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Protein

Estrogen receptor

Gene

ESR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1.20 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi185 – 250Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • ATPase binding Source: MGI
  • beta-catenin binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • estrogen receptor activity Source: UniProtKB
  • estrogen response element binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • nitric-oxide synthase regulator activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding Source: BHF-UCL
  • steroid binding Source: UniProtKB
  • steroid hormone receptor activity Source: ProtInc
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091831-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLinkiP03372.
SIGNORiP03372.

Chemistry databases

SwissLipidsiSLP:000001568.

Names & Taxonomyi

Protein namesi
Recommended name:
Estrogen receptor
Short name:
ER
Alternative name(s):
ER-alpha
Estradiol receptor
Nuclear receptor subfamily 3 group A member 1
Gene namesi
Name:ESR1
Synonyms:ESR, NR3A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3467. ESR1.

Subcellular locationi

Isoform 1 :
Isoform 3 :
  • Nucleus
  • Golgi apparatus
  • Cell membrane

  • Note: Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Estrogen resistance (ESTRR)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into adulthood and very tall adult stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present.
See also OMIM:615363
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004672364V → E in ESTRR; dominant-negative inhibitor of the wild-type ESR. 1 PublicationCorresponds to variant rs121913044dbSNPEnsembl.1
Natural variantiVAR_070072375Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant rs397509428dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39L → P: Impairs AF-1 transactivation. 1 Publication1
Mutagenesisi43Y → P: Impairs AF-1 transactivation. 1 Publication1
Mutagenesisi104S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1
Mutagenesisi106S → A: Loss of cyclin A-dependent induction of transcriptional activation. 1
Mutagenesisi118S → A: Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications1
Mutagenesisi118S → E: Enhances transactivation activity. Enhances interaction with DDX5. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications1
Mutagenesisi260R → A or K: Loss of methylation. 1 Publication1
Mutagenesisi386I → C: Loss of transmembrane localization, no effect on peripheral membrane localization. Impairs activation of estrogen-induced activation of NOS3 and production of nitric oxide. No effect on binding to ERES. 1 Publication1
Mutagenesisi447C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. 1 Publication1
Mutagenesisi539L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2099.
MalaCardsiESR1.
MIMi615363. phenotype.
OpenTargetsiENSG00000091831.
Orphaneti785. Estrogen resistance syndrome.
PharmGKBiPA156.

Chemistry databases

ChEMBLiCHEMBL206.
DrugBankiDB01431. Allylestrenol.
DB06401. Bazedoxifene.
DB00882. Clomifene.
DB00286. Conjugated Estrogens.
DB01406. Danazol.
DB00304. Desogestrel.
DB00890. Dienestrol.
DB00255. Diethylstilbestrol.
DB00783. Estradiol.
DB01196. Estramustine.
DB04573. Estriol.
DB00655. Estrone.
DB04574. Estropipate.
DB00977. Ethinyl Estradiol.
DB00823. Ethynodiol.
DB00294. Etonogestrel.
DB01185. Fluoxymesterone.
DB00947. Fulvestrant.
DB00367. Levonorgestrel.
DB00603. Medroxyprogesterone Acetate.
DB01065. Melatonin.
DB01357. Mestranol.
DB01183. Naloxone.
DB00957. Norgestimate.
DB04938. Ospemifene.
DB00396. Progesterone.
DB04575. Quinestrol.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB00539. Toremifene.
DB01108. Trilostane.
GuidetoPHARMACOLOGYi620.

Polymorphism and mutation databases

BioMutaiESR1.
DMDMi544257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536181 – 595Estrogen receptorAdd BLAST595

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi10O-linked (GlcNAc)By similarity1
Modified residuei104Phosphoserine; by CDK21 Publication1
Modified residuei106Phosphoserine; by CDK21 Publication1
Modified residuei118Phosphoserine1 Publication1
Modified residuei167Phosphoserine; by CK21 Publication1
Modified residuei260Asymmetric dimethylarginine; by PRMT11 Publication1
Lipidationi447S-palmitoyl cysteineBy similarity1
Modified residuei537Phosphotyrosine; by Tyr-kinases1 Publication1

Post-translational modificationi

Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro.7 Publications
Glycosylated; contains N-acetylglucosamine, probably O-linked.1 Publication
Ubiquitinated. Deubiquitinated by OTUB1.2 Publications
Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization.1 Publication
Palmitoylated (isoform 3). Not biotinylated (isoform 3).1 Publication
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP03372.
PaxDbiP03372.
PeptideAtlasiP03372.
PRIDEiP03372.

PTM databases

iPTMnetiP03372.
PhosphoSitePlusiP03372.
SwissPalmiP03372.
UniCarbKBiP03372.

Expressioni

Tissue specificityi

Widely expressed. Isoform 3 is not expressed in the pituitary gland.1 Publication

Gene expression databases

BgeeiENSG00000091831.
CleanExiHS_ESR1.
ExpressionAtlasiP03372. baseline and differential.
GenevisibleiP03372. HS.

Organism-specific databases

HPAiCAB000037.
CAB055099.
CAB072858.
HPA000449.
HPA000450.

