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P03372

- ESR1_HUMAN

UniProt

P03372 - ESR1_HUMAN

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Protein
Estrogen receptor
Gene
ESR1, ESR, NR3A1
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Isoform 3 can bind to ERE and inhibit isoform 1.19 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi185 – 25066Nuclear receptor
Add
BLAST
Zinc fingeri185 – 20521NR C4-type
Add
BLAST
Zinc fingeri221 – 24525NR C4-type
Add
BLAST

GO - Molecular functioni

  1. beta-catenin binding Source: BHF-UCL
  2. chromatin binding Source: Ensembl
  3. core promoter sequence-specific DNA binding Source: UniProtKB
  4. enzyme binding Source: UniProtKB
  5. estrogen receptor activity Source: UniProtKB
  6. estrogen response element binding Source: UniProtKB
  7. estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  8. identical protein binding Source: IntAct
  9. nitric-oxide synthase regulator activity Source: UniProtKB
  10. protein binding Source: IntAct
  11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  12. steroid binding Source: UniProtKB
  13. steroid hormone receptor activity Source: ProtInc
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. androgen metabolic process Source: Ensembl
  2. antral ovarian follicle growth Source: Ensembl
  3. cellular response to estradiol stimulus Source: UniProtKB
  4. chromatin remodeling Source: UniProtKB
  5. epithelial cell development Source: Ensembl
  6. epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
  7. gene expression Source: Reactome
  8. intracellular estrogen receptor signaling pathway Source: UniProtKB
  9. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  10. male gonad development Source: Ensembl
  11. mammary gland alveolus development Source: Ensembl
  12. mammary gland branching involved in pregnancy Source: Ensembl
  13. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  14. negative regulation of gene expression Source: UniProtKB
  15. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  16. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  17. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  18. positive regulation of fibroblast proliferation Source: Ensembl
  19. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  20. positive regulation of nitric-oxide synthase activity Source: UniProtKB
  21. positive regulation of phospholipase C activity Source: UniProtKB
  22. positive regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
  23. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  24. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  25. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
  26. prostate epithelial cord elongation Source: Ensembl
  27. regulation of apoptotic process Source: Ensembl
  28. regulation of branching involved in prostate gland morphogenesis Source: Ensembl
  29. regulation of transcription, DNA-templated Source: UniProtKB
  30. response to estradiol Source: BHF-UCL
  31. response to estrogen Source: UniProtKB
  32. signal transduction Source: ProtInc
  33. transcription initiation from RNA polymerase II promoter Source: Reactome
  34. transcription, DNA-templated Source: ProtInc
  35. uterus development Source: Ensembl
  36. vagina development Source: Ensembl
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

ReactomeiREACT_116022. Nuclear signaling by ERBB4.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP03372.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3467. ESR1.

Subcellular locationi

Isoform 1 : Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side
Note: A minor fraction is associated with the inner membrane.8 Publications
Isoform 3 : Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Single-pass type I membrane protein
Note: Associated with the inner membrane via palmitoylation Inferred. At least a subset exists as a transmembrane protein with a N-terminal extracellular domain.8 Publications
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.8 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Estrogen resistance (ESTRR) [MIM:615363]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti364 – 3641V → E in ESTRR; dominant-negative inhibitor of the wild-type ESR. 1 Publication
VAR_004672
Natural varianti375 – 3751Q → H in ESTRR; results in highly reduced activity. 1 Publication
VAR_070072

