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ER-beta (human)

Overview ER-beta a nuclear hormone receptor and transcription factor. Binds and activated by estrogen. Regulates gene expression and affects cellular proliferation and differentiation in target tissues. Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Eight alternatively-spliced isoforms have been described. Isoform beta-cx lacks ligand binding ability and has no or only very low ERE binding activity resulting in the loss of ligand-dependent transactivation ability. Note: This description may include information from UniProtKB. Protein type: DNA binding protein; Nuclear receptor Cellular Component: nucleoplasm; mitochondrion; extracellular region; nucleus Molecular Function: ligand-dependent nuclear receptor activity; protein binding; receptor antagonist activity; estrogen receptor activity; enzyme binding; DNA binding; zinc ion binding; transcription coactivator activity; estrogen response element binding; steroid hormone receptor activity; transcription factor activity; steroid binding Biological Process: transcription initiation from RNA polymerase II promoter; estrogen receptor signaling pathway; positive regulation of apoptosis; neuron migration; vagina development; negative regulation of transcription from RNA polymerase II promoter; uterus development; signal transduction; ovarian follicle development; regulation of transcription, DNA-dependent; cell-cell signaling; gene expression; positive regulation of transcription factor activity; negative regulation of cell growth; brain development; negative regulation of epithelial cell proliferation Reference #:  Q92731 (UniProtKB) Alt. Names/Synonyms: ER-beta; Erb; ESR-BETA; ESR2; ESRB; ESTRB; estrogen receptor 2 (ER beta); Estrogen receptor beta; estrogen receptor beta 4; NR3A2; Nuclear receptor subfamily 3 group A member 2 Gene Symbols: ESR2 Molecular weight: 59,216 Da Basal Isoelectric point: 8.81  Predict pI for various phosphorylation states CST Pathways:  MAPK/Erk in Growth and Differentiation

Select Structure to View Below ER-beta 1L2J - A/B=256-505 (human) 1NDE - A=256-501 (human) 1QKM - A=255-509 (human) 1U3Q - A/B/C/D=261-500 (human) 1U3R - A/B=261-501 (human) 1U3S - A/B=261-500 (human) 1U9E - A/B=261-501 (human) 1X76 - A/B=261-500 (human) 1X78 - A/B=261-500 (human) 1X7B - A/B=261-500 (human) 1X7J - A/B=261-500 (human) 1YY4 - A/B=263-530 (human) 1YYE - A/B=263-530 (human) 1ZAF - A/B=263-500 (human) 2FSZ - A/B=257-502 (human) 2GIU - A=260-500 (human) 2I0G - A/B=256-505 (human) 2JJ3 - A/B=251-505 (human) 2NV7 - A/B=263-500 (human) 2QTU - A/B=256-505 (human) 2YJD - A/B=261-500 (human) 2YLY - A/B=260-500 (human) 2Z4B - A/B=251-505 (human) 3OLL - A/B=261-500 (human) 3OLS - A/B=261-500 (human) 3OMO - A/B=261-500 (human) 3OMP - A/B=261-500 (human) 3OMQ - A/B=261-500 (human) 4J24 - A/D/C/B=261-500 (human) 4J26 - A/B=261-500 (human) 1HJ1 (rat) 1QKN (rat) 2J7X (rat) 2J7Y (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1L2J 1NDE 1QKM 1U3Q 1U3R 1U3S 1U9E 1X76 1X78 1X7B 1X7J 1YY4 1YYE 1ZAF 2FSZ 2GIU 2I0G 2JJ3 2NV7 2QTU 2YJD 2YLY 2Z4B 3OLL 3OLS 3OMO 3OMP 3OMQ 4J24 4J26  |  Phospho3D  |  DISEASE  |  Source  |  NURSA  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
activation: S87‑p, S105‑p intracellular localization: S105‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		Y56-p	YSPAVMNySIPSNVT
1	1		N61	MNySIPSNVTNLEGG
2	1		N61	MNySIPSNVTNLEGG
1	0		S75	GPGRQTTSPNVLWPT
3	0		S87-p	WPTPGHLsPLVVHRQ
4	0		S105-p	LYAEPQKsPWCEARS
1	0		S176-p	CKAFFKRsIQGHNDY
1	0		S200-p	IDKNRRKsCQACRLR
1	0		D236	VRRQRSADEQLHCAG
0	1		S463-p	ANLLMLLsHVRHAsN
0	1		S469-p	LsHVRHAsNKGMEHL
1	0		Y488	CKNVVPVYDLLLEML
0	1		S505	HVLRGCKSSITGSEC

	mouse
Y56	YSPAVMNYSVPSsTG
S61-p	MNYSVPSsTGNLEGG
S61-gl	MNYSVPSsTGNLEGG
S75-p	GPVRQTAsPNVLWPT
S87-p	WPTSGHLsPLATHCQ
S105-p	LYAEPQKsPWCEARS
S176	CKAFFKRSIQGHNDY
S200	IDKNRRKSCQACRLR
S236-p	VRRQRSAsEQVHCLN
S463	ANLLMLLSHVRHISN
S469	LSHVRHISNKGMEHL
Y488-p	CKNVVPVyDLLLEML
S505-p	HTLRGYKsSISGSEC

	rat
Y56	YSPAVMNYSVPGSTS
S61	MNYSVPGSTSNLDGG
S61	MNYSVPGSTSNLDGG
S75	GPVRLSTSPNVLWPT
S87	WPTSGHLSPLATHCQ
S105	LYAEPQKSPWCEARS
S176	CKAFFKRSIQGHNDY
S200	IDKNRRKSCQACRLR
S236	VRRQRSSSEQVHCLS
S463	ANLLMLLSHVRHISN
S469	LSHVRHISNKGMEHL
Y488	CKNVVPVYDLLLEML
S505	HTLRGYKSSISGSEC

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