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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1NCOA1: 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)
染色体(2番染色体 (ヒト))[1]
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)
染色体12番染色体 (マウス)[2]
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 transferase activity
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
ヒトマウス
Entrez
Ensembl
UniProt
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

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

  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

参考文献

  • “Peroxisome proliferator-activated receptors, coactivators, and downstream targets”. (Cell Biochemistry and Biophysics). 32 Spring (1–3): 187–204. (2001). doi:10.1385/cbb:32:1-3:187. PMID (11330046). 
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