Interactioni

Subunit structurei

Binds DNA as a homodimer. Can form a heterodimer with ESR2. Isoform 3 can probably homodimerize or heterodimerize with isoform 1 and ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By similarity). Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with CITED1; the interaction is estrogen-dependent. Interacts with NCOA5 and NCOA6 coactivators. Interacts with NCOA7; the interaction is a ligand-inducible. Interacts with PHB2, PELP1 and UBE1C. Interacts with AKAP13. Interacts with CUEDC2. Interacts with KDM5A. Interacts with SMARD1. Interacts with HEXIM1. Interacts with PBXIP1. Interaction with MUC1 is stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated transcription. Interacts with DNTTIP2, FAM120B and UIMC1. Interacts with isoform 4 of TXNRD1. Interacts with KMT2D/MLL2. Interacts with ATAD2 and this interaction is enhanced by estradiol. Interacts with KIF18A and LDB1. Interacts with RLIM (via C-terminus). Interacts with MACROD1. Interacts with SH2D4A and PLCG. Interaction with SH2D4A blocks binding to PLCG and inhibits estrogen-induced cell proliferation. Interacts with DYNLL1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Interacts with DYX1C1. Interacts with PRMT2. Interacts with PI3KR1 or PI3KR2, SRC and PTK2/FAK1. Interacts with RBFOX2. Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D. Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy. Interacts with DDX5. Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions. Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3. Interacts with NRIP1 (By similarity). Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts with CLOCK and the interaction is stimulated by estrogen. Interacts with BCAS3. Interacts with TRIP4 (ufmylated); estrogen dependent. Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with ZFHX3. Interacts with SFR1 in a ligand-dependent and -independent manner (PubMed:23874500).By similarity56 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-78473,EBI-78473
AKAP13Q128023EBI-78473,EBI-1373806
ASF1AQ9Y2942EBI-78473,EBI-749553
ASXL1Q8IXJ92EBI-78473,EBI-1646500
Asxl1P595982EBI-78473,EBI-5743705From a different organism.
BLCAPP629522EBI-78473,EBI-3895726
BRCA1P3839812EBI-78473,EBI-349905
BTF3P20290-25EBI-78473,EBI-1054703
CACUL1Q86Y375EBI-78473,EBI-8168227
CITED1Q999663EBI-78473,EBI-2624951
CUEDC2Q9H4672EBI-78473,EBI-1248228
DDX17Q928418EBI-78473,EBI-746012
DDX5P178449EBI-78473,EBI-351962
DNM1LO004292EBI-78473,EBI-724571
EGFRP005334EBI-4309277,EBI-297353
EP300Q094722EBI-78473,EBI-447295
FOXO1Q127782EBI-78473,EBI-1108782
GRIP1Q9Y3R02EBI-78473,EBI-5349621
HAX1O001652EBI-78473,EBI-357001
JunP056276EBI-78473,EBI-764369From a different organism.
KDM6BO150542EBI-78473,EBI-2831260
KMT2DO146863EBI-78473,EBI-996065
MACROD1Q9BQ694EBI-78473,EBI-5324932
MDM2Q009872EBI-78473,EBI-389668
MTA1Q133304EBI-78473,EBI-714236
MTA2O947763EBI-78473,EBI-1783035
MTA3Q9BTC83EBI-78473,EBI-2461787
MYL6P606603EBI-78473,EBI-300817
NCOA1Q1578810EBI-78473,EBI-455189
NCOA2Q155968EBI-78473,EBI-81236
NCOA3Q9Y6Q92EBI-78473,EBI-81196
Ncoa6Q9JLI42EBI-78473,EBI-286271From a different organism.
NDRG2Q9UN362EBI-78473,EBI-3895741
NFKB1P198383EBI-78473,EBI-697771
NR1H4Q96RI1-32EBI-78473,EBI-10921781
PAGR1Q9BTK65EBI-78473,EBI-2372223
PBXIP1Q96AQ69EBI-78473,EBI-740845
Pfn1P629623EBI-78473,EBI-647096From a different organism.
PHB2Q996234EBI-78473,EBI-358348
PIK3R1P279866EBI-78473,EBI-79464
PPP5CP530414EBI-78473,EBI-716663
PRMT2P553459EBI-78473,EBI-78458
RAC3P607635EBI-78473,EBI-767084
RBFOX2O432514EBI-78473,EBI-746056
RELAQ042067EBI-78473,EBI-73886
SAFB2Q141512EBI-78473,EBI-352869
SENP5Q96HI02EBI-78473,EBI-3895753
SHC1P293532EBI-4309277,EBI-78835
SMARCA4P515323EBI-78473,EBI-302489
SP1P080472EBI-78473,EBI-298336
SP3Q024472EBI-78473,EBI-348158
SRCP129319EBI-78473,EBI-621482
TXNRD1Q16881-44EBI-78473,EBI-9080335
ZNF366Q8N8956EBI-78473,EBI-2813661

GO - Molecular functioni

  • ATPase binding Source: MGI
  • beta-catenin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108403. 699 interactors.
DIPiDIP-5965N.
IntActiP03372. 465 interactors.
MINTiMINT-129047.
STRINGi9606.ENSP00000206249.

Chemistry databases

BindingDBiP03372.

Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni186 – 188Combined sources3
Beta strandi189 – 191Combined sources3
Beta strandi194 – 196Combined sources3
Beta strandi199 – 201Combined sources3
Helixi203 – 213Combined sources11
Beta strandi222 – 225Combined sources4
Turni231 – 236Combined sources6
Helixi238 – 248Combined sources11
Helixi288 – 291Combined sources4
Helixi302 – 304Combined sources3
Helixi307 – 309Combined sources3
Helixi312 – 322Combined sources11
Beta strandi330 – 332Combined sources3
Beta strandi334 – 336Combined sources3
Helixi339 – 361Combined sources23
Helixi367 – 369Combined sources3
Helixi372 – 394Combined sources23
Turni395 – 397Combined sources3
Beta strandi402 – 405Combined sources4
Beta strandi408 – 410Combined sources3
Helixi412 – 415Combined sources4
Beta strandi418 – 420Combined sources3
Helixi421 – 438Combined sources18
Helixi442 – 455Combined sources14
Helixi458 – 460Combined sources3
Turni464 – 466Combined sources3
Helixi467 – 469Combined sources3
Helixi473 – 492Combined sources20
Helixi497 – 530Combined sources34
Beta strandi531 – 533Combined sources3
Helixi538 – 545Combined sources8
Helixi547 – 549Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A52X-ray2.80A/B297-554[»]
1AKFmodel-A309-547[»]
1EREX-ray3.10A/B/C/D/E/F301-553[»]
1ERRX-ray2.60A/B301-553[»]
1G50X-ray2.90A/B/C304-550[»]
1GWQX-ray2.45A/B301-548[»]
1GWRX-ray2.40A/B305-549[»]
1HCPNMR-A180-254[»]
1HCQX-ray2.40A/B/E/F180-262[»]
1L2IX-ray1.95A/B297-554[»]
1PCGX-ray2.70A/B304-547[»]
1QKTX-ray2.20A304-551[»]
1QKUX-ray3.20A/B/C301-550[»]
1R5KX-ray2.70A/B/C297-554[»]
1SJ0X-ray1.90A307-554[»]
1UOMX-ray2.28A301-553[»]
1X7EX-ray2.80A/B305-549[»]
1X7RX-ray2.00A305-549[»]
1XP1X-ray1.80A307-554[»]
1XP6X-ray1.70A307-554[»]
1XP9X-ray1.80A307-554[»]
1XPCX-ray1.60A307-554[»]
1XQCX-ray2.05A/B/C/D301-553[»]
1YIMX-ray1.90A307-554[»]
1YINX-ray2.20A307-554[»]
1ZKYX-ray2.25A/B298-554[»]
2AYRX-ray1.90A304-551[»]
2B1VX-ray1.80A/B298-554[»]
2B1ZX-ray1.78A/B298-554[»]
2B23X-ray2.10A/B298-554[»]
2BJ4X-ray2.00A/B305-533[»]
2FAIX-ray2.10A/B298-554[»]
2G44X-ray2.65A/B298-554[»]
2G5OX-ray2.30A/B298-554[»]
2I0JX-ray2.90A/B/C/D304-547[»]
2IOGX-ray1.60A309-554[»]
2IOKX-ray2.40A/B301-554[»]
2JF9X-ray2.10A/B/C304-533[»]
2JFAX-ray2.55A/B304-533[»]
2LLONMR-B287-305[»]
2LLQNMR-B287-305[»]
2OCFX-ray2.95A298-595[»]
2OUZX-ray2.00A301-553[»]
2P15X-ray1.94A/B298-554[»]
2POGX-ray1.84A/B304-551[»]
2Q6JX-ray2.70A/B298-554[»]
2Q70X-ray1.95A/B304-551[»]
2QA6X-ray2.60A/B298-554[»]
2QA8X-ray1.85A/B298-554[»]
2QABX-ray1.89A/B298-554[»]
2QE4X-ray2.40A/B304-551[»]
2QGTX-ray2.15A/B298-554[»]
2QGWX-ray2.39A/B298-554[»]
2QH6X-ray2.70A/B298-554[»]
2QR9X-ray2.00A/B298-554[»]
2QSEX-ray1.85A/B298-554[»]
2QXMX-ray2.30A/B298-554[»]
2QXSX-ray1.70A/B298-554[»]
2QZOX-ray1.72A/B298-554[»]
2R6WX-ray2.00A/B304-551[»]
2R6YX-ray2.00A/B304-551[»]
2YATX-ray2.60A301-551[»]
2YJAX-ray1.82B299-551[»]
3CBMX-ray1.69B298-307[»]
3CBOX-ray1.65B298-307[»]
3CBPX-ray1.42B298-307[»]
3DT3X-ray2.40A/B299-551[»]
3ERDX-ray2.03A/B297-554[»]
3ERTX-ray1.90A297-554[»]
3HLVX-ray3.00A/B298-550[»]
3HM1X-ray2.33A/B298-550[»]
3L03X-ray1.90A/B298-550[»]
3OS8X-ray2.03A/B/C/D299-553[»]
3OS9X-ray2.30A/B/C/D299-553[»]
3OSAX-ray2.30A/B/C/D299-553[»]
3Q95X-ray2.05A/B298-554[»]
3Q97X-ray2.10A/B298-554[»]
3UU7X-ray2.20A/B302-552[»]
3UUAX-ray2.05A/B302-552[»]
3UUCX-ray2.10A/B/C/D302-552[»]
3UUDX-ray1.60A/B302-552[»]
4AA6X-ray2.60A/B/E/F182-252[»]
4DMAX-ray2.30A/B303-549[»]
4IU7X-ray2.29A/B303-549[»]
4IUIX-ray2.30A/B303-549[»]
4IV2X-ray2.14A/B303-549[»]
4IV4X-ray2.30A/B303-549[»]
4IVWX-ray2.06A/B303-549[»]
