関: steroid receptor coactivator 1

WordNet

of or relating to or constituting the nucleus of an atom; "nuclear physics"; "nuclear fission"; "nuclear forces"
(weapons) deriving destructive energy from the release of atomic energy; "nuclear war"; "nuclear weapons"; "atomic bombs" (同)atomic
constituting or like a nucleus; "annexation of the suburban fringe by the nuclear metropolis"; "the nuclear core of the congregation"
of or relating to or constituting the nucleus of a cell; "nuclear membrane"; "nuclear division"
a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response

PrepTutorEJDIC

『核の』,細胞核の / [『原子』]『核の』
=sense organ / 受信装置

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/08 18:37:30」(JST)

wiki en

The nuclear receptor coactivator 1 (NCOA1) is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity (EC 2.3.1.48). NCOA1 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA1, in turn, acylates histones, which makes downsteam DNA more accessible to transcription. Hence, NCOA1 assists nuclear receptors in the upregulation of DNA expression.^[1]^[2]

NCOA1 is also frequently called steroid receptor coactivator-1 (SRC-1).

Interactions

Nuclear receptor coactivator 1 possesses a basic helix-loop-helix (bHLH) domain and has been shown to interact with:

Androgen receptor,^[3]^[4]^[5]
C-Fos,^[6]^[7]
C-jun,^[6]^[7]^[8]
CIITA,^[9]
CREB-binding protein,^[10]^[11]
Cyclin D1,^[12]
DDX17,^[13]
DDX5^[13] and
Estrogen receptor alpha,^[13]^[10]^[14]^[15]^[16]
Glucocorticoid receptor,^[17]^[18]
NFKB1,^[6]^[19]
PCAF,^[20]
PPARGC1A,^[21]
Peroxisome proliferator-activated receptor alpha,^[22]^[23]
SNW1,^[24]
STAT3,^[25]
STAT6,^[26]^[27]
TRIP4,^[28] and
Thyroid hormone receptor beta.^[29]^[30]

