UNIPROT #

Q92731

PROTEIN NAME

Estrogen Receptor beta

SYNONYMS

ER BETA antibody; ER-beta antibody; Erb antibody; ESR B antibody; ESR BETA antibody; ESR2 antibody; ESR2_HUMAN antibody; ESRB antibody; ESTRB antibody; estrogen nuclear receptor beta variant a antibody; estrogen nuclear receptor beta variant b antibody; estrogen receptor 2 (ER beta) antibody; Estrogen receptor 2 antibody; estrogen receptor beta 4 antibody; Estrogen receptor beta antibody; NR3A2 antibody; Nuclear receptor subfamily 3 group A member 2 antibody

SEQUENCE SIMILARITIES

Belongs to the nuclear hormone receptor family. NR3 subfamily.

TISSUE SPECIFICITY

Isoform 1 is expressed in testis and ovary, and at a lower level in heart, brain, placenta, liver, skeletal muscle, spleen, thymus, prostate, colon, bone marrow, mammary gland and uterus. Also found in uterine bone, breast, and ovarian tumor cell lines, but not in colon and liver tumors. Isoform 2 is expressed in spleen, thymus, testis and ovary and at a lower level in skeletal muscle, prostate, colon, small intestine, leukocytes, bone marrow, mammary gland and uterus. Isoform 4 is found in testis. Isoform 5 is expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. Isoform 6 is expressed in testis, placenta, skeletal muscle, spleen and leukocytes, and at a lower level in heart, lung, liver, kidney, pancreas, thymus, prostate, colon, small intestine, bone marrow, mammary gland and uterus. Not expressed in brain.

POST-TRANSLATIONAL MODIFICATION

Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.

SUBCELLULAR LOCATION

Nucleus.

FUNCTION

Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ERα and ERβ, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ERα and ERβ have been shown to be differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ERα and ERβ may be regulated by distinct mechanisms even though they share many functional characteristics.