4IVYX-ray1.95A/B303-549[»]
4IW6X-ray1.98A/B303-549[»]
4IW8X-ray2.04A/B303-549[»]
4IWCX-ray2.24A/B303-549[»]
4IWFX-ray1.93A/B303-549[»]
4JC3X-ray2.05B585-595[»]
4JDDX-ray2.10B585-595[»]
4MG5X-ray2.05A/B302-552[»]
4MG6X-ray2.10A/B302-552[»]
4MG7X-ray2.15A/B302-552[»]
4MG8X-ray1.85A/B302-552[»]
4MG9X-ray2.00A/B302-552[»]
4MGAX-ray1.80A/B302-552[»]
4MGBX-ray1.85A/B302-552[»]
4MGCX-ray2.15A/B302-552[»]
4MGDX-ray1.90A/B302-552[»]
4O6FX-ray2.82B261-271[»]
4PP6X-ray2.20A/B305-548[»]
4PPPX-ray2.69A/B305-548[»]
4PPSX-ray1.93A/B305-548[»]
4PXMX-ray1.90A/B299-554[»]
4Q13X-ray2.24A/B299-554[»]
4Q50X-ray3.07A/B/C/D/E/F/G/H299-554[»]
4TUZX-ray1.90A/B302-552[»]
4TV1X-ray1.85A/B302-552[»]
4XI3X-ray2.49A/B/C/D306-548[»]
4ZN7X-ray1.93A/B301-559[»]
4ZN9X-ray2.21A/B301-559[»]
4ZNHX-ray1.93A/B301-559[»]
4ZNSX-ray1.86A/B301-559[»]
4ZNTX-ray1.90A/B301-559[»]
4ZNUX-ray2.40A/B301-559[»]
4ZNVX-ray1.77A/B301-559[»]
4ZNWX-ray2.31A/B301-559[»]
4ZUBX-ray2.39A/B304-549[»]
4ZUCX-ray1.82A/B305-549[»]
4ZWHX-ray1.85A/B303-549[»]
4ZWKX-ray2.07A/B303-549[»]
5AAUX-ray1.90A/B307-554[»]
5AAVX-ray1.95A307-554[»]
B306-554[»]
5ACCX-ray1.88A307-554[»]
5AK2X-ray2.19A/B307-554[»]
5BNUX-ray1.60A/B303-548[»]
5BP6X-ray2.03A/B303-548[»]
5BPRX-ray1.91A/B303-549[»]
5BQ4X-ray1.78A/B303-549[»]
5DI7X-ray2.24A/B298-554[»]
5DIDX-ray2.24A/B298-554[»]
5DIEX-ray2.24A/B298-554[»]
5DIGX-ray2.24A/B298-554[»]
5DK9X-ray2.28A/B298-554[»]
5DKBX-ray2.40A/B298-554[»]
5DKEX-ray2.60A/B298-554[»]
5DKGX-ray2.15A/B298-554[»]
5DKSX-ray2.60A/B298-554[»]
5DL4X-ray2.10A/B298-554[»]
5DLRX-ray2.26A/B298-554[»]
5DMCX-ray2.40A/B298-554[»]
5DMFX-ray2.40A/B298-554[»]
5DP0X-ray2.38A/B298-554[»]
5DRJX-ray2.07A/B298-554[»]
5DRMX-ray2.24A/B298-554[»]
5DTVX-ray2.29A/B298-554[»]
5DU5X-ray2.19A/B298-554[»]
5DUEX-ray2.09A/B298-554[»]
5DUGX-ray2.25A/B298-554[»]
5DUHX-ray2.24A/B298-554[»]
5DVSX-ray2.28A/B298-554[»]
5DVVX-ray2.50A/B298-554[»]
5DWEX-ray1.92A/B298-554[»]
5DWGX-ray2.30A/B298-554[»]
5DWIX-ray2.43A/B298-554[»]
5DWJX-ray2.00A/B298-554[»]
5DX3X-ray2.09A/B297-554[»]
5DXBX-ray2.08A/B297-554[»]
5DXEX-ray1.50A/B297-554[»]
5DXGX-ray1.86A/B297-554[»]
5DXKX-ray2.23A/B298-554[»]
5DXMX-ray2.37A/B298-554[»]
5DXPX-ray2.20A/B298-554[»]
5DXQX-ray2.40A/B298-554[»]
5DXRX-ray2.28A/B298-554[»]
5DY8X-ray2.03A/B298-554[»]
5DYBX-ray2.27A/B298-554[»]
5DYDX-ray2.48A/B298-554[»]
5DZ0X-ray2.24A/B298-554[»]
5DZ1X-ray2.20A/B298-554[»]
5DZ3X-ray2.15A/B298-554[»]
5DZHX-ray2.11A/B298-554[»]
5DZIX-ray1.90A/B298-554[»]
5E0WX-ray2.00A/B298-554[»]
5E0XX-ray2.01A/B298-554[»]
5E14X-ray2.22A/B298-554[»]
5E15X-ray2.10A/B298-554[»]
5E19X-ray2.24A/B298-554[»]
5E1CX-ray1.98A/B298-554[»]
5EGVX-ray2.86A/B298-554[»]
5EHJX-ray2.50A/B298-554[»]
5EI1X-ray2.40A/B298-554[»]
5EITX-ray2.68A/B298-554[»]
5FQPX-ray1.88A307-554[»]
5FQRX-ray1.88A307-554[»]
5FQSX-ray1.94A307-554[»]
5FQTX-ray1.99A307-554[»]
5FQVX-ray1.74A307-554[»]
5HYRX-ray2.27A/B302-559[»]
DisProtiDP00074.
ProteinModelPortaliP03372.
SMRiP03372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03372.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 184Modulating (transactivation AF-1); mediates interaction with MACROD11 PublicationAdd BLAST184
Regioni35 – 174Interaction with DDX5; self-associationAdd BLAST140
Regioni35 – 47Required for interaction with NCOA1Add BLAST13
Regioni185 – 310Mediates interaction with DNTTIP21 PublicationAdd BLAST126
Regioni251 – 310HingeAdd BLAST60
Regioni262 – 595Interaction with AKAP131 PublicationAdd BLAST334
Regioni264 – 595Self-associationAdd BLAST332
Regioni311 – 595Transactivation AF-2Add BLAST285
Regioni311 – 551Steroid-bindingAdd BLAST241

