1H3O Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >3258 bp
ATGGCGGCGGGCTCGGATCTGCTGGACGAGGTCTTCTTCAACAGCGAGGTGGACGAGAAA
GTGGTGAGCGACCTGGTGGGCTCGCTGGAGTCGCAGCTGGCGGCCAGCGCGGCCCACCAC
CACCACCTCGCGCCGCGCACGCCCGAGGTGCGGGCCGCGGCCGCCGGCGCGCTCGGGAAC
CATGTTGTGAGCGGCAGCCCGGCCGGAGCCGCGGGCGCAGGGCCGGCCGCCCCCGCCGAG
GGCGCGCCCGGAGCGGCGCCGGAGCCGCCCCCCGCAGGTAGAGCGCGGCCGGGGGGCGGG
GGGCCGCAGCGCCCGGGCCCCCCCTCACCGCGCCGCCCCCTTGTCCCCGCAGGGCCCGCG
CCGCCCGCCGCGAAGCTGAGGCCGCCGCCCGAGGGCAGCGCGGGGTCCTGCGCCCCGGTG
CCCGCCGCCGCCGCCGTCGCCGCGGGGCCCGAGCCCGCCCCCGCCGGCCCCGCCAAGCCC
GCCGGCCCCGCCGCGCTGGCCGCCCGCGCCGGCCCCGGCCCCGGGCCCGGCCCCGGCCCC
GGCCCCGGCCCTGGCCCTGGCAAGCCCGCCGGCCCCGGCGCCGCGCAAACTTTGAATGGG
AGCGCCGCGCTGCTGAACTCGCACCACGCCGCCGCACCTGCTGTCAGCCTGGTCAACAAC
GGGCCCGCCGCGCTGCTGCCGCTGCCCAAGCCCGCCGCCCCCGGCACTGTCATCCAGACG
CCCCCCTTCGTGGGCGCCGCCGCGCCCCCCGCGCCCGCCGCGCCCTCGCCCCCCGCCGCC
CCCGCGCCCGCCGCCCCCGCCGCCGCCCCGCCCCCGCCACCCCCCGCGCCCGCCACTCTG
GCCCGGCCGCCCGGCCACCCCGCCGGACCCCCGACCGCCGCGCCCGCCGTGCCGCCCCCC
GCCGCCGCCCAGAACGGGGGCAGCGCCGGGGCAGCCCCCGCCCCCGCCCCGGCCGCCGGG
GGCCCCGCGGGGGTCAGCGGCCAACCCGGGCCCGGCGCGGCGGCTGCGGCGCCGGCGCCG
GGGGTCAAGGCCGAGTCGCCCAAGAGGGTGGTGCAGGCGGCGCCCCCGGCGGCGCAGACC
CTGGCGGCCAGCGGCCCGGCCAGCACGGCGGCCAGCATGGTCATCGGGCCAACTATGCAA
GGGGCGCTGCCCAGCCCGGCCGCCGTCCCGCCGCCCGCCCCCGGGACCCCCACCGGGCTG
CCCAAAGGCGCGGCCGGCGCAGTGACCCAGAGCCTGTCCCGGACGCCCACGGCCACCACC
AGCGGGATTCGGGCCACCCTGACGCCCACCGTGCTGGCCCCCCGCTTGCCGCAGCCGCCT
CAGAACCCGACCAACATCCAGAACTTCCAGCTGCCCCCAGGAATGGTCCTCGTCCGAAGT
GAGAATGGGCAGTTGTTAATGATTCCTCAGCAGGCCTTGGCCCAGATGCAGGCGCAGGCC
CATGCCCAGCCTCAGACCACCATGGCGCCTCGCCCTGCCACCCCCACAAGTGCCCCTCCC
GTCCAGATCTCCACCGTACAGGCACCTGGAACACCTATCATTGCACGGCAGGTGACCCCA
ACTACCATAATTAAGCAAGTGTCTCAGGCCCAGACAACGGTGCAGCCCAGTGCAACCCTG
CAGCGCTCGCCCGGCGTCCAGCCTCAGCTCGTTCTGGGTGGCGCTGCCCAGACGGCTTCA
CTTGGGACGGCGACGGCTGTTCAGACGGGGACTCCTCAGCGCACGGTACCAGGGGCGACC
ACCACTTCCTCAGCTGCCACGGAAACTATGGAAAACGTGAAGAAATGTAAAAATTTCCTA
TCTACGTTAATAAAACTGGCTTCATCTGGCAAGCAGTCTACAGAGACAGCAGCTAATGTG
AAAGAGCTCGTGCAGAATTTACTGGATGGAAAAATAGAAGCAGAAGATTTCACAAGCAGG
TTATACCGAGAACTTAATTCTTCACCTCAACCTTACCTTGTGCCTTTCCTGAAGAGGAGC
TTACCCGCCTTGAGACAGCTGACCCCCGACTCCGCGGCCTTCATCCAGCAGAGCCAGCAG
CAGCCGCCACCGCCCACCTCGCAGGCCACCACTGCGCTCACGGCCGTGGTGCTGAGTAGC
TCGGTCCAGCGCACGGCCGGGAAGACGGCGGCCACCGTGACCAGTGCCCTCCAGCCCCCT
GTGCTCAGCCTCACGCAGCCCACGCAGGTCGGCGTCGGCAAGCAGGGGCAACCCACACCG
CTGGTCATCCAGCAGCCTCCGAAGCCAGGAGCCCTGATCCGGCCCCCGCAGGTGACGTTG