References

^ Onate SA, Tsai SY, Tsai MJ, O'Malley BW (1995). "Sequence and characterization of a coactivator for the steroid hormone receptor superfamily". Science 270 (5240): 1354–7. doi:10.1126/science.270.5240.1354. PMID 7481822.
^ Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW (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". J Biol Chem 273 (20): 12101–8. doi:10.1074/jbc.273.20.12101. PMID 9575154.
^ Masiello D, Chen SY, Xu Y, Verhoeven MC, Choi E, Hollenberg AN, Balk SP (Oct 2004). "Recruitment of beta-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells". Mol. Endocrinol. 18 (10): 2388–401. doi:10.1210/me.2003-0436. PMID 15256534.
^ Ueda T, Mawji NR, Bruchovsky N, Sadar MD (Oct 2002). "Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells". J. Biol. Chem. 277 (41): 38087–94. doi:10.1074/jbc.M203313200. PMID 12163482.
^ Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG (Dec 1999). "The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1". Mol. Cell. Biol. 19 (12): 8383–92. PMC 84931. PMID 10567563.
^ ^a ^b ^c Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW (Jun 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.
^ ^a ^b Lee SK, Kim HJ, Na SY, Kim TS, Choi HS, Im SY, Lee JW (Jul 1998). "Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits". J. Biol. Chem. 273 (27): 16651–4. doi:10.1074/jbc.273.27.16651. PMID 9642216.
^ 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 (Nov 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.
^ Tzortzakaki E, Spilianakis C, Zika E, Kretsovali A, Papamatheakis J (Dec 2003). "Steroid receptor coactivator 1 links the steroid and interferon gamma response pathways". Mol. Endocrinol. 17 (12): 2509–18. doi:10.1210/me.2002-0439. PMID 12933903.
^ ^a ^b Sheppard HM, Harries JC, Hussain S, Bevan C, Heery DM (Jan 2001). "Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1". Mol. Cell. Biol. 21 (1): 39–50. doi:10.1128/MCB.21.1.39-50.2001. PMC 86566. PMID 11113179.
^ Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW (May 2002). "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase". Mol. Cell. Biol. 22 (10): 3549–61. doi:10.1128/MCB.22.10.3549-3561.2002. PMC 133790. PMID 11971985.
^ Zwijsen RM, Buckle RS, Hijmans EM, Loomans CJ, Bernards R (Nov 1998). "Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1". Genes Dev. 12 (22): 3488–98. doi:10.1101/gad.12.22.3488. PMC 317237. PMID 9832502.
^ ^a ^b ^c Watanabe M, Yanagisawa J, Kitagawa H, Takeyama K, Ogawa S, Arao Y, Suzawa M, Kobayashi Y, Yano T, Yoshikawa H, Masuhiro Y, Kato S (Mar 2001). "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 J. 20 (6): 1341–52. doi:10.1093/emboj/20.6.1341. PMC 145523. PMID 11250900.
^ DiRenzo J, Shang Y, Phelan M, Sif S, Myers M, Kingston R, Brown M (Oct 2000). "BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation". Mol. Cell. Biol. 20 (20): 7541–9. doi:10.1128/MCB.20.20.7541-7549.2000. PMC 86306. PMID 11003650.
^ Kalkhoven E, Valentine JE, Heery DM, Parker MG (Jan 1998). "Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor". EMBO J. 17 (1): 232–43. doi:10.1093/emboj/17.1.232. PMC 1170374. PMID 9427757.
^ Kang YK, Guermah M, Yuan CX, Roeder RG (Mar 2002). "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". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMC 122401. PMID 11867769.
^ Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (Apr 2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501–11. doi:10.1210/mend.15.4.0624. PMID 11266503.
^ Kucera T, Waltner-Law M, Scott DK, Prasad R, Granner DK (Jul 2002). "A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1". J. Biol. Chem. 277 (29): 26098–102. doi:10.1074/jbc.M204013200. PMID 12118039.
^ Na SY, Lee SK, Han SJ, Choi HS, Im SY, Lee JW (May 1998). "Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations". J. Biol. Chem. 273 (18): 10831–4. doi:10.1074/jbc.273.18.10831. PMID 9556555.
^ Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW (Sep 1997). "Steroid receptor coactivator-1 is a histone acetyltransferase". Nature 389 (6647): 194–8. doi:10.1038/38304. PMID 9296499.
^ Puigserver P, Adelmant G, Wu Z, Fan M, Xu J, O'Malley B, Spiegelman BM (Nov 1999). "Activation of PPARgamma coactivator-1 through transcription factor docking". Science 286 (5443): 1368–71. doi:10.1126/science.286.5443.1368. PMID 10558993.
^ Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (Dec 1997). "p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha". J. Biol. Chem. 272 (52): 33435–43. doi:10.1074/jbc.272.52.33435. PMID 9407140.
^ Treuter E, Albrektsen T, Johansson L, Leers J, Gustafsson JA (Jun 1998). "A regulatory role for RIP140 in nuclear receptor activation". Mol. Endocrinol. 12 (6): 864–81. doi:10.1210/mend.12.6.0123. PMID 9626662.
^ Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (Nov 2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.
^ Giraud S, Bienvenu F, Avril S, Gascan H, Heery DM, Coqueret O (Mar 2002). "Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a". J. Biol. Chem. 277 (10): 8004–11. doi:10.1074/jbc.M111486200. PMID 11773079.
^ Litterst CM, Pfitzner E (Dec 2001). "Transcriptional activation by STAT6 requires the direct interaction with NCoA-1". J. Biol. Chem. 276 (49): 45713–21. doi:10.1074/jbc.M108132200. PMID 11574547.
^ Litterst CM, Pfitzner E (Sep 2002). "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1". J. Biol. Chem. 277 (39): 36052–60. doi:10.1074/jbc.M203556200. PMID 12138096.
^ Kim HJ, Yi JY, Sung HS, Moore DD, Jhun BH, Lee YC, Lee JW (Sep 1999). "Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation". Mol. Cell. Biol. 19 (9): 6323–32. PMC 84603. PMID 10454579.
^ Liu Y, Takeshita A, Misiti S, Chin WW, Yen PM (Oct 1998). "Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors". Endocrinology 139 (10): 4197–204. doi:10.1210/endo.139.10.6218. PMID 9751500.
^ Jeyakumar M, Tanen MR, Bagchi MK (Jun 1997). "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. doi:10.1210/mend.11.6.0003. PMID 9171239.

