NCOA6

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Nuclear receptor coactivator 6
Identifiers
Symbols NCOA6 ; AIB3; ASC2; NRC; PRIP; RAP250; TRBP
External IDs OMIM605299 MGI1929915 HomoloGene40920 GeneCards: NCOA6 Gene
RNA expression pattern
PBB GE NCOA6 208979 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 23054 56406
Ensembl ENSG00000198646 ENSMUSG00000038369
UniProt Q14686 A2AQM9
RefSeq (mRNA) NM_001242539 NM_001242558
RefSeq (protein) NP_001229468 NP_001229487
Location (UCSC) Chr 20:
33.28 – 33.41 Mb
Chr 2:
155.39 – 155.47 Mb
PubMed search [1] [2]

Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.[1][2][3]

Function[edit]

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.[3]

Interactions[edit]

NCOA6 has been shown to interact with:

See also[edit]


References[edit]

  1. ^ Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (November 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. doi:10.1093/dnares/3.1.17. PMID 8724849. 
  2. ^ Estey A, Kemp M, Allison S, Lamb C (January 1994). "Evaluation of a patient information booklet". J Nurs Staff Dev 9 (6): 278–82. PMID 8263591. 
  3. ^ a b "Entrez Gene: NCOA6 nuclear receptor coactivator 6". 
  4. ^ a b c d e f g 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 (January 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–9. doi:10.1128/mcb.23.1.140-149.2003. PMC 140670. PMID 12482968. 
  5. ^ Hong S, Choi HM, Park MJ, Kim YH, Choi YH, Kim HH, Choi YH, Cheong J (April 2004). "Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid". J. Biol. Chem. 279 (17): 16996–7003. doi:10.1074/jbc.M311752200. PMID 14734562. 
  6. ^ a b Goo YH, Na SY, Zhang H, Xu J, Hong S, Cheong J, Lee SK, Lee JW (February 2004). "Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation". J. Biol. Chem. 279 (8): 7131–5. doi:10.1074/jbc.M312563200. PMID 14645241. 
  7. ^ a b c d e f g 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 (November 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. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  8. ^ a b c d e f g Lee SK, Jung SY, Kim YS, Na SY, Lee YC, Lee JW (February 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. doi:10.1210/me.15.2.241. PMID 11158331. 
  9. ^ a b c d e f Ko L, Cardona GR, Chin WW (May 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. doi:10.1073/pnas.97.11.6212. PMC 18584. PMID 10823961. 
  10. ^ Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG, Lee JW, Cheong J (November 2003). "Interaction and functional cooperation of the cancer-amplified transcriptional coactivator activating signal cointegrator-2 and E2F-1 in cell proliferation". Mol. Cancer Res. 1 (13): 948–58. PMID 14638867. 
  11. ^ a b c d Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW (January 2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. doi:10.1210/mend.16.1.0755. PMID 11773444. 
  12. ^ a b Kong HJ, Park MJ, Hong S, Yu HJ, Lee YC, Choi YH, Cheong J (November 2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology 38 (5): 1258–66. doi:10.1053/jhep.2003.50451. PMID 14578865. 
  13. ^ Hong S, Kim SH, Heo MA, Choi YH, Park MJ, Yoo MA, Kim HD, Kang HS, Cheong J (February 2004). "Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock". FEBS Lett. 559 (1-3): 165–70. doi:10.1016/S0014-5793(04)00028-6. PMID 14960326. 
  14. ^ a b Ko L, Chin WW (March 2003). "Nuclear receptor coactivator thyroid hormone receptor-binding protein (TRBP) interacts with and stimulates its associated DNA-dependent protein kinase". J. Biol. Chem. 278 (13): 11471–9. doi:10.1074/jbc.M209723200. PMID 12519782. 
  15. ^ a b Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW (June 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. doi:10.1210/mend.14.6.0471. PMID 10847592. 
  16. ^ Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK (May 2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212. 
  17. ^ Zhu Y, Qi C, Cao WQ, Yeldandi AV, Rao MS, Reddy JK (August 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. PMC 56969. PMID 11517327. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.