ACGCAGACACCCATGGTCGCCCTGCGGCAGCCTCACAACCGGATCATGCTCACCACGCCT
CAGCAGATCCAGCTGAACCCACTGCAGCCAGTCCCTGTGGTGAAACCCGCCGTGTTACCT
GGAACCAAAGCCCTTTCTGCTGTCTCGGCACAAGCAGCTGCTGCACAGAAAAATAAACTC
AAGGAGCCTGGGGGAGGTTCGTTTCGGGACGATGATGACATTAATGATGTTGCATCGATG
GCTGGAGTAAACTTGTCAGAAGAAAGTGCAAGAATATTAGCCACGAACTCTGAATTGGTG
GGCACGCTAACGCGGTCCTGTAAAGATGAAACCTTCCTCCTCCAAGCGCCTTTGCAGAGA
AGAATATTAGAAATAGGTAAAAAACATGGTATAACGGAATTACATCCAGATGTAGTAAGT
TATGTATCACATGCCACGCAACAAAGGCTACAGAATCTTGTAGAGAAAATATCAGAAACA
GCTCAGCAGAAGAACTTTTCTTACAAGGATGACGACAGATATGAGCAGGCGAGTGACGTC
CGGGCACAGCTCAAGTTTTTTGAACAGCTTGATCAAATCGAAAAGCAGAGGAAGGATGAG
CAGGAGCGGGAGATCCTGATGAGGGCAGCAAAGTCTCGGTCAAGACAAGAAGATCCAGAA
CAGTTAAGGCTGAAACAGAAGGCAAAGGAGATGCAGCAACAGGAACTGGCACAAATGAGA
CAGCGGGACGCCAACCTCACAGCACTAGCAGCGATCGGGCCCAGGAAAAAGAGGAAAGTG
GACTGTCCGGGGCCGGGCTCAGGAGCAGAGGGGTCGGGCCCCGGCTCAGTGGTCCCAGGC
AGCTCGGGTGTCGGAACCCCCAGACAGTTCACGCGACAAAGAATCACGCGGGTCAACCTC
AGGGACCTCATATTTTGTTTAGAAAATGAACGTGAGACAAGCCATTCACTGCTGCTCTAC
AAAGCATTCCTTAAGTGA
Enzyme 7 GenBank Gene ID AL109911 Link Image
Enzyme 7 GeneCard ID TAF4 Link Image
Enzyme 7 GenAtlas ID TAF4 Link Image
Enzyme 7 HGNC ID HGNC:11537 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 20q13.33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Mengus G, May M, Carre L, Chambon P, Davidson I: Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells. Genes Dev. 1997 Jun 1;11(11):1381-95. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A: Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13611-6. [PubMed Link Image]
  4. Damania B, Alwine JC: TAF-like function of SV40 large T antigen. Genes Dev. 1996 Jun 1;10(11):1369-81. [PubMed Link Image]
  5. Brand M, Yamamoto K, Staub A, Tora L: Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J Biol Chem. 1999 Jun 25;274(26):18285-9. [PubMed Link Image]
  6. Cavusoglu N, Brand M, Tora L, Van Dorsselaer A: Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis. Proteomics. 2003 Feb;3(2):217-23. [PubMed Link Image]
  7. Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell. 2005 Jun 17;121(6):873-85. [PubMed Link Image]
  8. Hamard PJ, Dalbies-Tran R, Hauss C, Davidson I, Kedinger C, Chatton B: A functional interaction between ATF7 and TAF12 that is modulated by TAF4. Oncogene. 2005 May 12;24(21):3472-83. [PubMed Link Image]