External links

nuclear receptor coactivator 1 at the US National Library of Medicine Medical Subject Headings (MeSH)
NURSA C89

UpToDate Contents

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1. 甲状腺ホルモンの作用 thyroid hormone action
2. 選択的エストロゲン受容体モジュレーターの作用機序 mechanisms of action of selective estrogen receptor modulators
3. エストロゲン作用の分子生物学および生理学 molecular biology and physiology of estrogen action
4. 喘息における吸入ステロイドの分子学的影響 molecular effects of inhaled glucocorticoid therapy in asthma
5. 去勢抵抗性前立腺癌：アンドロゲンの作用経路を標的する療法 castration resistant prostate cancer treatments targeting the androgen pathway

English Journal

A structural explanation of the effects of dissociated glucocorticoids on glucocorticoid receptor transactivation.

Dezitter X1, Fagart J, Taront S, Fay M, Masselot B, Hétuin D, Formstecher P, Rafestin-Oblin ME, Idziorek T.Author information 1Institut National de la Santé et de la Recherche Médicale U837, Institut de Recherche pour le Cancer de Lille, Lille, France (X.D., S.T., B.M., D.H., P.F., T.I.); Institut National de la Santé et de la Recherche Médicale U773, Centre de Recherche Biomédicale Bichat-Beaujon, CRB3 (J.F., M.F., M.-E.R.-O.); and Université Paris 7- Denis Diderot, site Bichat, Paris, France (J.F., M.F., M.-E.R.-O.).AbstractThere is a therapeutic need for glucocorticoid receptor (GR) ligands that distinguish between the transrepression and transactivation activity of the GR, the later thought to be responsible for side effects. These ligands are known as "dissociated glucocorticoids" (dGCs). The first published dGCs, RU24782 (9α-fluoro-11β-hydroxy-16α-methylpregna-21-thiomethyl-1,4-diene-3,20-dione) and RU24858 (9α-fluoro-11β-hydroxy-16α-methylpregna-21-cyanide-1,4-diene-3,20-dione), do not have the 17α-hydroxyl group that characterizes dexamethasone (Dex; 9α-fluoro-11β,17α,21-trihydroxy-16α-methylpregna-1,4-diene-3,20-dione), and they differ from one another by having C21-thiomethyl and C21-cyanide moieties, respectively. Our aim was therefore to establish the structural basis of their activity. Both RU24782 and RU24858 induced a transactivation activity highly dependent on the GR expression level but always lower than dexamethasone. They also display less ability than dexamethasone to trigger steroid receptor coactivator 1 (SRC-1) recruitment and histone H3 acetylation. Docking studies, validated by mutagenesis experiments, revealed that dGCs are not anchored by Gln642, in contrast to Dex, which is hydrogen bonded to this residue via its 17α-hydroxyl group. This contact is essential for SRC-1 recruitment and subsequent dexamethasone-induced GR transactivation, but not transrepression. The ability of dGCs to make contacts with Ile747, for both RU24858 and RU24782 and with Asn564 for RU24858 are not strong enough to maintain GR in a conformation able to efficiently recruit SRC-1, unless SRC-1 is overexpressed. Overall, our findings provide some structural guidelines for the synthesis of potential new dissociated glucocorticoids with a better therapeutic ratio.
Molecular pharmacology.Mol Pharmacol.2014 Feb;85(2):226-36. doi: 10.1124/mol.113.085860. Epub 2013 Nov 13.
There is a therapeutic need for glucocorticoid receptor (GR) ligands that distinguish between the transrepression and transactivation activity of the GR, the later thought to be responsible for side effects. These ligands are known as "dissociated glucocorticoids" (dGCs). The first published dGCs, R
PMID 24225022

Nur77 inhibits androgen-induced bladder cancer growth.

