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Description
Estrogen receptor alpha (ERalpha), a member of the steroid receptor superfamily, contains highly conserved DNA binding (DBD) and ligand binding domains (LBD) . Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERalpha regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery . Phosphorylation provides an important mechanism to regulate ERalpha activity . ERalpha is phosphorylated on multiple sites . Ser104, 106, 118 and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serines plays an important role in regulating ERalpha activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 . Ser167 may be phosphorylated by p90RSK and Akt . Phosphorylation of Ser167 may confer tamoxifen resistance in breast cancer patients . Synonyms: ESR1,DKFZp686N23123,ER,ESR,ESRA,Era,NR3A1 , Estrogen Receptor alpha