  9. Gangloff YG, Werten S, Romier C, Carre L, Poch O, Moras D, Davidson I: The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs. Mol Cell Biol. 2000 Jan;20(1):340-51. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 17105
Enzyme 8 Name Nuclear receptor coactivator 6
Enzyme 8 Synonyms
  1. Activating signal cointegrator 2
  2. ASC-2
  3. Amplified in breast cancer protein 3
  4. Cancer-amplified transcriptional coactivator ASC-2
  5. Nuclear receptor coactivator RAP250
  6. NRC RAP250
  7. Nuclear receptor-activating protein, 250 kDa
  8. Peroxisome proliferator-activated receptor-interacting protein
  9. PPAR-interacting protein
  10. PRIP
  11. Thyroid hormone receptor-binding protein
Enzyme 8 Gene Name NCOA6
Enzyme 8 Protein Sequence >Nuclear receptor coactivator 6
MVLDDLPNLEDIYTSLCSSTMEDSEMDFDSGLEDDDTKSDSILEDSTIFVAFKGNIDDKD
FKWKLDAILKNVPNLLHMESSKLKVQKVEPWNSVRVTFNIPREAAERLRILAQSNNQQLR
DLGILSVQIEGEGAINLALAQNRSQDVRMNGPMGAGNSVRMEAGFPMASGPGIIRMNNPA
TVMIPPGGNVSSSMMAPGPNPELQPRTPRPASQSDAMDPLLSGLHIQQQSHPSGSLAPPH
HPMQPVSVNRQMNPANFPQLQQQQQQQQQQQQQQQQQQQQQQQQQLQARPPQQHQQQQPQ
GIRPQFTAPTQVPVPPGWNQLPSGALQPPPAQGSLGTMTANQGWKKAPLPGPMQQQLQAR
PSLATVQTPSHPPPPYPFGSQQASQAHTNFPQMSNPGQFTAPQMKSLQGGPSRVPTPLQQ
PHLTNKSPASSPSSFQQGSPASSPTVNQTQQQMGPRPPQNNPLPQGFQQPVSSPGRNPMV
QQGNVPPNFMVMQQQPPNQGPQSLHPGLGGMPKRLPPGFSAGQANPNFMQGQVPSTTATT
PGNSGAPQLQANQNVQHAGGQGAGPPQNQMQVSHGPPNMMQPSLMGIHGNMNNQQAGTSG
VPQVNLSNMQGQPQQGPPSQLMGMHQQIVPSQGQMVQQQGTLNPQNPMILSRAQLMPQGQ
MMVNPPSQNLGPSPQRMTPPKQMLSQQGPQMMAPHNQMMGPQGQVLLQQNPMIEQIMTNQ
MQGNKQQFNTQNQSNVMPGPAQIMRGPTPNMQGNMVQFTGQMSGQMLPQQGPVNNSPSQV
MGIQGQVLRPPGPSPHMAQQHGDPATTANNDVSLSQMMPDVSIQQTNMVPPHVQAMQGNS
ASGNHFSGHGMSFNAPFSGAPNGNQMSCGQNPGFPVNKDVTLTSPLLVNLLQSDISAGHF
GVNNKQNNTNANKPKKKKPPRKKKNSQQDLNTPDTRPAGLEEADQPPLPGEQGINLDNSG
PKLPEFSNRPPGYPSQPVEQRPLQQMPPQLMQHVAPPPQPPQQQPQPQLPQQQQPPPPSQ
PQSQQQQQQQQQMMMMLMMQQDPKSVRLPVSQNVHPPRGPLNPDSQRMPMQQSGSVPVMV
SLQGPASVPPSPDKQRMPMPVNTPLGSNSRKMVYQESPQNPSSSPLAEMASLPEASGSEA
PSVPGGPNNMPSHVVLPQNQLMMTGPKPGPSPLSATQGATPQQPPVNSLPSSHGHHFPNV
AAPTQTSRPKTPNRASPRPYYPQTPNNRPPSTEPSEISLSPERLNASIAGLFPPQINIPL
PPRPNLNRGFDQQGLNPTTLKAIGQAPSNLTMNPSNFATPQTHKLDSVVVNSGKQSNSGA
TKRASPSNSRRSSPGSSRKTTPSPGRQNSKAPKLTLASQTNAALLQNVELPRNVLVSPTP
LANPPVPGSFPNNSGLNPQNSTVSVAAVGGVVEDNKESLNVPQDSDCQNSQSRKEQVNIE
LKAVPAQEVKMVVPEDQSKKDGQPSDPNKLPSVEENKNLVSPAMREAPTSLSQLLDNSGA
PNVTIKPPGLTDLEVTPPVVSGEDLKKASVIPTLQDLSSSKEPSNSLNLPHSNELCSSLV