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391L → P: Impairs AF-1 transactivation. 1 Publication
Mutagenesisi43 – 431Y → P: Impairs AF-1 transactivation. 1 Publication
Mutagenesisi104 – 1041S → A: Loss of cyclin A-dependent induction of transcriptional activation.
Mutagenesisi106 – 1061S → A: Loss of cyclin A-dependent induction of transcriptional activation.
Mutagenesisi118 – 1181S → A: Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications
Mutagenesisi118 – 1181S → E: Enhances transactivation activity. Enhances interaction with DDX5. Insensitive to PPP5C inhibition of transactivation activity. 2 Publications
Mutagenesisi260 – 2601R → A or K: Loss of methylation. 1 Publication
Mutagenesisi386 – 3861I → 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 Publication
Mutagenesisi447 – 4471C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. 1 Publication
Mutagenesisi539 – 5391L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615363. phenotype.
Orphaneti785. Estrogen resistance syndrome.
PharmGKBiPA156.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Estrogen receptor
PRO_0000053618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi10 – 101O-linked (GlcNAc) By similarity
Modified residuei104 – 1041Phosphoserine; by CDK21 Publication
Modified residuei106 – 1061Phosphoserine; by CDK21 Publication
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei167 – 1671Phosphoserine; by CK21 Publication
Modified residuei260 – 2601Asymmetric dimethylarginine; by PRMT11 Publication
Lipidationi447 – 4471S-palmitoyl cysteine By similarity
Modified residuei537 – 5371Phosphotyrosine; by Tyr-kinases1 Publication

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.6 Publications
Glycosylated; contains N-acetylglucosamine, probably O-linked.1 Publication
Ubiquitinated. Deubiquitinated by OTUB1.1 Publication
Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization.1 Publication
Palmitoylated (isoform 3). Not biotinylated (isoform 3).2 Publications
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.2 Publications

Keywords - PTMi

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

Proteomic databases

PaxDbiP03372.
PRIDEiP03372.

PTM databases

PhosphoSiteiP03372.
UniCarbKBiP03372.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP03372.
BgeeiP03372.
CleanExiHS_ESR1.
GenevestigatoriP03372.

Organism-specific databases

HPAiCAB000037.
CAB055099.
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 ESE1 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.50 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
DDX17Q928417EBI-78473,EBI-746012
DDX5P178448EBI-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
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

Protein-protein interaction databases

BioGridi108403. 529 interactions.
DIPiDIP-5965N.
IntActiP03372. 376 interactions.
MINTiMINT-129047.
STRINGi9606.ENSP00000206249.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni186 – 1883
Beta strandi189 – 1913
Beta strandi194 – 1963
Beta strandi199 – 2013
Helixi203 – 21311
Beta strandi222 – 2254
Turni231 – 2366
Helixi238 – 24811
Helixi288 – 2914
Helixi302 – 3043
Helixi307 – 3093
Helixi312 – 32110
Beta strandi330 – 3323
Beta strandi334 – 3363
Helixi337 – 3393
Helixi342 – 36322
Helixi367 – 3693
Helixi372 – 39524
Beta strandi396 – 3983
Beta strandi401 – 4055
Beta strandi408 – 4114
Helixi412 – 4154
Beta strandi417 – 4204
Helixi421 – 43818
Helixi442 – 45514
Turni456 – 4594
Helixi466 – 49227
Helixi497 – 52529
Beta strandi528 – 5303
Beta strandi531 – 5333
Helixi536 – 5449
Turni546 – 5483

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4O6FX-ray2.82B261-271[»]
4PP6X-ray2.20A/B305-548[»]
4PPPX-ray2.69A/B305-548[»]
4PPSX-ray1.93A/B305-548[»]
DisProtiDP00074.
ProteinModelPortaliP03372.
SMRiP03372. Positions 180-551.

