NCOA6
Protein-coding gene in the species Homo sapiens
title: "NCOA6" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["gene-expression", "transcription-coregulators", "human-proteins"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/gene-expression" source: "https://en.wikipedia.org/wiki/NCOA6" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0
::summary Protein-coding gene in the species Homo sapiens ::
Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.
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.
Interactions
NCOA6 has been shown to interact with:
- ASCL2 and
- Activating transcription factor 2,
- Androgen receptor,
- CREB-binding protein,
- DNA-PKcs,
- E2F1,
- EP300,
- Estrogen receptor alpha,
- Estrogen receptor beta,
- HBXIP,
- HIST2H3C,
- HSF1,
- Ku70,
- Ku80,
- Liver X receptor beta,
- MLL3,
- RBBP5,
- Retinoblastoma protein,
- Retinoic acid receptor alpha,
- Retinoid X receptor alpha,
- Src,
- TGS1,
- TUBA4A,
- TUBB,
- Thyroid hormone receptor alpha, and
- Thyroid hormone receptor beta.
References
References
- (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.
- (January 1994). "Evaluation of a patient information booklet". J Nurs Staff Dev.
- "Entrez Gene: NCOA6 nuclear receptor coactivator 6".
- (April 2004). "Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid". J. Biol. Chem..
- (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..
- (February 2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol..
- (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..
- (November 2003). "Hepatitis B virus X protein regulates transactivation activity and protein stability of the cancer-amplified transcription coactivator ASC-2". Hepatology.
- (February 2004). "Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock". FEBS Lett..
- (May 2000). "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator". Proc. Natl. Acad. Sci. U.S.A..
- (March 2003). "Nuclear receptor coactivator thyroid hormone receptor-binding protein (TRBP) interacts with and stimulates its associated DNA-dependent protein kinase". J. Biol. Chem..
- (January 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol..
- (February 2004). "Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation". J. Biol. Chem..
- (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..
- (May 2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem..
- (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..
- (January 2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol..
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