Wikipedia

核内受容体コアクチベーター1

核内受容体コアクチベーター1 （NCOA1: nuclear receptor coactivator 1）は、いくつかの核内受容体相互作用ドメインと固有のヒストンアセチルトランスフェラーゼ活性を含む転写共調節タンパク質である。 NCOA1は、リガンドで活性化される核内受容体によってDNAプロモーター部位に動員される。次に、NCOA1はヒストンをアシル化し、下流のDNAを転写しやすくする。したがって、NCOA1はDNA発現の上方調節において核内受容体を援助する[5][6]。

NCOA1
PDBに登録されている構造
PDBオルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧

1FM6, 1FM9, 1K74, 1K7L, 1KV6, 1K4W, 1N4H, 1NQ7, 1NRL, 1P8D, 1PZL, 1RDT, 1TFC, 1U3R, 1U3S, 1X76, 1XIU, 1XV9, 1XVP, 1YY4, 1ZAF, 2A3I, 2C52, 2FVJ, 2GTK, 2HBH, 2HC4, 2HCD, 2HFP, 2NPA, 2NV7, 2P54, 2PRG, 3BEJ, 3BQD, 3CTB, 3CWD, 3DCT, 3DCU, 3DR1, 3ET1, 3ET3, 3FEI, 3FEJ, 3FUR, 3FXV, 3G8I, 3G9E, 3GYT, 3GYU, 3H0A, 3HC5, 3HC6, 3HVL, 3IPQ, 3IPS, 3IPU, 3KMR, 3LMP, 3OKH, 3OKI, 3OLF, 3OLL, 3OLS, 3OMK, 3OMM, 3OMO, 3OMP, 3OMQ, 3OOF, 3OOK, 3P88, 3P89, 3QT0, 3RUT, 3RUU, 3RVF, 3S9S, 3T03, 3UU7, 3UUA, 3UUD, 3V9Y, 3VN2, 4DK7, 4DK8, 4DM6, 4DM8, 4DQM, 4F9M, 4FGY, 4G1D, 4G1Y, 4G1Z, 4G20, 4G21, 4G2H, 4HEE, 4J5X, 4JYG, 4JYH, 4JYI, 4MG5, 4MG6, 4MG7, 4MG8, 4MG9, 4MGA, 4MGB, 4MGC, 4MGD, 4TUZ, 4TV1, 5AVI, 5AVL, 4Y29, 4RUJ, 4RUP, 5A86, 5E7V, 4UDB, 4UDA, 5AZT, 5HJS

識別子
記号NCOA1, F-SRC-1, KAT13A, RIP160, SRC1, bHLHe42, bHLHe74, nuclear receptor coactivator 1
外部IDOMIM: 602691 MGI: 1276523 HomoloGene: 7859 GeneCards: NCOA1
遺伝子の位置 (ヒト)
2番染色体 (ヒト)
染色体2番染色体 (ヒト)[1]
2番染色体 (ヒト)
NCOA1遺伝子の位置
NCOA1遺伝子の位置
バンドデータ無し開始点24,491,254 bp[1]
終点24,770,702 bp[1]
遺伝子の位置 (マウス)
12番染色体 (マウス)
染色体12番染色体 (マウス)[2]
12番染色体 (マウス)
NCOA1遺伝子の位置
NCOA1遺伝子の位置
バンドデータ無し開始点4,247,362 bp[2]
終点4,477,182 bp[2]
RNA発現パターン