Wu J1, Liu J, Jia R, Song H.Author information 1Department of Urology, Nanjing First Hospital, Nanjing Medical University, Nanjing, China.AbstractCurrently, bladder cancer ranks as the second most common genitourinary malignancy which is exacting significant morbidity and mortality worldwide. Although there are abundant epidemiological and basic studies which strongly suggest the role of androgen hormone in bladder cancer, the underlying mechanism is not fully understood. In the current study, we sought to identify a new competitive inhibitor for androgen receptor in bladder cancer cells. Our results showed that Nur77 hyperexpression inhibits UM-UC-3 cell growth and cell cycle progression while Nur77 knockdown exerts the opposite effect. In our cell culture model, we also demonstrated that Nur77 competitively inhibits androgen-dependent transcription activity and more specifically, Nur77 competes with androgen receptor for binding to src-1, a well-known coactivator for steroids. More importantly, we also showed that a small molecule agonist for Nur77, Cytosporone B, significantly inhibits androgen-dependent bladder cancer cell growth in two different cell lines. These data provide a good proof-of-principle that Nur77 signaling machinery could be a new target for growth control of androgen-dependent bladder cancer cells.
Cancer investigation.Cancer Invest.2013 Dec;31(10):654-60. doi: 10.3109/07357907.2013.853077.
Currently, bladder cancer ranks as the second most common genitourinary malignancy which is exacting significant morbidity and mortality worldwide. Although there are abundant epidemiological and basic studies which strongly suggest the role of androgen hormone in bladder cancer, the underlying mech
PMID 24299210

Steroid receptor coactivator-1: a versatile regulator and promising therapeutic target for breast cancer.

Zhang Y1, Duan C, Bian C, Xiong Y, Zhang J.Author information 1Department of Neurobiology, Chongqing Key Laboratory of Neurobiology, Third Military Medical University, Chongqing 400038, China; Company Ten of Cadet Brigade, Third Military Medical University, Chongqing 400038, China.AbstractBreast cancer is the leading cause of cancer death for women worldwide. Various therapeutic approaches have been proposed, among which endocrine therapy has recently become popular due to the high sensitivity of breast tissues to steroids such as estrogens and progesterone. The underlying mechanisms of steroid regulation in breast cancer cell proliferation, invasiveness, metastasis and endocrine resistance, however, remain largely unknown. Steroid receptor coactivator-1 (SRC-1) has attracted much attention because it is an important co-regulator and plays a pivotal role in modulating the transcriptional activities of steroid nuclear receptors. Accumulated research has established a strong correlation between SRC-1 and the pathological progression or disease-related features of breast cancer, which supports its potential as a target for specific therapeutic intervention in the clinical management of breast cancer. In addition, a diverse group of downstream molecules have also been shown to participate in various functional pathways related to SRC-1-associated regulation of breast cancer. These downstream molecules are also considered promising therapeutic targets, providing additional options for targeted treatments. In this review, the expression of SRC-1 in breast cancer and the close relationships between SRC-1 and the cell proliferation, invasiveness, metastasis and endocrine resistance of breast cancer will be discussed, followed by a brief summary of its putative functional mechanisms with an emphasis on the potential therapeutic role of SRC-1.
The Journal of steroid biochemistry and molecular biology.J Steroid Biochem Mol Biol.2013 Nov;138:17-23. doi: 10.1016/j.jsbmb.2013.02.010. Epub 2013 Mar 6.
Breast cancer is the leading cause of cancer death for women worldwide. Various therapeutic approaches have been proposed, among which endocrine therapy has recently become popular due to the high sensitivity of breast tissues to steroids such as estrogens and progesterone. The underlying mechanisms
PMID 23474438

Japanese Journal

Transcriptional regulation of genes related to progesterone production [Review]

Mizutani Tetsuya,Ishikane Shin,Kawabe Shinya,Umezawa Akihiro,Miyamoto Kaoru
Endocrine Journal advpub(0), 2015
… Members of the nuclear receptor 5A (NR5A) family (steroidogenic factor 1 and liver receptor homolog 1) play a crucial role in the transcriptional regulation of these genes. …
NAID 130005085779

Akirin2 is critical for inducing inflammatory genes by bridging IκB-ζ and the SWI/SNF complex.