HPELSEVSSNVAPSIPPVMSRPVSSSSISTPLPPNQITVFVTSNPITTSANTSAALPTHL
QSALMSTVVTMPNAGSKVMVSEGQSAAQSNARPQFITPVFINSSSIIQVMKGSQPSTIPA
APLTTNSGLMPPSVAVVGPLHIPQNIKFSSAPVPPNALSSSPAPNIQTGRPLVLSSRATP
VQLPSPPCTSSPVVPSHPPVQQVKELNPDEASPQVNTSADQNTLPSSQSTTMVSPLLTNS
PGSSGNRRSPVSSSKGKGKVDKIGQILLTKACKKVTGSLEKGEEQYGADGETEGQGLDTT
APGLMGTEQLSTELDSKTPTPPAPTLLKMTSSPVGPGTASAGPSLPGGALPTSVRSIVTT
LVPSELISAVPTTKSNHGGIASESLAGGLVEEKVGSHPELLPSIAPSQNLVSKETSTTAL
QASVARPELEVNAAIVSGQSSEPKEIVEKSKIPGRRNSRTEEPTVASESVENGHRKRSSR
PASASSSTKDITSAVQSKRRKSK
Enzyme 8 Number of Residues 2063
Enzyme 8 Molecular Weight 219144.8
Enzyme 8 Theoretical pI 10.06
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Involved in chromatin binding
Enzyme 8 Specific Function Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7140574 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q14686 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NCOA6_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >6192 bp
ATGGTTTTGGATGACCTTCCAAACTTAGAAGACATCTATACTTCCTTGTGTTCATCAACA
ATGGAAGACTCAGAGATGGATTTTGACTCTGGACTAGAAGATGATGACACAAAAAGTGAT
AGTATTTTGGAGGATTCCACAATTTTTGTGGCCTTCAAAGGAAATATAGATGATAAAGAC
TTCAAATGGAAATTAGATGCAATATTGAAAAACGTGCCCAATTTGTTACACATGGAGTCC
AGCAAGCTAAAAGTACAGAAGGTGGAGCCCTGGAACAGCGTGCGTGTGACATTCAACATC
CCCCGGGAAGCAGCGGAGCGGCTACGGATCCTTGCTCAGAGCAACAACCAGCAGCTTCGG
GATTTAGGGATTCTCTCCGTTCAGATTGAAGGGGAAGGTGCTATTAACCTGGCTTTGGCT
CAGAACCGAAGCCAAGATGTGAGAATGAATGGACCCATGGGAGCTGGAAATTCAGTTAGG
ATGGAGGCGGGATTTCCTATGGCAAGTGGTCCAGGAATAATAAGGATGAACAACCCTGCC
ACTGTTATGATACCCCCGGGTGGAAATGTGTCATCTTCCATGATGGCACCAGGCCCCAAT
CCAGAGCTGCAGCCCAGGACTCCTCGCCCTGCTTCTCAGTCAGATGCAATGGATCCACTC
CTCTCTGGGCTCCATATACAGCAGCAAAGTCATCCCTCAGGATCTTTAGCTCCCCCACAT
CACCCAATGCAGCCTGTCTCTGTGAACAGACAAATGAACCCAGCTAATTTTCCCCAGCTG
CAGCAGCAGCAGCAACAACAACAACAGCAGCAGCAGCAGCAGCAGCAGCAACAACAGCAA
CAGCAGCAACAACAGTTGCAGGCAAGACCCCCACAGCAACATCAGCAGCAACAGCCACAG
GGAATTCGACCCCAGTTTACTGCCCCAACTCAGGTGCCTGTTCCTCCAGGCTGGAACCAG
CTGCCTTCTGGAGCCCTTCAACCTCCTCCAGCCCAGGGTTCTCTGGGCACAATGACTGCA
AACCAAGGGTGGAAGAAGGCTCCCTTGCCCGGCCCAATGCAACAGCAACTCCAGGCAAGA
CCATCCTTAGCCACGGTACAGACGCCTTCCCACCCTCCCCCTCCATATCCCTTTGGCAGC
CAGCAAGCCTCACAAGCCCACACAAACTTTCCTCAGATGAGCAACCCAGGCCAGTTCACA
GCTCCTCAGATGAAGAGTTTGCAGGGAGGGCCCTCTAGGGTCCCAACTCCCTTGCAGCAG
CCCCACCTCACCAACAAGTCTCCTGCCTCCTCACCCTCCTCCTTCCAGCAGGGATCCCCT
GCATCCTCCCCAACGGTTAACCAAACTCAGCAGCAGATGGGACCAAGGCCACCTCAAAAT