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner. AF-1 seems to provide the major transactivation function in differentiated cells.

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Transmembrane, Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOVERGENiHBG108344.
InParanoidiP03372.
KOiK08550.
OMAiAFYRPNS.
OrthoDBiEOG091G03V4.
PhylomeDBiP03372.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR001292. Oestr_rcpt.
IPR024736. Oestrogen-typ_rcpt_final_C_dom.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSiPR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P03372-1) [UniParc]FASTAAdd to basket
Also known as: Long, hER-alpha66, ER66

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA
60 70 80 90 100
VYNYPEGAAY EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL
110 120 130 140 150
NSVSPSPLML LHPPPQLSPF LQPHGQQVPY YLENEPSGYT VREAGPPAFY
160 170 180 190 200
RPNSDNRRQG GRERLASTND KGSMAMESAK ETRYCAVCND YASGYHYGVW
210 220 230 240 250
SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC RLRKCYEVGM
260 270 280 290 300
MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR
310 320 330 340 350
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA
360 370 380 390 400
DRELVHMINW AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG
410 420 430 440 450
KLLFAPNLLL DRNQGKCVEG MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS
460 470 480 490 500
IILLNSGVYT FLSSTLKSLE EKDHIHRVLD KITDTLIHLM AKAGLTLQQQ
510 520 530 540 550
HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL LEMLDAHRLH
560 570 580 590
APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV
Length:595
Mass (Da):66,216
Last modified:June 1, 1994 - v2
Checksum:i5455C57AB0CCCAA7
GO
Isoform 2 (identifier: P03372-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     255-366: Missing.

Show »
Length:483
Mass (Da):53,687
Checksum:i449BC03EF22E80A5
GO
Isoform 3 (identifier: P03372-3) [UniParc]FASTAAdd to basket
Also known as: hER-alpha46, ER46

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:422
Mass (Da):47,629
Checksum:iC51DF9A9644127C0
GO
Isoform 4 (identifier: P03372-4) [UniParc]FASTAAdd to basket
Also known as: hER-alpha36, ER36

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.
     458-595: VYTFLSSTLK...GEAEGFPATV → FTISHVEAKKRILNLHPKIFGNKWFPRV

Note: Produced by alternative splicing of isoform 3.
Show »
Length:312
Mass (Da):35,547
Checksum:i85C8DEAD873F9AEC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti452I → L in CAE45969 (PubMed:17974005).Curated1

Polymorphismi

Genetic variations in ESR1 are correlated with bone mineral density (BMD). Low BMD is a risk factor for osteoporotic fracture. Osteoporosis is characterized by reduced bone mineral density, disruption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0330286H → Y in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs139960913dbSNPEnsembl.1
Natural variantiVAR_01890577G → S.1 PublicationCorresponds to variant rs9340773dbSNPEnsembl.1
Natural variantiVAR_004671160G → C.1 PublicationCorresponds to variant rs149308960dbSNPEnsembl.1
Natural variantiVAR_033029264M → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_004672364V → E in ESTRR; dominant-negative inhibitor of the wild-type ESR. 1 PublicationCorresponds to variant rs121913044dbSNPEnsembl.1
Natural variantiVAR_070072375Q → H in ESTRR; results in highly reduced activity. 1 PublicationCorresponds to variant rs397509428dbSNPEnsembl.1
Natural variantiVAR_004673400G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. 1 Publication1
Natural variantiVAR_010143411D → RNQGKCVEGMVEIFDMLLAT SSRFRMMNLQGEEFVCLKSI ILLNSGVYTFLSSTLKSLEE KDHIHRVLDKITDTLIHLMA KAGLTLQQQHQRLAQLLLIL SHIRHM in a 80 kDa form found in a breast cancer line; contains an in-frame duplication of exons 6 and 7. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0424601 – 173Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST173
Alternative sequenceiVSP_003680255 – 366Missing in isoform 2. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_042461458 – 595VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4. 2 PublicationsAdd BLAST138

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03635 mRNA. Translation: CAA27284.1.
M12674 mRNA. Translation: AAA52399.1.
U47678 mRNA. Translation: AAB00115.1.
AY425004 Genomic DNA. Translation: AAQ91815.1.
BX640939 mRNA. Translation: CAE45969.1.
AL356311
, AL049821, AL078582, AL590993 Genomic DNA. Translation: CAI21012.1.
AL049821
, AL078582, AL356311, AL590993 Genomic DNA. Translation: CAI22123.1.
AL590993
, AL049821, AL078582, AL356311 Genomic DNA. Translation: CAI14237.1.
AL078582, AL356311, AL590993 Genomic DNA. Translation: CAI42285.1.
CH471051 Genomic DNA. Translation: EAW47740.1.
BC128573 mRNA. Translation: AAI28574.1.
BC128574 mRNA. Translation: AAI28575.1.
AH008151 Genomic DNA. Translation: AAD52984.1.
X73067 mRNA. Translation: CAA51528.1.
Z75126 mRNA. Translation: CAA99436.1.
CCDSiCCDS5234.1. [P03372-1]
PIRiS64737.
RefSeqiNP_000116.2. NM_000125.3. [P03372-1]
NP_001116212.1. NM_001122740.1. [P03372-1]
NP_001116213.1. NM_001122741.1. [P03372-1]
NP_001116214.1. NM_001122742.1. [P03372-1]
NP_001278159.1. NM_001291230.1.
NP_001278170.1. NM_001291241.1.
NP_001315029.1. NM_001328100.1.
XP_006715438.1. XM_006715375.3. [P03372-3]
XP_011533845.1. XM_011535543.2. [P03372-1]
XP_011533846.1. XM_011535544.2. [P03372-1]
XP_011533847.1. XM_011535545.2. [P03372-1]
XP_016865865.1. XM_017010376.1. [P03372-1]
XP_016865866.1. XM_017010377.1. [P03372-1]
XP_016865867.1. XM_017010378.1. [P03372-1]
XP_016865868.1. XM_017010379.1. [P03372-1]
XP_016865869.1. XM_017010380.1. [P03372-1]
XP_016865870.1. XM_017010381.1. [P03372-1]
UniGeneiHs.208124.
Hs.744830.