Tartey Sarang,Matsushita Kazufumi,Vandenbon Alexis,Ori Daisuke,Imamura Tomoko,Mino Takashi,Standley Daron M,Hoffmann Jules A,Reichhart Jean-Marc,Akira Shizuo,Takeuchi Osamu
The EMBO Journal 33(20), 2332-2348, 2014-10-16
… Here, we show that Akirin2, an evolutionarily conserved nuclear protein, bridges NF-κB and the chromatin remodeling SWI/SNF complex by interacting with BRG1-Associated Factor 60 (BAF60) proteins as well as IκB-ζ, which forms a complex with the NF-κB p50 subunit. … These interactions are essential for Toll-like receptor-, RIG-I-, and Listeria-mediated expression of proinflammatory genes including Il6 and Il12b in macrophages. …
NAID 120005649311

Alteration of energy metabolism in the pathogenesis of bile duct lesions in primary biliary cirrhosis

Harada Kenichi,Kakuda Yuko,Sato Yasunori,Ikeda Hiroko,Shimoda Shinji,Yamamoto Yasuhiko,Inoue Hiroshi,Ohta Hajime,Kasashima Satomi,Kawashima Atsuhiro,Nakanuma Yasuni
Journal of Clinical Pathology 67(5), 396-402, 2014-05
… Oestrogen-related receptor-α (ERRa) is functionally activated by inducible coactivators such as peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) and Bcl-3. … Results: The nuclear expression of PGC-1α, Bcl-3 and ERRa was exclusively observed in CNSDC of PBC. …
NAID 120005469783

Related Pictures

★リンクテーブル★

リンク元	「核内受容体コアクチベーター1」「核内レセプターコアクチベーター1」
関連記事	「nuclear」「nuclear receptor」

「核内受容体コアクチベーター1」

Nuclear receptor coactivator 1
	; PDB rendering based on 1oj5.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1FM6, 1FM9, 1K4W, 1K74, 1K7L, 1KV6, 1N4H, 1NQ7, 1NRL, 1P8D, 1PZL, 1RDT, 1TFC, 1U3R, 1U3S, 1X76, 1X78, 1X7B, 1X7J, 1XIU, 1XV9, 1XVP, 1YY4, 1YYE, 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
Identifiers
Symbols	NCOA1 ; F-SRC-1; KAT13A; RIP160; SRC1; bHLHe42; bHLHe74
External IDs	OMIM: 602691 MGI: 1276523 HomoloGene: 7859 ChEMBL: 1615387 GeneCards: NCOA1 Gene
EC number	2.3.1.48
Gene ontology
Molecular function	• RNA polymerase II regulatory region DNA binding; • RNA polymerase II transcription coactivator activity; • chromatin binding; • transcription coactivator activity; • histone acetyltransferase activity; • signal transducer activity; • protein binding; • ligand-dependent nuclear receptor binding; • enzyme binding; • estrogen receptor binding; • ligand-dependent nuclear receptor transcription coactivator activity; • protein complex binding; • progesterone receptor binding; • nuclear hormone receptor binding; • retinoid X receptor binding; • protein dimerization activity; • protein N-terminus binding; • androgen receptor binding;
Cellular component	• nuclear chromatin; • nucleoplasm; • cytoplasm; • neuron projection;
Biological process	• positive regulation of transcription from RNA polymerase II promoter by galactose; • transcription, DNA-templated; • lactation; • male gonad development; • cerebellum development; • hippocampus development; • hypothalamus development; • cerebral cortex development; • androgen receptor signaling pathway; • response to estradiol; • response to retinoic acid; • response to progesterone; • cellular response to hormone stimulus; • positive regulation of apoptotic process; • histone H4 acetylation; • cellular lipid metabolic process; • small molecule metabolic process; • positive regulation of neuron differentiation; • positive regulation of transcription, DNA-templated; • positive regulation of female receptivity; • positive regulation of transcription from RNA polymerase II promoter; • male mating behavior; • estrous cycle phase; • labyrinthine layer morphogenesis; • regulation of cellular response to drug;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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