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The article completion score is designed to help authors identify parts of their articles that can be expanded upon. We highly recommend completing the following steps to significantly increase this article's score: Please provide more information in the Overview section of the Summary tab. Please add more papers to the Papers tab. Please provide more information in the Covalent modifications section of the Protein tab. If applicable, please provide more information in the Isoforms section of the Protein tab. Please provide more information in the Overview section of the Targets tab. Please provide more information in the Genetics section of the Genetics tab. Please provide more information in the Overview section of the Expression tab. Please provide more information in the Overview section of the Structure tab. Please provide more information in the Overview section of the Interactions tab. Please add at least three references to the Overview section of the Summary tab. Please provide more information in the Overview section of the TFBS tab. Please indicate which papers should be considered as important or preferred in the Papers tab. Comments (post) There are no comments posted here... Yet. Overview No annotation is available in this section for this article. The content below is taken from a related TF, ESR2 (Homo sapiens). Cellular signaling of estrogen is mediated through two estrogen receptors (ERs), ESR1 and ESR2. The first ER, now known as ESR1, was cloned in 1986. This receptor was regarded as the only ER that mediates estrogenic effects, until a second ER, now known as ESR2, was cloned from rat prostate. ESR1 and ESR2 belong to the superfamily of nuclear receptors and specifically to the family of steroid receptors that act as ligand-regulated transcription factors. ESR1 and ESR2 have a high sequence homology and share affinity for the same ligands and DNA response elements. Binding of ligand activates ERs, by a mechanism that involves dissociation of heat shock proteins and dimerization of receptor proteins. Estrogen-modulated gene transcription is exerted via different mechanisms: the genomic and the nongenomic pathways. The canonical model for ER-mediated regulation of gene expression involves the direct binding of dimeric ER to DNA sequences known as estrogen response elements (EREs), followed by recruitment of a variety of coregulators to alter chromatin structure and facilitate recruitment of the RNA polymerase II (Pol II) transcriptional machinery. The transcriptional activity of ERs can be modulated by different types of post-translational modifications such as phosphorylation, acetylation, sumoylation, ubiquitination and methylation. ESR1 and ESR2 exhibit different affinities for some natural compounds, and distinct expression patterns in a variety of tissues. Transcriptional activation by ESR1 is mediated by two distinct activation functions: the constitutively active AF-1 and the ligand-dependent AF-2. ESR2 seems to have a weaker corresponding AF-1 function and thus depends more on the AF-2 for its transcriptional activation function. ESR1 and ESR2 have different activities in certain ligand, cell-type, and promoter contexts. Figures No annotation is available in this section for this article. The content below is taken from a related TF, ESR2 (Homo sapiens).
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