Biology:NCOA6
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.[1][2][3]
Function
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
NCOA6 has been shown to interact with:
- ASCL2[4] and
- Activating transcription factor 2,[5]
- Androgen receptor,[6]
- CREB-binding protein,[7][8]
- DNA-PKcs,[9]
- E2F1,[10]
- EP300,[9]
- Estrogen receptor alpha,[7][11]
- Estrogen receptor beta,[8][11]
- HBXIP,[12]
- HIST2H3C,[4]
- HSF1,[13]
- Ku70,[9][14]
- Ku80,[9][14]
- Liver X receptor beta,[8]
- MLL3,[4]
- RBBP5,[4]
- Retinoblastoma protein,[6]
- Retinoic acid receptor alpha,[7][8][9]
- Retinoid X receptor alpha,[7][8][11][12]
- Src,[4][7][8][15]
- TGS1,[16][17]
- TUBA4A,[4]
- TUBB,[4]
- Thyroid hormone receptor alpha,[7][15] and
- Thyroid hormone receptor beta.[7][8][9][11]
See also
References
- ↑ "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. November 1996. doi:10.1093/dnares/3.1.17. PMID 8724849.
- ↑ "Evaluation of a patient information booklet". J Nurs Staff Dev 9 (6): 278–82. January 1994. PMID 8263591.
- ↑ 3.0 3.1 "Entrez Gene: NCOA6 nuclear receptor coactivator 6". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23054.
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 4.6 "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. January 2003. doi:10.1128/mcb.23.1.140-149.2003. PMID 12482968.
- ↑ "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. April 2004. doi:10.1074/jbc.M311752200. PMID 14734562.
- ↑ 6.0 6.1 "Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation". J. Biol. Chem. 279 (8): 7131–5. February 2004. doi:10.1074/jbc.M312563200. PMID 14645241.
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 "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. November 1999. doi:10.1074/jbc.274.48.34283. PMID 10567404.
- ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. February 2001. doi:10.1210/mend.15.2.0595. PMID 11158331.
- ↑ 9.0 9.1 9.2 9.3 9.4 9.5 "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. May 2000. doi:10.1073/pnas.97.11.6212. PMID 10823961. Bibcode: 2000PNAS...97.6212K.
- ↑ "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. November 2003. PMID 14638867.
- ↑ 11.0 11.1 11.2 11.3 "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. January 2002. doi:10.1210/mend.16.1.0755. PMID 11773444.
- ↑ 12.0 12.1 "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology 38 (5): 1258–66. November 2003. doi:10.1053/jhep.2003.50451. PMID 14578865.
- ↑ "Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock". FEBS Lett. 559 (1–3): 165–70. February 2004. doi:10.1016/S0014-5793(04)00028-6. PMID 14960326.
- ↑ 14.0 14.1 "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. March 2003. doi:10.1074/jbc.M209723200. PMID 12519782.
- ↑ 15.0 15.1 "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. June 2000. doi:10.1210/mend.14.6.0471. PMID 10847592.
- ↑ "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. May 2002. doi:10.1074/jbc.M201739200. PMID 11912212.
- ↑ "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. August 2001. doi:10.1073/pnas.181347498. PMID 11517327. Bibcode: 2001PNAS...9810380Z.
Further reading
- "A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein". Mol. Cell. Biol. 20 (14): 5048–63. July 2000. doi:10.1128/MCB.20.14.5048-5063.2000. PMID 10866662.
- "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. 2003. doi:10.1093/dnares/9.3.99. PMID 12168954.
- "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. 1995. doi:10.1016/0378-1119(94)00758-K. PMID 7536696.
- "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. 1996. PMID 8758910.
- "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. 1999. doi:10.1074/jbc.274.48.34283. PMID 10567404.
- "Cloning and characterization of RAP250, a novel nuclear receptor coactivator". J. Biol. Chem. 275 (8): 5308–17. 2000. doi:10.1074/jbc.275.8.5308. PMID 10681503.
- "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR". J. Biol. Chem. 275 (18): 13510–6. 2000. doi:10.1074/jbc.275.18.13510. PMID 10788465.
- "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. 2000. doi:10.1073/pnas.97.11.6212. PMID 10823961. Bibcode: 2000PNAS...97.6212K.
- "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. 2000. doi:10.1210/mend.14.6.0471. PMID 10847592.
- "A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein". Mol. Cell. Biol. 20 (14): 5048–63. 2000. doi:10.1128/MCB.20.14.5048-5063.2000. PMID 10866662.
- "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. 2001. doi:10.1210/mend.15.2.0595. PMID 11158331.
- "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. 2001. doi:10.1006/bbrc.2001.4727. PMID 11302752.
- "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. 2001. doi:10.1074/jbc.M101517200. PMID 11443112.
- "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. 2001. doi:10.1073/pnas.181347498. PMID 11517327. Bibcode: 2001PNAS...9810380Z.
- "Molecular cloning and characterization of CAPER, a novel coactivator of activating protein-1 and estrogen receptors". J. Biol. Chem. 277 (2): 1229–34. 2002. doi:10.1074/jbc.M110417200. PMID 11704680.
- "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. 2002. doi:10.1210/mend.16.1.0755. PMID 11773444.
- "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. 277 (32): 28624–30. 2002. doi:10.1074/jbc.M201053200. PMID 12039952.
- "NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation". J. Biomol. NMR 23 (2): 151–2. 2003. doi:10.1023/A:1016398403157. PMID 12153040.
External links
- NCOA6 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- NURSA C94
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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