Miscellaneous databases

EvolutionaryTraceiP03372.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 184184Modulating (transactivation AF-1); mediates interaction with MACROD1
Add
BLAST
Regioni35 – 174140Interaction with DDX5; self-association
Add
BLAST
Regioni35 – 4713Required for interaction with NCOA1
Add
BLAST
Regioni185 – 310126Mediates interaction with DNTTIP2
Add
BLAST
Regioni251 – 31060Hinge
Add
BLAST
Regioni262 – 595334Interaction with AKAP13
Add
BLAST
Regioni264 – 595332Self-association
Add
BLAST
Regioni311 – 595285Transactivation AF-2
Add
BLAST
Regioni311 – 551241Steroid-binding
Add
BLAST

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

Keywords - Domaini

Transmembrane, Zinc-finger

Phylogenomic databases

eggNOGiNOG320746.
HOVERGENiHBG108344.
InParanoidiP03372.
KOiK08550.
OrthoDBiEOG7288S1.
PhylomeDBiP03372.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR001292. Oestr_rcpt.
IPR024736. Oestrogen-typ_rcpt_final_C_dom.
IPR001723. Str_hrmn_rcpt.
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. Align

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

MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA    50
VYNYPEGAAY EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL 100
NSVSPSPLML LHPPPQLSPF LQPHGQQVPY YLENEPSGYT VREAGPPAFY 150
RPNSDNRRQG GRERLASTND KGSMAMESAK ETRYCAVCND YASGYHYGVW 200
SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC RLRKCYEVGM 250
MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR 300
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA 350
DRELVHMINW AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG 400
KLLFAPNLLL DRNQGKCVEG MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS 450
IILLNSGVYT FLSSTLKSLE EKDHIHRVLD KITDTLIHLM AKAGLTLQQQ 500
HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL LEMLDAHRLH 550
APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV 595
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

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, disrutption 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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61H → Y in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs139960913 [ dbSNP | Ensembl ].
VAR_033028
Natural varianti77 – 771G → S.1 Publication
Corresponds to variant rs9340773 [ dbSNP | Ensembl ].
VAR_018905
Natural varianti160 – 1601G → C.1 Publication
Corresponds to variant rs149308960 [ dbSNP | Ensembl ].
VAR_004671
Natural varianti264 – 2641M → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_033029
Natural varianti364 – 3641V → E in ESTRR; dominant-negative inhibitor of the wild-type ESR. 1 Publication
VAR_004672
Natural varianti375 – 3751Q → H in ESTRR; results in highly reduced activity. 1 Publication
VAR_070072
Natural varianti400 – 4001G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. 1 Publication
VAR_004673
Natural varianti411 – 4111D → 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.
VAR_010143

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 173173Missing in isoform 3 and isoform 4.
VSP_042460Add
BLAST
Alternative sequencei255 – 366112Missing in isoform 2.
VSP_003680Add
BLAST
Alternative sequencei458 – 595138VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4.
VSP_042461Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti452 – 4521I → L in CAE45969. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
XP_006715438.1. XM_006715375.1. [P03372-3]
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]
ENST00000456483; ENSP00000415934; ENSG00000091831. [P03372-2]
GeneIDi2099.
KEGGihsa:2099.
UCSCiuc003qom.4. human. [P03372-1]