Genome annotation databases

EnsembliENST00000206249; ENSP00000206249; ENSG00000091831. [P03372-1]
ENST00000338799; ENSP00000342630; ENSG00000091831. [P03372-1]
ENST00000440973; ENSP00000405330; ENSG00000091831. [P03372-1]
ENST00000443427; ENSP00000387500; ENSG00000091831. [P03372-1]
GeneIDi2099.
KEGGihsa:2099.
UCSCiuc003qom.5. human. [P03372-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Estrogen receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03635 mRNA. Translation: CAA27284.1.
M12674 mRNA. Translation: AAA52399.1.
U47678 mRNA. Translation: AAB00115.1.
AY425004 Genomic DNA. Translation: AAQ91815.1.
BX640939 mRNA. Translation: CAE45969.1.
AL356311
, AL049821, AL078582, AL590993 Genomic DNA. Translation: CAI21012.1.
AL049821
, AL078582, AL356311, AL590993 Genomic DNA. Translation: CAI22123.1.
AL590993
, AL049821, AL078582, AL356311 Genomic DNA. Translation: CAI14237.1.
AL078582, AL356311, AL590993 Genomic DNA. Translation: CAI42285.1.
CH471051 Genomic DNA. Translation: EAW47740.1.
BC128573 mRNA. Translation: AAI28574.1.
BC128574 mRNA. Translation: AAI28575.1.
AH008151 Genomic DNA. Translation: AAD52984.1.
X73067 mRNA. Translation: CAA51528.1.
Z75126 mRNA. Translation: CAA99436.1.
CCDSiCCDS5234.1. [P03372-1]
PIRiS64737.
RefSeqiNP_000116.2. NM_000125.3. [P03372-1]
NP_001116212.1. NM_001122740.1. [P03372-1]
NP_001116213.1. NM_001122741.1. [P03372-1]
NP_001116214.1. NM_001122742.1. [P03372-1]
NP_001278159.1. NM_001291230.1.
NP_001278170.1. NM_001291241.1.
NP_001315029.1. NM_001328100.1.
XP_006715438.1. XM_006715375.3. [P03372-3]
XP_011533845.1. XM_011535543.2. [P03372-1]
XP_011533846.1. XM_011535544.2. [P03372-1]
XP_011533847.1. XM_011535545.2. [P03372-1]
XP_016865865.1. XM_017010376.1. [P03372-1]
XP_016865866.1. XM_017010377.1. [P03372-1]
XP_016865867.1. XM_017010378.1. [P03372-1]
XP_016865868.1. XM_017010379.1. [P03372-1]
XP_016865869.1. XM_017010380.1. [P03372-1]
XP_016865870.1. XM_017010381.1. [P03372-1]
UniGeneiHs.208124.
Hs.744830.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A52X-ray2.80A/B297-554[»]
1AKFmodel-A309-547[»]
1EREX-ray3.10A/B/C/D/E/F301-553[»]
1ERRX-ray2.60A/B301-553[»]
1G50X-ray2.90A/B/C304-550[»]
1GWQX-ray2.45A/B301-548[»]
1GWRX-ray2.40A/B305-549[»]
1HCPNMR-A180-254[»]
1HCQX-ray2.40A/B/E/F180-262[»]
1L2IX-ray1.95A/B297-554[»]
1PCGX-ray2.70A/B304-547[»]
1QKTX-ray2.20A304-551[»]
1QKUX-ray3.20A/B/C301-550[»]
1R5KX-ray2.70A/B/C297-554[»]
1SJ0X-ray1.90A307-554[»]
1UOMX-ray2.28A301-553[»]
1X7EX-ray2.80A/B305-549[»]
1X7RX-ray2.00A305-549[»]
1XP1X-ray1.80A307-554[»]
1XP6X-ray1.70A307-554[»]
1XP9X-ray1.80A307-554[»]
1XPCX-ray1.60A307-554[»]
1XQCX-ray2.05A/B/C/D301-553[»]
1YIMX-ray1.90A307-554[»]
1YINX-ray2.20A307-554[»]
1ZKYX-ray2.25A/B298-554[»]
2AYRX-ray1.90A304-551[»]
2B1VX-ray1.80A/B298-554[»]
2B1ZX-ray1.78A/B298-554[»]
2B23X-ray2.10A/B298-554[»]
2BJ4X-ray2.00A/B305-533[»]
2FAIX-ray2.10A/B298-554[»]
2G44X-ray2.65A/B298-554[»]
2G5OX-ray2.30A/B298-554[»]
2I0JX-ray2.90A/B/C/D304-547[»]
2IOGX-ray1.60A309-554[»]
2IOKX-ray2.40A/B301-554[»]
2JF9X-ray2.10A/B/C304-533[»]
2JFAX-ray2.55A/B304-533[»]
2LLONMR-B287-305[»]
2LLQNMR-B287-305[»]
2OCFX-ray2.95A298-595[»]
2OUZX-ray2.00A301-553[»]
2P15X-ray1.94A/B298-554[»]
2POGX-ray1.84A/B304-551[»]
2Q6JX-ray2.70A/B298-554[»]
2Q70X-ray1.95A/B304-551[»]
2QA6X-ray2.60A/B298-554[»]
2QA8X-ray1.85A/B298-554[»]
2QABX-ray1.89A/B298-554[»]
2QE4X-ray2.40A/B304-551[»]
2QGTX-ray2.15A/B298-554[»]
2QGWX-ray2.39A/B298-554[»]
2QH6X-ray2.70A/B298-554[»]
2QR9X-ray2.00A/B298-554[»]
2QSEX-ray1.85A/B298-554[»]
2QXMX-ray2.30A/B298-554[»]
2QXSX-ray1.70A/B298-554[»]
2QZOX-ray1.72A/B298-554[»]
2R6WX-ray2.00A/B304-551[»]
2R6YX-ray2.00A/B304-551[»]
2YATX-ray2.60A301-551[»]
2YJAX-ray1.82B299-551[»]
3CBMX-ray1.69B298-307[»]
3CBOX-ray1.65B298-307[»]