さらなる参照発現データ
遺伝子オントロジー
分子機能• トランスフェラーゼ活性
• DNA結合
• transcription coactivator activity
• protein dimerization activity
• protein N-terminus binding
• 転写因子結合
• クロマチン結合
• histone acetyltransferase activity
• 血漿タンパク結合
• androgen receptor binding
• 酵素結合
• acyltransferase activity
• nuclear receptor coactivator activity
• aryl hydrocarbon receptor binding
• nuclear receptor binding
• estrogen receptor binding
• DNA-binding transcription factor activity, RNA polymerase II-specific
• progesterone receptor binding
• retinoic acid receptor binding
• protein-containing complex binding
• retinoid X receptor binding
細胞の構成要素• 細胞核
• 核質
• 細胞質基質
• 細胞膜
• 高分子複合体
• 細胞質
• neuron projection
生物学的プロセス• androgen receptor signaling pathway
• regulation of RNA biosynthetic process
• regulation of transcription, DNA-templated
• cellular response to Thyroglobulin triiodothyronine
• regulation of cellular response to drug
• transcription, DNA-templated
• positive regulation of transcription, DNA-templated
• labyrinthine layer morphogenesis
• positive regulation of neuron differentiation
• bile acid and bile salt transport
• positive regulation of apoptotic process
• histone H4 acetylation
• regulation of thyroid hormone mediated signaling pathway
• positive regulation of transcription by RNA polymerase II
• intracellular receptor signaling pathway
• positive regulation of transcription from RNA polymerase II promoter by galactose
• regulation of lipid metabolic process
• transcription by RNA polymerase II
• cellular response to hormone stimulus
• 授乳
• 男性生殖腺発生
• ホルモンへの反応
• 小脳発生
• 海馬発生
• 視床下部発生
• 大脳皮質発生
• エストラジオールへの反応
• response to retinoic acid
• response to progesterone
• 発情周期
• positive regulation of female receptivity
• male mating behavior
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

8648

17977

Ensembl

ENSG00000084676

ENSMUSG00000020647

UniProt

Q15788

P70365

RefSeq
(mRNA)
NM_003743
NM_147223
NM_147233
NM_001362950
NM_001362952

NM_001362954
NM_001362955

NM_010881

RefSeq
(タンパク質)
NP_003734
NP_671756
NP_671766
NP_001349879
NP_001349881

NP_001349883
NP_001349884

NP_035011

場所
(UCSC)		Chr 2: 24.49 – 24.77 MbChr 2: 4.25 – 4.48 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

NCOA1は、ステロイド受容体コアクチベーター1（SRC-1: steroid receptor coactivator-1）と同一である。

相互作用分子

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NCOA1は、塩基性ヘリックスループヘリックス（bHLH）ドメインを有しており、以下の生体分子と相互作用することができる。