Polymorphism databases

DMDMi544257.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5234.1. [P03372-1 ]
PIRi S64737.
RefSeqi NP_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.
XP_006715438.1. XM_006715375.1. [P03372-3 ]
UniGenei Hs.208124.
Hs.744830.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A52 X-ray 2.80 A/B 297-554 [» ]
1AKF model - A 309-547 [» ]
1ERE X-ray 3.10 A/B/C/D/E/F 301-553 [» ]
1ERR X-ray 2.60 A/B 301-553 [» ]
1G50 X-ray 2.90 A/B/C 304-550 [» ]
1GWQ X-ray 2.45 A/B 301-548 [» ]
1GWR X-ray 2.40 A/B 305-549 [» ]
1HCP NMR - A 180-254 [» ]
1HCQ X-ray 2.40 A/B/E/F 180-262 [» ]
1L2I X-ray 1.95 A/B 297-554 [» ]
1PCG X-ray 2.70 A/B 304-547 [» ]
1QKT X-ray 2.20 A 304-551 [» ]
1QKU X-ray 3.20 A/B/C 301-550 [» ]
1R5K X-ray 2.70 A/B/C 297-554 [» ]
1SJ0 X-ray 1.90 A 307-554 [» ]
1UOM X-ray 2.28 A 301-553 [» ]
1X7E X-ray 2.80 A/B 305-549 [» ]
1X7R X-ray 2.00 A 305-549 [» ]
1XP1 X-ray 1.80 A 307-554 [» ]
1XP6 X-ray 1.70 A 307-554 [» ]
1XP9 X-ray 1.80 A 307-554 [» ]
1XPC X-ray 1.60 A 307-554 [» ]
1XQC X-ray 2.05 A/B/C/D 301-553 [» ]
1YIM X-ray 1.90 A 307-554 [» ]
1YIN X-ray 2.20 A 307-554 [» ]
1ZKY X-ray 2.25 A/B 298-554 [» ]
2AYR X-ray 1.90 A 304-551 [» ]
2B1V X-ray 1.80 A/B 298-554 [» ]
2B1Z X-ray 1.78 A/B 298-554 [» ]
2B23 X-ray 2.10 A/B 298-554 [» ]
2BJ4 X-ray 2.00 A/B 305-533 [» ]
2FAI X-ray 2.10 A/B 298-554 [» ]
2G44 X-ray 2.65 A/B 298-554 [» ]
2G5O X-ray 2.30 A/B 298-554 [» ]
2I0J X-ray 2.90 A/B/C/D 304-547 [» ]
2IOG X-ray 1.60 A 309-554 [» ]
2IOK X-ray 2.40 A/B 301-554 [» ]
2JF9 X-ray 2.10 A/B/C 304-533 [» ]
2JFA X-ray 2.55 A/B 304-533 [» ]
2LLO NMR - B 287-305 [» ]
2LLQ NMR - B 287-305 [» ]
2OCF X-ray 2.95 A 298-595 [» ]
2OUZ X-ray 2.00 A 301-553 [» ]
2P15 X-ray 1.94 A/B 298-554 [» ]
2POG X-ray 1.84 A/B 304-551 [» ]
2Q6J X-ray 2.70 A/B 298-554 [» ]
2Q70 X-ray 1.95 A/B 304-551 [» ]
2QA6 X-ray 2.60 A/B 298-554 [» ]
2QA8 X-ray 1.85 A/B 298-554 [» ]
2QAB X-ray 1.89 A/B 298-554 [» ]
2QE4 X-ray 2.40 A/B 304-551 [» ]
2QGT X-ray 2.15 A/B 298-554 [» ]
2QGW X-ray 2.39 A/B 298-554 [» ]
2QH6 X-ray 2.70 A/B 298-554 [» ]
2QR9 X-ray 2.00 A/B 298-554 [» ]
2QSE X-ray 1.85 A/B 298-554 [» ]
2QXM X-ray 2.30 A/B 298-554 [» ]
2QXS X-ray 1.70 A/B 298-554 [» ]
2QZO X-ray 1.72 A/B 298-554 [» ]
2R6W X-ray 2.00 A/B 304-551 [» ]
2R6Y X-ray 2.00 A/B 304-551 [» ]
2YAT X-ray 2.60 A 301-551 [» ]
2YJA X-ray 1.82 B 299-551 [» ]
3CBM X-ray 1.69 B 298-307 [» ]
3CBO X-ray 1.65 B 298-307 [» ]
3CBP X-ray 1.42 B 298-307 [» ]
3DT3 X-ray 2.40 A/B 299-551 [» ]
3ERD X-ray 2.03 A/B 297-554 [» ]
3ERT X-ray 1.90 A 297-554 [» ]
3HLV X-ray 3.00 A/B 298-550 [» ]
3HM1 X-ray 2.33 A/B 298-550 [» ]
3L03 X-ray 1.90 A/B 298-550 [» ]
3OS8 X-ray 2.03 A/B/C/D 299-553 [» ]
3OS9 X-ray 2.30 A/B/C/D 299-553 [» ]
3OSA X-ray 2.30 A/B/C/D 299-553 [» ]
3Q95 X-ray 2.05 A/B 298-554 [» ]
3Q97 X-ray 2.10 A/B 298-554 [» ]
3UU7 X-ray 2.20 A/B 302-552 [» ]
3UUA X-ray 2.05 A/B 302-552 [» ]
3UUC X-ray 2.10 A/B/C/D 302-552 [» ]
3UUD X-ray 1.60 A/B 302-552 [» ]
4AA6 X-ray 2.60 A/B/E/F 182-252 [» ]
4DMA X-ray 2.30 A/B 303-549 [» ]
4IU7 X-ray 2.29 A/B 303-549 [» ]
4IUI X-ray 2.30 A/B 303-549 [» ]
4IV2 X-ray 2.14 A/B 303-549 [» ]
4IV4 X-ray 2.30 A/B 303-549 [» ]
4IVW X-ray 2.06 A/B 303-549 [» ]
4IVY X-ray 1.95 A/B 303-549 [» ]
4IW6 X-ray 1.98 A/B 303-549 [» ]
4IW8 X-ray 2.04 A/B 303-549 [» ]
4IWC X-ray 2.24 A/B 303-549 [» ]
4IWF X-ray 1.93 A/B 303-549 [» ]
4JC3 X-ray 2.05 B 585-595 [» ]
4JDD X-ray 2.10 B 585-595 [» ]
4O6F X-ray 2.82 B 261-271 [» ]
4PP6 X-ray 2.20 A/B 305-548 [» ]
4PPP X-ray 2.69 A/B 305-548 [» ]
4PPS X-ray 1.93 A/B 305-548 [» ]
DisProti DP00074.
ProteinModelPortali P03372.
SMRi P03372. Positions 180-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108403. 529 interactions.
DIPi DIP-5965N.
IntActi P03372. 376 interactions.
MINTi MINT-129047.
STRINGi 9606.ENSP00000206249.