3CBPX-ray1.42B298-307[»]
3DT3X-ray2.40A/B299-551[»]
3ERDX-ray2.03A/B297-554[»]
3ERTX-ray1.90A297-554[»]
3HLVX-ray3.00A/B298-550[»]
3HM1X-ray2.33A/B298-550[»]
3L03X-ray1.90A/B298-550[»]
3OS8X-ray2.03A/B/C/D299-553[»]
3OS9X-ray2.30A/B/C/D299-553[»]
3OSAX-ray2.30A/B/C/D299-553[»]
3Q95X-ray2.05A/B298-554[»]
3Q97X-ray2.10A/B298-554[»]
3UU7X-ray2.20A/B302-552[»]
3UUAX-ray2.05A/B302-552[»]
3UUCX-ray2.10A/B/C/D302-552[»]
3UUDX-ray1.60A/B302-552[»]
4AA6X-ray2.60A/B/E/F182-252[»]
4DMAX-ray2.30A/B303-549[»]
4IU7X-ray2.29A/B303-549[»]
4IUIX-ray2.30A/B303-549[»]
4IV2X-ray2.14A/B303-549[»]
4IV4X-ray2.30A/B303-549[»]
4IVWX-ray2.06A/B303-549[»]
4IVYX-ray1.95A/B303-549[»]
4IW6X-ray1.98A/B303-549[»]
4IW8X-ray2.04A/B303-549[»]
4IWCX-ray2.24A/B303-549[»]
4IWFX-ray1.93A/B303-549[»]
4JC3X-ray2.05B585-595[»]
4JDDX-ray2.10B585-595[»]
4MG5X-ray2.05A/B302-552[»]
4MG6X-ray2.10A/B302-552[»]
4MG7X-ray2.15A/B302-552[»]
4MG8X-ray1.85A/B302-552[»]
4MG9X-ray2.00A/B302-552[»]
4MGAX-ray1.80A/B302-552[»]
4MGBX-ray1.85A/B302-552[»]
4MGCX-ray2.15A/B302-552[»]
4MGDX-ray1.90A/B302-552[»]
4O6FX-ray2.82B261-271[»]
4PP6X-ray2.20A/B305-548[»]
4PPPX-ray2.69A/B305-548[»]
4PPSX-ray1.93A/B305-548[»]
4PXMX-ray1.90A/B299-554[»]
4Q13X-ray2.24A/B299-554[»]
4Q50X-ray3.07A/B/C/D/E/F/G/H299-554[»]
4TUZX-ray1.90A/B302-552[»]
4TV1X-ray1.85A/B302-552[»]
4XI3X-ray2.49A/B/C/D306-548[»]
4ZN7X-ray1.93A/B301-559[»]
4ZN9X-ray2.21A/B301-559[»]
4ZNHX-ray1.93A/B301-559[»]
4ZNSX-ray1.86A/B301-559[»]
4ZNTX-ray1.90A/B301-559[»]
4ZNUX-ray2.40A/B301-559[»]
4ZNVX-ray1.77A/B301-559[»]
4ZNWX-ray2.31A/B301-559[»]
4ZUBX-ray2.39A/B304-549[»]
4ZUCX-ray1.82A/B305-549[»]
4ZWHX-ray1.85A/B303-549[»]
4ZWKX-ray2.07A/B303-549[»]
5AAUX-ray1.90A/B307-554[»]
5AAVX-ray1.95A307-554[»]
B306-554[»]
5ACCX-ray1.88A307-554[»]
5AK2X-ray2.19A/B307-554[»]
5BNUX-ray1.60A/B303-548[»]
5BP6X-ray2.03A/B303-548[»]
5BPRX-ray1.91A/B303-549[»]
5BQ4X-ray1.78A/B303-549[»]
5DI7X-ray2.24A/B298-554[»]
5DIDX-ray2.24A/B298-554[»]
5DIEX-ray2.24A/B298-554[»]
5DIGX-ray2.24A/B298-554[»]
5DK9X-ray2.28A/B298-554[»]
5DKBX-ray2.40A/B298-554[»]
5DKEX-ray2.60A/B298-554[»]
5DKGX-ray2.15A/B298-554[»]
5DKSX-ray2.60A/B298-554[»]
5DL4X-ray2.10A/B298-554[»]
5DLRX-ray2.26A/B298-554[»]
5DMCX-ray2.40A/B298-554[»]
5DMFX-ray2.40A/B298-554[»]
5DP0X-ray2.38A/B298-554[»]
5DRJX-ray2.07A/B298-554[»]
5DRMX-ray2.24A/B298-554[»]
5DTVX-ray2.29A/B298-554[»]
5DU5X-ray2.19A/B298-554[»]
5DUEX-ray2.09A/B298-554[»]
5DUGX-ray2.25A/B298-554[»]
5DUHX-ray2.24A/B298-554[»]
5DVSX-ray2.28A/B298-554[»]
5DVVX-ray2.50A/B298-554[»]
5DWEX-ray1.92A/B298-554[»]
5DWGX-ray2.30A/B298-554[»]
5DWIX-ray2.43A/B298-554[»]
5DWJX-ray2.00A/B298-554[»]
5DX3X-ray2.09A/B297-554[»]
5DXBX-ray2.08A/B297-554[»]
5DXEX-ray1.50A/B297-554[»]
5DXGX-ray1.86A/B297-554[»]
5DXKX-ray2.23A/B298-554[»]
5DXMX-ray2.37A/B298-554[»]
5DXPX-ray2.20A/B298-554[»]
5DXQX-ray2.40A/B298-554[»]
5DXRX-ray2.28A/B298-554[»]
5DY8X-ray2.03A/B298-554[»]
5DYBX-ray2.27A/B298-554[»]
5DYDX-ray2.48A/B298-554[»]
5DZ0X-ray2.24A/B298-554[»]
5DZ1X-ray2.20A/B298-554[»]
5DZ3X-ray2.15A/B298-554[»]
5DZHX-ray2.11A/B298-554[»]
5DZIX-ray1.90A/B298-554[»]
5E0WX-ray2.00A/B298-554[»]
5E0XX-ray2.01A/B298-554[»]
5E14X-ray2.22A/B298-554[»]
5E15X-ray2.10A/B298-554[»]
5E19X-ray2.24A/B298-554[»]
5E1CX-ray1.98A/B298-554[»]
5EGVX-ray2.86A/B298-554[»]
5EHJX-ray2.50A/B298-554[»]
5EI1X-ray2.40A/B298-554[»]
5EITX-ray2.68A/B298-554[»]
5FQPX-ray1.88A307-554[»]
5FQRX-ray1.88A307-554[»]
5FQSX-ray1.94A307-554[»]
5FQTX-ray1.99A307-554[»]
5FQVX-ray1.74A307-554[»]
5HYRX-ray2.27A/B302-559[»]
DisProtiDP00074.
ProteinModelPortaliP03372.
SMRiP03372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108403. 699 interactors.
DIPiDIP-5965N.
IntActiP03372. 465 interactors.
MINTiMINT-129047.
STRINGi9606.ENSP00000206249.

