Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner (PubMed:20074560). Lacks ligand binding ability and has no or only very low ERE binding activity resulting in the loss of ligand-dependent transactivation ability. Binds DNA as a homodimer. Can form a heterodimer with ESR1. Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with UBE1C. Interacts with AKAP13. Interacts with DNTTIP2. Interacts with isoform 4 of TXNRD1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes, including cyclin-D1/CCND1 AP-1 promoter. Interacts with DNAAF4 (By similarity). Interacts with PRMT2. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with RBM39, in the presence of estradiol (E2) (By similarity). Preferentially forms a heterodimer with ESR1 rather than ESR2 isoform 1 and inhibits DNA-binding by ESR1. 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. 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. Expressed in the testis. Expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. 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. Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Phosphorylation at Ser-87 and Ser-105 recruits NCOA1. The disease may be caused by variants affecting the gene represented in this entry. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Does not form homodimers. Does not form homodimers. Belongs to the nuclear hormone receptor family. NR3 subfamily. Had previously been shown to interact with PELP1. However this paper was retracted as cell-based data was viewed as unreliable. Truncated N-terminus. Estrogen receptor entry