Chemistry

BindingDBi P03372.
ChEMBLi CHEMBL2093866.
DrugBanki DB00269. Chlorotrianisene.
DB00882. Clomifene.
DB00286. Conjugated Estrogens.
DB01406. Danazol.
DB00304. Desogestrel.
DB00890. Dienestrol.
DB00255. Diethylstilbestrol.
DB00858. Dromostanolone.
DB01395. Drospirenone.
DB00783. Estradiol.
DB01196. Estramustine.
DB04573. Estriol.
DB00655. Estrone.
DB00977. Ethinyl Estradiol.
DB00823. Ethynodiol Diacetate.
DB00294. Etonogestrel.
DB01185. Fluoxymesterone.
DB00947. Fulvestrant.
DB01006. Letrozole.
DB00367. Levonorgestrel.
DB00603. Medroxyprogesterone.
DB00351. Megestrol.
DB01065. Melatonin.
DB01357. Mestranol.
DB01183. Naloxone.
DB00957. Norgestimate.
DB00506. Norgestrel.
DB00396. Progesterone.
DB04575. Quinestrol.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB00539. Toremifene.
GuidetoPHARMACOLOGYi 620.

PTM databases

PhosphoSitei P03372.
UniCarbKBi P03372.

Polymorphism databases

DMDMi 544257.

Proteomic databases

PaxDbi P03372.
PRIDEi P03372.