Chemistry databases

BindingDBiP03372.
ChEMBLiCHEMBL206.
DrugBankiDB01431. Allylestrenol.
DB06401. Bazedoxifene.
DB00882. Clomifene.
DB00286. Conjugated Estrogens.
DB01406. Danazol.
DB00304. Desogestrel.
DB00890. Dienestrol.
DB00255. Diethylstilbestrol.
DB00783. Estradiol.
DB01196. Estramustine.
DB04573. Estriol.
DB00655. Estrone.
DB04574. Estropipate.
DB00977. Ethinyl Estradiol.
DB00823. Ethynodiol.
DB00294. Etonogestrel.
DB01185. Fluoxymesterone.
DB00947. Fulvestrant.
DB00367. Levonorgestrel.
DB00603. Medroxyprogesterone Acetate.
DB01065. Melatonin.
DB01357. Mestranol.
DB01183. Naloxone.
DB00957. Norgestimate.
DB04938. Ospemifene.
DB00396. Progesterone.
DB04575. Quinestrol.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB00539. Toremifene.
DB01108. Trilostane.
GuidetoPHARMACOLOGYi620.
SwissLipidsiSLP:000001568.

PTM databases

iPTMnetiP03372.
PhosphoSitePlusiP03372.
SwissPalmiP03372.
UniCarbKBiP03372.

Polymorphism and mutation databases

BioMutaiESR1.
DMDMi544257.

Proteomic databases

EPDiP03372.
PaxDbiP03372.
PeptideAtlasiP03372.
PRIDEiP03372.

Protocols and materials databases

DNASUi2099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000206249; ENSP00000206249; ENSG00000091831. [P03372-1]
ENST00000338799; ENSP00000342630; ENSG00000091831. [P03372-1]
ENST00000440973; ENSP00000405330; ENSG00000091831. [P03372-1]
ENST00000443427; ENSP00000387500; ENSG00000091831. [P03372-1]
GeneIDi2099.
KEGGihsa:2099.
UCSCiuc003qom.5. human. [P03372-1]

Organism-specific databases

CTDi2099.
DisGeNETi2099.
GeneCardsiESR1.
HGNCiHGNC:3467. ESR1.
HPAiCAB000037.
CAB055099.
CAB072858.
HPA000449.
HPA000450.
MalaCardsiESR1.
MIMi133430. gene.
615363. phenotype.
neXtProtiNX_P03372.
OpenTargetsiENSG00000091831.
Orphaneti785. Estrogen resistance syndrome.
PharmGKBiPA156.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOVERGENiHBG108344.
InParanoidiP03372.
KOiK08550.
OMAiAFYRPNS.
OrthoDBiEOG091G03V4.
PhylomeDBiP03372.
TreeFamiTF323751.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091831-MONOMER.
ReactomeiR-HSA-1251985. Nuclear signaling by ERBB4.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLinkiP03372.
SIGNORiP03372.

Miscellaneous databases

ChiTaRSiESR1. human.
EvolutionaryTraceiP03372.
GeneWikiiEstrogen_receptor_alpha.
GenomeRNAii2099.
PROiP03372.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000091831.
CleanExiHS_ESR1.
ExpressionAtlasiP03372. baseline and differential.
GenevisibleiP03372. HS.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR001292. Oestr_rcpt.
IPR024736. Oestrogen-typ_rcpt_final_C_dom.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSiPR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiESR1_HUMAN
AccessioniPrimary (citable) accession number: P03372
Secondary accession number(s): Q13511
, Q14276, Q5T5H7, Q6MZQ9, Q9NU51, Q9UDZ7, Q9UIS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 235 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Selective estrogen receptor modulators (SERMs), such as tamoxifen, raloxifene, toremifene, lasofoxifene, clomifene, femarelle and ormeloxifene, have tissue selective agonistic and antagonistic effects on the estrogen receptor (ER). They interfere with the ER association with coactivators or corepressors, mainly involving the AF-2 domain.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.