AACCCACTTCCCCAGGGATTTCAGCAGCCTGTCAGCTCTCCGGGTCGGAATCCTATGGTT
CAACAGGGAAATGTGCCACCTAACTTCATGGTGATGCAGCAGCAACCACCAAACCAGGGG
CCACAGAGTTTACATCCAGGCCTAGGAGGAATGCCTAAACGCCTCCCACCTGGCTTCTCA
GCAGGACAGGCCAATCCGAACTTTATGCAAGGTCAGGTGCCTTCGACCACAGCAACCACC
CCTGGGAATTCAGGAGCCCCTCAGCTGCAAGCAAATCAAAATGTCCAGCATGCAGGTGGT
CAAGGAGCTGGTCCTCCTCAAAACCAGATGCAGGTGTCCCACGGGCCGCCAAATATGATG
CAGCCCAGCCTCATGGGAATTCATGGCAACATGAACAATCAGCAGGCTGGTACTTCTGGG
GTTCCTCAAGTGAACCTCAGCAACATGCAAGGCCAGCCCCAGCAGGGCCCACCATCTCAG
CTGATGGGCATGCACCAGCAAATCGTGCCCTCCCAGGGCCAGATGGTCCAGCAACAAGGA
ACCTTGAACCCTCAGAACCCTATGATCCTTTCAAGGGCCCAGCTTATGCCACAGGGCCAG
ATGATGGTGAACCCCCCGAGCCAAAATCTTGGGCCCTCGCCCCAAAGGATGACCCCACCC
AAGCAGATGCTTTCCCAGCAGGGCCCACAAATGATGGCGCCACATAACCAGATGATGGGG
CCTCAGGGGCAGGTTTTGCTCCAACAGAACCCAATGATAGAGCAGATTATGACCAATCAA
ATGCAGGGGAATAAGCAGCAGTTTAACACTCAGAACCAGTCCAATGTCATGCCGGGACCA
GCCCAGATAATGAGGGGACCAACTCCGAACATGCAAGGAAATATGGTGCAGTTTACGGGA
CAGATGTCAGGACAGATGCTGCCCCAGCAAGGGCCTGTGAACAACAGTCCATCTCAGGTT
ATGGGCATTCAGGGACAGGTCCTGCGGCCACCAGGGCCCAGCCCACACATGGCCCAGCAG
CATGGTGATCCTGCTACTACAGCAAATAACGATGTCAGTTTATCTCAGATGATGCCTGAT
GTTAGCATTCAACAAACCAACATGGTCCCCCCTCATGTGCAGGCCATGCAGGGAAACAGT
GCCTCGGGAAACCACTTCTCAGGCCATGGGATGTCTTTCAATGCACCTTTCAGTGGAGCT
CCCAATGGAAATCAGATGTCCTGTGGTCAAAATCCAGGCTTCCCAGTCAATAAGGATGTC
ACGCTAACGAGCCCATTGTTGGTCAACTTATTGCAGAGTGACATATCTGCAGGCCATTTT
GGGGTAAACAATAAGCAAAATAATACCAACGCAAATAAACCGAAGAAGAAGAAACCCCCT
CGGAAGAAGAAAAATAGTCAGCAAGATCTAAACACCCCAGATACTCGCCCAGCTGGTCTG
GAAGAGGCTGATCAGCCACCGTTGCCTGGAGAACAAGGAATTAGCTTGGATAACTCAGGC
CCTAAACTGCCAGAATTTTCAAACCGGCCACCAGGTTATCCTTCTCAACCAGTTGAACAG
AGGCCACTTCAGCAGATGCCTCCTCAACTCATGCAGCATGTGGCACCCCCACCACAGCCA
CCACAGCAGCAGCCACAGCCACAACTGCCTCAGCAGCAGCAGCCACCACCTCCCAGTCAG
CCACAGTCTCAGCAGCAGCAGCAGCAGCAGCAACAAATGATGATGATGCTCATGATGCAG
CAGGATCCCAAATCAGTTAGGCTTCCAGTCTCTCAAAATGTCCATCCTCCAAGGGGCCCC
CTGAACCCCGACTCCCAGAGAATGCCCATGCAACAGAGTGGCAGTGTGCCTGTCATGGTC
AGTCTGCAAGGACCTGCCTCCGTGCCACCATCACCTGATAAACAAAGAATGCCAATGCCT
GTGAATACTCCCTTGGGAAGCAATTCAAGGAAAATGGTCTATCAGGAGAGCCCGCAGAAT
CCTTCCAGCTCGCCACTGGCGGAGATGGCCTCACTCCCTGAAGCAAGTGGCAGTGAAGCA
CCATCTGTCCCAGGAGGCCCAAACAACATGCCTTCACATGTAGTACTTCCCCAGAATCAG
TTAATGATGACAGGGCCAAAACCTGGACCATCGCCCCTTTCAGCAACTCAAGGTGCAACT
CCCCAGCAACCCCCTGTAAATTCCCTGCCCAGCTCTCACGGCCACCACTTCCCAAATGTG
GCTGCGCCAACCCAGACATCTAGGCCCAAAACACCAAACAGAGCCAGCCCCAGACCCTAT
TATCCTCAGACACCCAACAACCGCCCTCCCAGCACAGAACCTTCAGAAATCAGTCTGTCA