脚注

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084676 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020647 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ Sergio A. Oñate, Sophia Y. Tsai, Ming-Jer Tsai, Bert W. O'Malley (24 Nov 1995). “Sequence and characterization of a coactivator for the steroid hormone receptor superfamily”. Science 270 (5240): 1354–1357. doi:10.1126/science.270.5240.1354. PMID 7481822. 
  6. ^ Sergio A. Onate, Viroj Boonyaratanakornkit, Thomas E. Spencer, Sophia Y. Tsai, Dean P. Edwards, Bert W. O'Malley (15 May 1998). “The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors”. Journal of Biological Chemistry 273 (20): 12101–12108. doi:10.1074/jbc.273.20.12101. PMID 9575154. 
  7. ^ “Recruitment of beta-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells”. Molecular Endocrinology 18 (10): 2388–2401. (1 October 2004). doi:10.1210/me.2003-0436. PMID 15256534. 
  8. ^ “Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells”. Journal of Biological Chemistry 277 (41): 38087–38094. (11 October 2002). doi:10.1074/jbc.M203313200. PMID 12163482. 
  9. ^ “The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1”. Molecular and Cellular Biology 19 (12): 8383–8392. (Dec 1999). doi:10.1128/mcb.19.12.8383. PMC 84931. PMID 10567563. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84931/. 
  10. ^ a b c “Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2”. Molecular Endocrinology 14 (6): 915–925. (1 June 2000). doi:10.1210/mend.14.6.0471. PMID 10847592. 
  11. ^ a b “Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits”. Journal of Biological Chemistry 273 (27): 16651–16654. (1998 Jul 3). doi:10.1074/jbc.273.27.16651. PMID 9642216. 
  12. ^ “A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo”. Journal of Biological Chemistry 274 (48): 34283–34293. (26 November 1999). doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  13. ^ “Steroid receptor coactivator 1 links the steroid and interferon gamma response pathways”. Molecular Endocrinology 17 (12): 2509–2518. (01 December 2003). doi:10.1210/me.2002-0439. PMID 12933903. 
  14. ^ a b “Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1”. Molecular and Cellular Biology 21 (1): 39–50. (2001 Jan). doi:10.1128/MCB.21.1.39-50.2001. PMC 86566. PMID 11113179. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86566/. 
  15. ^ “Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase”. Molecular and Cellular Biology 22 (10): 3549–3461. (May 2002). doi:10.1128/MCB.22.10.3549-3561.2002. PMC 133790. PMID 11971985. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC133790/. 
  16. ^ “Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1”. Genes & Development 12 (22): 3488–3498. (1998 Nov 15). doi:10.1101/gad.12.22.3488. PMC 317237. PMID 9832502. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC317237/. 
  17. ^ a b c “A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA”. EMBO Journal 20 (6): 1341–1352. (15 March 2001). doi:10.1093/emboj/20.6.1341. PMC 145523. PMID 11250900. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC145523/. 
  18. ^ “BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation”. Molecular and Cellular Biology 20 (20): 7541–7549. (Oct 2000). doi:10.1128/MCB.20.20.7541-7549.2000. PMC 86306. PMID 11003650. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC86306/. 
  19. ^ “Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor”. EMBO Journal 17 (1): 232–243. (1998 Jan 2). doi:10.1093/emboj/17.1.232. PMC 1170374. PMID 9427757. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170374/. 
  20. ^ “The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro”. Proceedings of the National Academy of Sciences, USA 99 (5): 2642–2647. (March 5, 2002). doi:10.1073/pnas.261715899. PMC 122401. PMID 11867769. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC122401/. 
  21. ^ “Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140”. Molecular Endocrinology 15 (4): 501–511. (1 April 2001). doi:10.1210/mend.15.4.0624. PMID 11266503. 
  22. ^ “A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1”. Journal of Biological Chemistry 277 (29): 26098–260102. (2002 Jul 19). doi:10.1074/jbc.M204013200. PMID 12118039. 
  23. ^ “Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations”. Journal of Biological Chemistry 273 (18): 10831–10834. (1998 May 1). doi:10.1074/jbc.273.18.10831. PMID 9556555. 
  24. ^ “Steroid receptor coactivator-1 is a histone acetyltransferase”. Nature 389 (6647): 194–198. (11 September 1997). doi:10.1038/38304. PMID 9296499. 
  25. ^ “Activation of PPARgamma coactivator-1 through transcription factor docking”. Science 286 (5443): 1368–1371. (12 Nov 1999). doi:10.1126/science.286.5443.1368. PMID 10558993. 
  26. ^ “p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha”. Journal of Biological Chemistry 272 (52): 33435–33443. (26 December 1997). doi:10.1074/jbc.272.52.33435. PMID 9407140. 
  27. ^ “A regulatory role for RIP140 in nuclear receptor activation”. Molecular Endocrinology 12 (6): 864–881. (01 June 1998). doi:10.1210/mend.12.6.0123. PMID 9626662. 
  28. ^ “Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription”. Journal of Biological Chemistry 276 (44): 40614–40620. (2 Nov 2001). doi:10.1074/jbc.M106263200. PMID 11514567. 
  29. ^ “Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a”. Journal of Biological Chemistry 277 (10): 8004–811. (8 Mar 2002). doi:10.1074/jbc.M111486200. PMID 11773079. 
  30. ^ “Transcriptional activation by STAT6 requires the direct interaction with NCoA-1”. Journal of Biological Chemistry 276 (49): 45713–45721. (7 Dec 2001). doi:10.1074/jbc.M108132200. PMID 11574547. 
  31. ^ “An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1”. Journal of Biological Chemistry 277 (39): 36052–36060. (27 Sep 2002). doi:10.1074/jbc.M203556200. PMID 12138096. 
  32. ^ “Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation”. Molecular and Cellular Biology 19 (9): 6323–6332. (Sep 1999). doi:10.1128/mcb.19.9.6323. PMC 84603. PMID 10454579. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84603/. 
  33. ^ “Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors”. Endocrinology 139 (10): 4197–4204. (1 Oct 1998). doi:10.1210/endo.139.10.6218. PMID 9751500. 
  34. ^ “Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor”. Molecular Endocrinology 11 (6): 755–767. (1 Jun 1997). doi:10.1210/mend.11.6.0003. PMID 9171239. 

外部リンク

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参考文献

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