Protocols and materials databases

DNASUi 2099.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000206249 ; ENSP00000206249 ; ENSG00000091831 . [P03372-1 ]
ENST00000338799 ; ENSP00000342630 ; ENSG00000091831 . [P03372-1 ]
ENST00000440973 ; ENSP00000405330 ; ENSG00000091831 . [P03372-1 ]
ENST00000443427 ; ENSP00000387500 ; ENSG00000091831 . [P03372-1 ]
ENST00000456483 ; ENSP00000415934 ; ENSG00000091831 . [P03372-2 ]
GeneIDi 2099.
KEGGi hsa:2099.
UCSCi uc003qom.4. human. [P03372-1 ]

Organism-specific databases

CTDi 2099.
GeneCardsi GC06P151985.
HGNCi HGNC:3467. ESR1.
HPAi CAB000037.
CAB055099.
HPA000449.
HPA000450.
MIMi 133430. gene.
615363. phenotype.
neXtProti NX_P03372.
Orphaneti 785. Estrogen resistance syndrome.
PharmGKBi PA156.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320746.
HOVERGENi HBG108344.
InParanoidi P03372.
KOi K08550.
OrthoDBi EOG7288S1.
PhylomeDBi P03372.
TreeFami TF323751.

Enzyme and pathway databases

Reactomei REACT_116022. Nuclear signaling by ERBB4.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P03372.

Miscellaneous databases

ChiTaRSi ESR1. human.
EvolutionaryTracei P03372.
GeneWikii Estrogen_receptor_alpha.
GenomeRNAii 2099.
NextBioi 8491.
PROi P03372.
SOURCEi Search...