CCAGAAAGACTCAATGCCTCCATAGCAGGACTCTTCCCTCCACAGATTAATATTCCTTTA
CCTCCTAGGCCAAATTTAAACAGGGGCTTTGATCAACAAGGCCTAAATCCAACAACTTTG
AAGGCCATCGGGCAAGCACCTTCAAATCTTACCATGAATCCTTCCAATTTTGCTACCCCA
CAAACTCACAAATTAGATTCTGTGGTAGTGAATTCTGGAAAGCAGTCTAATTCTGGAGCA
ACAAAACGGGCAAGTCCAAGCAACAGTCGCAGGTCTAGTCCTGGGTCCAGTAGGAAAACC
ACTCCAAGCCCTGGGAGGCAAAATTCAAAAGCCCCTAAACTTACTCTGGCCTCTCAGACA
AATGCAGCCCTATTGCAGAATGTGGAGTTGCCGAGAAATGTATTGGTCAGTCCCACTCCT
CTGGCCAATCCCCCTGTACCTGGGAGCTTTCCTAACAACAGTGGGCTGAATCCTCAGAAT
TCTACTGTGTCTGTGGCTGCAGTTGGGGGTGTTGTTGAGGATAACAAGGAGAGCTTGAAT
GTGCCTCAGGACAGTGATTGCCAGAATTCCCAGAGTAGGAAGGAACAGGTAAACATTGAA
CTAAAAGCAGTCCCTGCCCAAGAAGTTAAAATGGTTGTCCCTGAAGATCAGTCCAAAAAG
GATGGGCAGCCTTCGGATCCTAACAAACTTCCCAGTGTCGAAGAGAACAAAAATTTGGTG
TCTCCTGCTATGAGGGAAGCACCAACATCGTTAAGTCAACTTCTTGACAACTCTGGAGCT
CCCAATGTGACAATTAAACCCCCTGGGCTTACAGATCTGGAAGTAACACCTCCAGTAGTT
TCTGGGGAGGACCTCAAAAAAGCATCTGTCATTCCCACACTGCAGGATCTGTCTTCTTCT
AAAGAACCTTCTAATTCCCTAAACTTACCTCACAGTAATGAGCTGTGTTCATCCCTTGTG
CATCCCGAATTGAGTGAGGTCAGTTCTAACGTTGCACCAAGCATCCCTCCAGTAATGTCA
AGACCTGTTAGCTCTTCCTCCATTTCCACTCCCTTGCCCCCAAATCAAATAACTGTATTT
GTCACTTCCAATCCCATCACAACTTCAGCTAACACATCAGCAGCTTTGCCAACTCACTTG
CAGTCTGCATTGATGTCAACAGTTGTCACAATGCCCAATGCGGGTAGCAAGGTTATGGTT
TCTGAGGGACAGTCAGCTGCTCAGTCTAATGCCCGGCCTCAGTTCATTACACCTGTCTTT
ATCAATTCATCCTCAATAATTCAGGTTATGAAAGGATCACAGCCAAGCACAATTCCTGCA
GCCCCACTGACAACCAACTCTGGCCTGATGCCTCCCTCTGTTGCAGTTGTTGGCCCTTTA
CACATACCTCAGAACATAAAATTTTCTTCTGCTCCTGTACCGCCTAATGCCCTCTCCAGT
AGTCCTGCTCCAAACATCCAGACAGGTCGACCTTTGGTCCTTAGCTCACGAGCCACCCCT
GTTCAGCTTCCTTCCCCTCCTTGTACGTCTTCTCCAGTTGTCCCTTCTCATCCCCCTGTG
CAGCAAGTGAAAGAATTGAATCCAGATGAGGCTAGCCCTCAGGTGAACACCTCAGCAGAT
CAGAACACTCTTCCCTCTTCACAGTCAACCACAATGGTTTCTCCCCTTTTGACCAATAGT
CCAGGGTCCTCTGGCAACCGGCGAAGCCCAGTCTCGTCTAGTAAGGGCAAAGGAAAAGTG
GACAAAATTGGCCAAATTTTGTTGACCAAGGCATGTAAGAAAGTTACAGGCTCTCTTGAG
AAAGGGGAAGAACAATATGGTGCAGATGGAGAGACTGAAGGCCAAGGGCTAGACACCACA
GCTCCGGGGCTCATGGGAACAGAGCAGTTATCCACAGAGCTGGACAGTAAAACCCCAACG
CCCCCAGCACCCACTCTGCTAAAAATGACCTCTAGCCCTGTGGGCCCGGGCACTGCCTCA
GCAGGACCCAGCTTACCTGGCGGTGCTCTCCCCACCAGTGTACGCTCGATAGTAACCACT
CTGGTACCCTCCGAGCTCATCTCCGCCGTACCGACCACAAAAAGCAATCATGGTGGCATA
GCATCTGAGTCACTTGCGGGTGGCCTAGTGGAGGAGAAGGTGGGATCCCATCCAGAACTT
CTACCCAGCATAGCCCCGTCGCAGAATTTAGTCTCAAAGGAAACTTCAACCACAGCACTG
CAGGCCTCTGTTGCCAGACCAGAGCTGGAGGTAAATGCTGCCATAGTCTCTGGACAAAGC
AGTGAGCCCAAAGAGATAGTTGAAAAGTCCAAAATCCCAGGCCGAAGAAACTCCCGAACT
