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Enzyme 1
[top]
|
| Enzyme 1 ID |
5255 |
| Enzyme 1 Name |
Nuclear receptor coactivator 3 |
| Enzyme 1 Synonyms |
- NCoA-3
- ACTR
- Amplified in breast cancer 1 protein
- AIB-1
- CBP-interacting protein
- pCIP
- Class E basic helix-loop-helix protein 42
- bHLHe42
- Receptor-associated coactivator 3
- RAC-3
- Steroid receptor coactivator protein 3
- SRC-3
- Thyroid hormone receptor activator molecule 1
- 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
32307126  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9Y6Q9  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NCOA3_HUMAN  |
| Enzyme 1 PDB ID |
1KBH  |
| 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  |
| Enzyme 1 GeneCard ID |
NCOA3  |
| Enzyme 1 GenAtlas ID |
NCOA3  |
| Enzyme 1 HGNC ID |
HGNC:7670  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
20q12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
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| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
|
| Enzyme 2 ID |
6325 |
| Enzyme 2 Name |
Sterol 26-hydroxylase, mitochondrial |
| Enzyme 2 Synonyms |
- 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
- Cytochrome P-450C27/25
- Cytochrome P450 27
- Sterol 27-hydroxylase
- 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q02318  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CP27A_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
CYP27A1  |
| Enzyme 2 GenAtlas ID |
CYP27A1  |
| Enzyme 2 HGNC ID |
HGNC:2605  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
2q33-qter |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- 25-OHD-1 alpha-hydroxylase
- 25-hydroxyvitamin D(3) 1-alpha-hydroxylase
- VD3 1A hydroxylase
- Calcidiol 1-monooxygenase
- Cytochrome P450 subfamily XXVIIB polypeptide 1
- Cytochrome P450C1 alpha
- Cytochrome P450VD1-alpha
- 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O15528  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CP27B_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
CYP27B1  |
| Enzyme 3 GenAtlas ID |
CYP27B1  |
| Enzyme 3 HGNC ID |
HGNC:2606  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
12q13.1-q13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
7156 |
| Enzyme 4 Name |
Vitamin D3 receptor |
| Enzyme 4 Synonyms |
- VDR
- 1,25-dihydroxyvitamin D3 receptor
- 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
340203  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P11473  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
VDR_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
VDR  |
| Enzyme 4 GenAtlas ID |
VDR  |
| Enzyme 4 HGNC ID |
HGNC:12679  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
12q13.11 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- 24-OHase
- Vitamin D(3) 24-hydroxylase
- Cytochrome P450 24A1
- 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
7939322  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q07973  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
CP24A_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
CYP24A1  |
| Enzyme 5 GenAtlas ID |
CYP24A1  |
| Enzyme 5 HGNC ID |
HGNC:2602  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
20q13 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8179 |
| Enzyme 6 Name |
Vitamin D 25-hydroxylase |
| Enzyme 6 Synonyms |
- 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
33591222  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q6VVX0  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
CP2R1_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
CYP2R1  |
| Enzyme 6 GenAtlas ID |
CYP2R1  |
| Enzyme 6 HGNC ID |
HGNC:20580  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
11p15.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- RNA polymerase II TBP-associated factor subunit C
- TBP-associated factor 4
- Transcription initiation factor TFIID 130 kDa subunit
- TAF(II)130
- TAFII-130
- TAFII130
- Transcription initiation factor TFIID 135 kDa subunit
- TAF(II)135
- TAFII-135
- 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
56204142  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O00268  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
TAF4_HUMAN  |
| Enzyme 7 PDB ID |
1H3O  |
| 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  |
| Enzyme 7 GeneCard ID |
TAF4  |
| Enzyme 7 GenAtlas ID |
TAF4  |
| Enzyme 7 HGNC ID |
HGNC:11537  |
| Enzyme 7 Chromosome Location |
2 |
| Enzyme 7 Locus |
20q13.33 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- 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
]
- Damania B, Alwine JC: TAF-like function of SV40 large T antigen. Genes Dev. 1996 Jun 1;10(11):1369-81. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
17105 |
| Enzyme 8 Name |
Nuclear receptor coactivator 6 |
| Enzyme 8 Synonyms |
- Activating signal cointegrator 2
- ASC-2
- Amplified in breast cancer protein 3
- Cancer-amplified transcriptional coactivator ASC-2
- Nuclear receptor coactivator RAP250
- NRC RAP250
- Nuclear receptor-activating protein, 250 kDa
- Peroxisome proliferator-activated receptor-interacting protein
- PPAR-interacting protein
- PRIP
- 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
7140574  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q14686  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NCOA6_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
NCOA6  |
| Enzyme 8 GenAtlas ID |
NCOA6  |
| Enzyme 8 HGNC ID |
HGNC:15936  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
20q11 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
194388804  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B4DRV7  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B4DRV7_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
Not Available |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
HGNC:12679  |
| 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 |