Gene expression databases

ArrayExpressi P03372.
Bgeei P03372.
CleanExi HS_ESR1.
Genevestigatori P03372.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR001292. Oestr_rcpt.
IPR024736. Oestrogen-typ_rcpt_final_C_dom.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PIRSFi PIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSi PR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A."
    Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P., Chambon P.
    Nature 320:134-139(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Sequence and expression of human estrogen receptor complementary DNA."
    Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.
    Science 231:1150-1154(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "A novel 80 kDa human estrogen receptor containing a duplication of exons 6 and 7."
    Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.
    Nucleic Acids Res. 24:962-969(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  4. NIEHS SNPs program
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-77.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  6. "Identification, cloning, and expression of human estrogen receptor-alpha36, a novel variant of human estrogen receptor-alpha66."
    Wang Z., Zhang X., Shen P., Loggie B.W., Chang Y., Deuel T.F.
    Biochem. Biophys. Res. Commun. 336:1023-1027(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE PROMOTER USAGE, SUBCELLULAR LOCATION.
    Tissue: Placenta.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor."
    Joel P.B., Traish A.M., Lannigan D.A.
    Mol. Endocrinol. 9:1041-1052(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 110-117, PHOSPHORYLATION, MUTAGENESIS.
  11. "Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene and breast cancer susceptibility."
    Schubert E.L., Lee M.K., Newman B., King M.C.
    J. Steroid Biochem. Mol. Biol. 71:21-27(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 152-595 (ISOFORM 1).
  12. "Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-responsive human breast cancer cell lines."
    Pfeffer U., Fecarotta E., Castagnetta L., Vidali G.
    Cancer Res. 53:741-743(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 216-434, ALTERNATIVE SPLICING.
    Tissue: Mammary carcinoma.
  13. "Mechanisms of acquired tamoxifen resistance in a xenotransplanted human breast carcinoma."
    Naundorf H., Becker M., Fiebig C., Buettner B., Fichtner I.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 354-548.
    Tissue: Mammary carcinoma.
  14. "Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro."
    Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.
    Mol. Endocrinol. 9:24-33(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 532-542, PHOSPHORYLATION AT TYR-537.
  15. "Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation."
    Reese J.C., Katzenellenbogen B.S.
    J. Biol. Chem. 267:9868-9873(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-447.
  16. "Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor."
    Arnold S.F., Obourn J.D., Jaffe H., Notides A.C.
    Mol. Endocrinol. 8:1208-1214(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-167 BY CK2.
  17. "Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta."
    Stein B., Yang M.X.
    Mol. Cell. Biol. 15:4971-4979(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSREPRESSION OF NF-KAPPA-B.
  18. "Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha."
    Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S., Kato S.
    Mol. Cell. Biol. 19:5363-5372(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX5, MUTAGENESIS OF SER-118.
  19. "Identification of a new isoform of the human estrogen receptor-alpha (hER-alpha) that is encoded by distinct transcripts and that is able to repress hER-alpha activation function 1."
    Flouriot G., Brand H., Denger S., Metivier R., Kos M., Reid G., Sonntag-Buck V., Gannon F.
    EMBO J. 19:4688-4700(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE PROMOTER USAGE (ISOFORM 3), SUBUNIT.
  20. "Function of N-terminal transactivation domain of the estrogen receptor requires a potential alpha-helical structure and is negatively regulated by the A domain."
    Metivier R., Petit F.G., Valotaire Y., Pakdel F.
    Mol. Endocrinol. 14:1849-1871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-39 AND TYR-43.
  21. "Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells."
    Bai Y., Giguere V.
    Mol. Endocrinol. 17:589-599(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA1; NCOA2 AND NCOA3, SUBUNIT, MUTAGENESIS OF LEU-539.
  22. "Plasma membrane localization and function of the estrogen receptor alpha variant (ER46) in human endothelial cells."
    Li L., Haynes M.P., Bender J.R.
    Proc. Natl. Acad. Sci. U.S.A. 100:4807-4812(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), PALMITOYLATION (ISOFORM 3).
  23. "A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine."
    Jiang M.S., Hart G.W.
    J. Biol. Chem. 272:2421-2428(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  24. "Functional synergy between the transcription factor Sp1 and the estrogen receptor."
    Porter W., Saville B., Hoivik D., Safe S.
    Mol. Endocrinol. 11:1569-1580(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP1.
  25. "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action."
    Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.
    Oncogene 16:2513-2526(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP13.
  26. "Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex."
    Rogatsky I., Trowbridge J.M., Garabedian M.J.
    J. Biol. Chem. 274:22296-22302(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-104 AND SER-106, MUTAGENESIS.
  27. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
    Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
    J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  28. "An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens."
    Montano M.M., Ekena K., Delage-Mourroux R., Chang W., Martini P., Katzenellenbogen B.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:6947-6952(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHB2.
  29. "Synergy between estrogen receptor alpha activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2."
    Benecke A., Chambon P., Gronemeyer H.
    EMBO Rep. 1:151-157(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA2.
  30. "Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent activation at GC-rich (Sp1) promoter elements."
    Saville B., Wormke M., Wang F., Nguyen T., Enmark E., Kuiper G., Gustafsson J.A., Safe S.
    J. Biol. Chem. 275:5379-5387(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP1.
