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Estrogen receptor positive

estrogen receptor 1 (ER-alpha)
PBB Protein ESR1 image.png
A dimer of the ligand-binding region of ERα (PDB rendering based on 3erd​).
Identifiers
Symbol ESR1
Alt. symbols ER-α, NR3A1
Entrez 2099
HUGO 3467
OMIM 133430
PDB 1ERE
RefSeq NM_000125
UniProt P03372
Other data
Locus Chr. 6 q24-q27
estrogen receptor 2 (ER-beta)
Estrogen receptor beta 1U3S.png
A dimer of the ligand-binding region of ERβ (PDB rendering based on 1u3s​).
Identifiers
Symbol ESR2
Alt. symbols ER-β, NR3A2
Entrez 2100
HUGO 3468
OMIM 601663
PDB 1QKM
RefSeq NM_001040275
UniProt Q92731
Other data
Locus Chr. 14 q21-q22
Estrogen receptor alpha
N-terminal AF1 domain
Identifiers
Symbol Oest_recep
Pfam PF02159
InterPro IPR001292
SCOP 1hcp
SUPERFAMILY 1hcp
Estrogen and estrogen related receptor C-terminal domain
Identifiers
Symbol ESR1_C
Pfam PF12743

Estrogen receptors (ERs) are a group of proteins found inside and on cells. They are receptors that are activated by the hormone estrogen (17β-estradiol). Two classes of ER exist: nuclear estrogen receptors (ERα and ERβ), which are members of the nuclear receptor family of intracellular receptors, and membrane estrogen receptors (mERs) (GPER (GPR30), ER-X, and Gq-mER), which are mostly G protein-coupled receptors. This article refers to the former (ER).

Once activated by estrogen, the ER is able to translocate into the nucleus and bind to DNA to regulate the activity of different genes (i.e. it is a DNA-binding transcription factor). However, it also has additional functions independent of DNA binding.

As hormone receptors for sex steroids (steroid hormone receptors), ERs, androgen receptors (ARs), and progesterone receptors (PRs) are important in sexual maturation and gestation.

There are two different forms of the estrogen receptor, usually referred to as α and β, each encoded by a separate gene (ESR1 and ESR2, respectively). Hormone-activated estrogen receptors form dimers, and, since the two forms are coexpressed in many cell types, the receptors may form ERα (αα) or ERβ (ββ) homodimers or ERαβ (αβ) heterodimers. Estrogen receptor alpha and beta show significant overall sequence homology, and both are composed of five domains designated A/B through F (listed from the N- to C-terminus; amino acid sequence numbers refer to human ER).


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