A synthetic peptide of human Estrogen Receptor alpha
Conjugation:
Unconjugated
Alternative Names:
ESR, NR3A1, Estrogen receptor, ER, ER-alpha, Estradiol receptor, Nuclear receptor subfamily 3 group A member 1
Estrogen receptor alpha (ERalpha), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains. 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 at multiple sites provides an important mechanism to regulate ERalpha activity. Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERalpha activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt. According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients.
