Estrogen receptor alpha

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Estrogen receptor 1
Protein ESR1 PDB 1a52.png
PDB rendering based on 1a52.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ESR1 ; ER; ESR; ESRA; Era; NR3A1
External IDs OMIM133430 MGI1352467 HomoloGene47906 IUPHAR: NR3A1 ChEMBL: 206 GeneCards: ESR1 Gene
Orthologs
Species Human Mouse
Entrez 2099 13982
Ensembl ENSG00000091831 ENSMUSG00000019768
UniProt P03372 P19785
RefSeq (mRNA) NM_000125 NM_007956
RefSeq (protein) NP_000116 NP_031982
Location (UCSC) Chr 6:
151.98 – 152.45 Mb
Chr 10:
4.61 – 5.01 Mb
PubMed search [1] [2]

Estrogen receptor alpha (ER-α), also known as NR3A1 (nuclear receptor subfamily 3, group A, member 1), is one of two main types of estrogen receptor, a nuclear receptor that is activated by the sex hormone estrogen. In humans, ER-α is encoded by the gene ESR1 (EStrogen Receptor 1).[1][2][3]

Structure[edit]

The estrogen receptor (ESR) is a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription.[4] Alternative splicing results in several ESR1 mRNA transcripts, which differ primarily in their 5-prime untranslated regions. The translated receptors show less variability.[5][1]

Coactivators[edit]

Coactivators of ER-α include:

Interactions[edit]

Estrogen receptor alpha has been shown to interact with:


References[edit]

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Further reading[edit]

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  • Simoncini T, Fornari L, Mannella P et al. (2003). "Novel non-transcriptional mechanisms for estrogen receptor signaling in the cardiovascular system. Interaction of estrogen receptor alpha with phosphatidylinositol 3-OH kinase". Steroids 67 (12): 935–9. doi:10.1016/S0039-128X(02)00040-5. PMID 12398989. 
  • Lannigan DA (2003). "Estrogen receptor phosphorylation". Steroids 68 (1): 1–9. doi:10.1016/S0039-128X(02)00110-1. PMID 12475718. 
  • Herrington, David M. (2003). "Role of estrogen receptor-alpha in pharmacogenetics of estrogen action". Curr. Opin. Lipidol. 14 (2): 145–50. doi:10.1097/00041433-200304000-00005. PMID 12642782. 
  • Tanaka Y, Sasaki M, Kaneuchi M et al. (2004). "Estrogen receptor alpha polymorphisms and renal cell carcinoma--a possible risk". Mol. Cell. Endocrinol. 202 (1–2): 109–16. doi:10.1016/S0303-7207(03)00071-6. PMID 12770739. 
  • Ali S, Coombes RC (2004). "Estrogen receptor alpha in human breast cancer: occurrence and significance". Journal of Mammary Gland Biology and Neoplasia 5 (3): 271–81. doi:10.1023/A:1009594727358. PMID 14973389. 
  • Olsson H (2004). "Estrogen receptor content in malignant breast tumors in men--a review". Journal of Mammary Gland Biology and Neoplasia 5 (3): 283–7. doi:10.1023/A:1009546811429. PMID 14973390. 
  • Surmacz E, Bartucci M (2005). "Role of estrogen receptor alpha in modulating IGF-I receptor signaling and function in breast cancer". J. Exp. Clin. Cancer Res. 23 (3): 385–94. PMID 15595626. 
  • Evinger AJ, Levin ER (2005). "Requirements for estrogen receptor alpha membrane localization and function". Steroids 70 (5–7): 361–3. doi:10.1016/j.steroids.2005.02.015. PMID 15862818. 
  • Wang CL, Tang XY, Chen WQ et al. (2007). "Association of estrogen receptor alpha gene polymorphisms with bone mineral density in Chinese women: a meta-analysis". Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA 18 (3): 295–305. doi:10.1007/s00198-006-0239-2. PMID 17089081. 
  • Keaveney M, Klug J, Gannon F (1992). "Sequence analysis of the 5' flanking region of the human estrogen receptor gene". DNA Seq. 2 (6): 347–58. doi:10.3109/10425179209020816. PMID 1476547. 
  • Piva R, Gambari R, Zorzato F et al. (1992). "Analysis of upstream sequences of the human estrogen receptor gene". Biochem. Biophys. Res. Commun. 183 (3): 996–1002. doi:10.1016/S0006-291X(05)80289-X. PMID 1567414. 
  • Reese JC, Katzenellenbogen BS (1992). "Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation". J. Biol. Chem. 267 (14): 9868–73. PMID 1577818. 
  • Dotzlaw H, Alkhalaf M, Murphy LC (1992). "Characterization of estrogen receptor variant mRNAs from human breast cancers". Mol. Endocrinol. 6 (5): 773–85. doi:10.1210/me.6.5.773. PMID 1603086. 
  • Keaveney M, Klug J, Dawson MT et al. (1991). "Evidence for a previously unidentified upstream exon in the human oestrogen receptor gene". J. Mol. Endocrinol. 6 (1): 111–5. doi:10.1677/jme.0.0060111. PMID 2015052. 
  • Reese JC, Katzenellenbogen BS (1991). "Mutagenesis of cysteines in the hormone binding domain of the human estrogen receptor. Alterations in binding and transcriptional activation by covalently and reversibly attaching ligands". J. Biol. Chem. 266 (17): 10880–7. PMID 2040605. 
  • Schwabe JW, Neuhaus D, Rhodes D (1991). "Solution structure of the DNA-binding domain of the oestrogen receptor". Nature 348 (6300): 458–61. doi:10.1038/348458a0. PMID 2247153. 
  • Tora L, Mullick A, Metzger D et al. (1989). "The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties". EMBO J. 8 (7): 1981–6. PMC 401066. PMID 2792078. 
  • Ponglikitmongkol M, Green S, Chambon P (1989). "Genomic organization of the human oestrogen receptor gene". EMBO J. 7 (11): 3385–8. PMC 454836. PMID 3145193. 
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External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.