NCOA6

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Nuclear receptor coactivator 6
Identifiers
Symbol(s) NCOA6; HOXA7; ANTP; HOX1.1; PRIP; TRBP; AIB3; ASC2; KIAA0181; NRC; RAP250
External IDs OMIM: 605299 MGI: 1929915 HomoloGene: 40920
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 23054 56406
Ensembl ENSG00000198646 ENSMUSG00000038369
Uniprot Q14686 Q3TAG3
Refseq NM_014071 (mRNA)
NP_054790 (protein)		 NM_019825 (mRNA)
NP_062799 (protein)
Location Chr 20: 32.77 - 32.88 Mb Chr 2: 155.08 - 155.13 Mb
Pubmed search [1] [2]

Nuclear receptor coactivator 6, also known as NCOA6, is a human gene.[1]

The protein encoded by this gene is a transcriptional coactivator that can interact with nuclear hormone receptors to enhance their transcriptional activator functions. The encoded protein has been shown to be involved in the hormone-dependent coactivation of several receptors, including prostanoid, retinoid, vitamin D3, thyroid hormone, and steroid receptors. The encoded protein may also act as a general coactivator since it has been shown to interact with some basal transcription factors, histone acetyltransferases, and methyltransferases.[1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: NCOA6 nuclear receptor coactivator 6.

[edit] Further reading

  • Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954. 
  • Carney JP, McKnight C, VanEpps S, Kelley MR (1995). "Random rapid amplification of cDNA ends (RRACE) allows for cloning of multiple novel human cDNA fragments containing (CAG)n repeats.". Gene 155 (2): 289–92. PMID 7536696. 
  • Nagase T, Seki N, Ishikawa K, et al. (1996). "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. 3 (1): 17–24. PMID 8724849. 
  • Guan XY, Xu J, Anzick SL, et al. (1996). "Hybrid selection of transcribed sequences from microdissected DNA: isolation of genes within amplified region at 20q11-q13.2 in breast cancer.". Cancer Res. 56 (15): 3446–50. PMID 8758910. 
  • Lee SK, Anzick SL, Choi JE, et al. (1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo.". J. Biol. Chem. 274 (48): 34283–93. PMID 10567404. 
  • Caira F, Antonson P, Pelto-Huikko M, et al. (2000). "Cloning and characterization of RAP250, a novel nuclear receptor coactivator.". J. Biol. Chem. 275 (8): 5308–17. PMID 10681503. 
  • Zhu Y, Kan L, Qi C, et al. (2000). "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.". J. Biol. Chem. 275 (18): 13510–6. PMID 10788465. 
  • Ko L, Cardona GR, Chin WW (2000). "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator.". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 6212–7. PMID 10823961. 
  • Lee SK, Na SY, Jung SY, et al. (2000). "Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2.". Mol. Endocrinol. 14 (6): 915–25. PMID 10847592. 
  • Mahajan MA, Samuels HH (2000). "A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein.". Mol. Cell. Biol. 20 (14): 5048–63. PMID 10866662. 
  • Lee SK, Jung SY, Kim YS, et al. (2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2.". Mol. Endocrinol. 15 (2): 241–54. PMID 11158331. 
  • Hong S, Lee MY, Cheong J (2001). "Functional interaction of transcriptional coactivator ASC-2 and C/EBPalpha in granulocyte differentiation of HL-60 promyelocytic cell.". Biochem. Biophys. Res. Commun. 282 (5): 1257–62. doi:10.1006/bbrc.2001.4727. PMID 11302752. 
  • Iwasaki T, Chin WW, Ko L (2001). "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. 276 (36): 33375–83. doi:10.1074/jbc.M101517200. PMID 11443112. 
  • Zhu Y, Qi C, Cao WQ, et al. (2001). "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. 98 (18): 10380–5. doi:10.1073/pnas.181347498. PMID 11517327. 
  • Jung DJ, Na SY, Na DS, Lee JW (2002). "Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors.". J. Biol. Chem. 277 (2): 1229–34. doi:10.1074/jbc.M110417200. PMID 11704680. 
  • Ko L, Cardona GR, Iwasaki T, et al. (2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs.". Mol. Endocrinol. 16 (1): 128–40. PMID 11773444. 
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052. 
  • Qi C, Chang J, Zhu Y, et al. (2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha.". J. Biol. Chem. 277 (32): 28624–30. doi:10.1074/jbc.M201053200. PMID 12039952. 
  • Espejo F, Green M, Preece NE, Assa-Munt N (2003). "NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.". J. Biomol. NMR 23 (2): 151–2. PMID 12153040. 

[edit] External links

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v • d • e
Transcription coregulators
Coactivators
ARA54 - ARA55 - CARM1 - CRTC1 - CRTC2 - CBP - PPARGC1A - PPARGC1B - TGFB1I1
NCOA1 (SRC-1) - NCOA2 (GRIP1/SRC-2/TIF2) - NCOA3 (AIB/SRC-3/TRAM-1) - NCOA4 (ARA70) - NCOA5 (CIA) - NCOA6 (RAP250) - NCOA7 (ERAP140)
Corepressors
Hairless homolog - NRIP1 - PELP-1 - RCOR1 - Rb - SIN3A - SIN3B - Tripartite motif-containing (TRIM24, TRIM28, TRIM33)
NCOR1 - NCOR2 (SMRT)
ATP-dependent remodeling factors