GAAGAGCCAACTGTGGCCTCTGAAAGTGTGGAAAATGGACATCGTAAACGATCTTCTCGA
CCTGCTTCAGCCTCCAGCTCTACTAAAGACATAACCAGTGCGGTGCAATCCAAGCGAAGA
AAATCCAAGTAA
Enzyme 8 GenBank Gene ID AF128458 Link Image
Enzyme 8 GeneCard ID NCOA6 Link Image
Enzyme 8 GenAtlas ID NCOA6 Link Image
Enzyme 8 HGNC ID HGNC:15936 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 20q11
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed Link Image]
  2. Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed Link Image]
  3. Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed Link Image]
  4. Ko L, Cardona GR, Chin WW: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6212-7. [PubMed Link Image]
  5. Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N: Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1996 Feb 29;3(1):17-24. [PubMed Link Image]
  6. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  7. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Zhu Y, Qi C, Cao WQ, Yeldandi AV, Rao MS, Reddy JK: Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function. Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10380-5. Epub 2001 Aug 21. [PubMed Link Image]
  10. Iwasaki T, Chin WW, Ko L: Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM). J Biol Chem. 2001 Sep 7;276(36):33375-83. Epub 2001 Jul 6. [PubMed Link Image]
  11. Qi C, Chang J, Zhu Y, Yeldandi AV, Rao SM, Zhu YJ: Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J Biol Chem. 2002 Aug 9;277(32):28624-30. Epub 2002 May 30. [PubMed Link Image]
  12. Mahajan MA, Murray A, Samuels HH: NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC. Mol Cell Biol. 2002 Oct;22(19):6883-94. [PubMed Link Image]
  13. Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW: Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol Cell Biol. 2003 Jan;23(1):140-9. [PubMed Link Image]
  14. Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW: Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs. Mol Endocrinol. 2002 Jan;16(1):128-40. [PubMed Link Image]
  15. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  16. Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed Link Image]
  17. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 17106
Enzyme 9 Name cDNA FLJ51539, highly similar to Vitamin D3 receptor
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name Not Available
Enzyme 9 Protein Sequence >cDNA FLJ51539, highly similar to Vitamin D3 receptor
MSMEHAALTATGAGGSWRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKE
FILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQ
FRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDS
DDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIM
LRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVL
LMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRS
LNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS
Enzyme 9 Number of Residues 395
Enzyme 9 Molecular Weight 44678.6
Enzyme 9 Theoretical pI 6.51
Enzyme 9 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 9 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 194388804 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID B4DRV7 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B4DRV7_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1188 bp
ATGTCCATGGAACATGCGGCGCTCACAGCCACAGGAGCAGGAGGGTCTTGGCGAAGCATG
AAGCGGAAGGCACTATTCACCTGCCCCTTCAACGGGGACTGCCGCATCACCAAGGACAAC
CGACGCCACTGCCAGGCCTGCCGGCTCAAACGCTGTGTGGACATCGGCATGATGAAGGAG
TTCATTCTGACAGATGAGGAAGTGCAGAGGAAGCGGGAGATGATCCTGAAGCGGAAGGAG
GAGGAGGCCTTGAAGGACAGTCTGCGGCCCAAGCTGTCTGAGGAGCAGCAGCGCATCATT
GCCATACTGCTGGACGCCCACCATAAGACCTACGACCCCACCTACTCCGACTTCTGCCAG
TTCCGGCCTCCAGTTCGTGTGAATGATGGTGGAGGGAGCCATCCTTCCAGGCCCAACTCC
AGACACACTCCCAGCTTCTCTGGGGACTCCTCCTCCTCCTGCTCAGATCACTGTATCACC
TCTTCAGACATGATGGACTCGTCCAGCTTCTCCAATCTGGATCTGAGTGAAGAAGATTCA
GATGACCCTTCTGTGACCCTAGAGCTGTCCCAGCTCTCCATGCTGCCCCACCTGGCTGAC
CTGGTCAGTTACAGCATCCAAAAGGTCATTGGCTTTGCTAAGATGATACCAGGATTCAGA
GACCTCACCTCTGAGGACCAGATCGTACTGCTGAAGTCAAGTGCCATTGAGGTCATCATG
TTGCGCTCCAATGAGTCCTTCACCATGGACGACATGTCCTGGACCTGTGGCAACCAAGAC
TACAAGTACCGCGTCAGTGACGTGACCAAAGCCGGACACAGCCTGGAGCTGATTGAGCCC
CTCATCAAGTTCCAGGTGGGACTGAAGAAGCTGAACTTGCATGAGGAGGAGCATGTCCTG
CTCATGGCCATCTGCATCGTCTCCCCAGATCGTCCTGGGGTGCAGGACGCCGCGCTGATT
GAGGCCATCCAGGACCGCCTGTCCAACACACTGCAGACGTACATCCGCTGCCGCCACCCG
CCCCCGGGCAGCCACCTGCTCTATGCCAAGATGATCCAGAAGCTAGCCGACCTGCGCAGC
CTCAATGAGGAGCACTCCAAGCAGTACCGCTGCCTCTCCTTCCAGCCTGAGTGCAGCATG
AAGCTAACGCCCCTTGTGCTCGAAGTGTTTGGCAATGAGATCTCCTGA
Enzyme 9 GenBank Gene ID AK299446 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID HGNC:12679 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs Not Available
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available