  31. "Inhibition of vascular endothelial growth factor expression in HEC1A endometrial cancer cells through interactions of estrogen receptor alpha and Sp3 proteins."
    Stoner M., Wang F., Wormke M., Nguyen T., Samudio I., Vyhlidal C., Marme D., Finkenzeller G., Safe S.
    J. Biol. Chem. 275:22769-22779(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP3.
  32. "Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein."
    Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., Isselbacher K.J., Brown M., Shioda T.
    Genes Dev. 15:2598-2612(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED1 AND EP300.
  33. "Characterization of the physical interaction between estrogen receptor alpha and JUN proteins."
    Teyssier C., Belguise K., Galtier F., Chalbos D.
    J. Biol. Chem. 276:36361-36369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JUN; JUNB AND JUND.
  34. "Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription."
    Chan S.W., Hong W.
    J. Biol. Chem. 276:28402-28412(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDM5A.
  35. "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
    Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
    Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA5.
  36. "Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains."
    Metivier R., Penot G., Flouriot G., Pakdel F.
    Mol. Endocrinol. 15:1953-1970(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCOA1 AND DDX5.
  37. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
    Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
    J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT2.
  38. "Suppression of estrogen receptor-mediated transcription and cell growth by interaction with TR2 orphan receptor."
    Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C.
    J. Biol. Chem. 277:33571-33579(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR2C1.
  39. "ERAP140, a conserved tissue-specific nuclear receptor coactivator."
    Shao W., Halachmi S., Brown M.
    Mol. Cell. Biol. 22:3358-3372(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA7.
  40. Cited for: INTERACTION WITH RBFOX2.
  41. "Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
    Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  42. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
    Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
    Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARD1.
  43. "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
    Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
    Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNTTIP2.
  44. "The relative contribution exerted by AF-1 and AF-2 transactivation functions in estrogen receptor alpha transcriptional activity depends upon the differentiation stage of the cell."
    Merot Y., Metivier R., Penot G., Manu D., Saligaut C., Gannon F., Pakdel F., Kah O., Flouriot G.
    J. Biol. Chem. 279:26184-26191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  45. "An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling."
    Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.
    J. Biol. Chem. 279:38721-38729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXNRD1.
  46. "Protein phosphatase 5 is a negative regulator of estrogen receptor-mediated transcription."
    Ikeda K., Ogawa S., Tsukui T., Horie-Inoue K., Ouchi Y., Kato S., Muramatsu M., Inoue S.
    Mol. Endocrinol. 18:1131-1143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-118, DEPHOSPHORYLATION AT SER-118 BY PPP5C, MUTAGENESIS OF SER-118.
  47. "Estrogen receptor inhibits interleukin-6 gene expression by disruption of nuclear factor kappaB transactivation."
    Liu H., Liu K., Bodenner D.L.
    Cytokine 31:251-257(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NF-KAPPA-B TRANSREPRESSION.
  48. "Functional regulation of oestrogen receptor pathway by the dynein light chain 1."
    Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R., Kumar R.
    EMBO Rep. 6:538-544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DYNLL1.
  49. "The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1."
    Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.
    Oncogene 24:5576-5588(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEXIM1.
  50. "Identification of the MLL2 complex as a coactivator for estrogen receptor alpha."
    Mo R., Rao S.M., Zhu Y.-J.
    J. Biol. Chem. 281:15714-15720(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KMT2D.
  51. "Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells."
    Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C., Peng S., Barnekow A., Kremerskothen J., Kumar R.
    J. Biol. Chem. 281:19092-19099(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  52. "MUC1 oncoprotein stabilizes and activates estrogen receptor alpha."
    Wei X., Xu H., Kufe D.
    Mol. Cell 21:295-305(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUC1.
  53. "ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases."
    Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.
    Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF366.
  54. "An inherent role of microtubule network in the action of nuclear receptor."
    Manavathi B., Acconcia F., Rayala S.K., Kumar R.
    Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PBXIP1.
  55. "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain."
    Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.
    Biochem. Biophys. Res. Commun. 361:127-132(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1S.
  56. "CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome."
    Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X., Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.
    EMBO J. 26:1831-1842(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUEDC2.
  57. "Estrogenically regulated LRP16 interacts with estrogen receptor alpha and enhances the receptor's transcriptional activity."
    Han W.-D., Zhao Y.-L., Meng Y.G., Zang L., Wu Z.-Q., Li Q., Si Y.-L., Huang K., Ba J.-M., Morinaga H., Nomura M., Mu Y.-M.
    Endocr. Relat. Cancer 14:741-753(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MACROD1.
  58. "MS-KIF18A, a kinesin, is associated with estrogen receptor."
    Luboshits G., Benayahu D.
    J. Cell. Biochem. 100:693-702(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF18A.
  59. "PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor."
    Meyer R., Wolf S.S., Obendorf M.
    J. Steroid Biochem. Mol. Biol. 107:1-14(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT2.
  60. "Ubiquitin-interaction motifs of RAP80 are critical in its regulation of estrogen receptor alpha."
    Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.
    Nucleic Acids Res. 35:1673-1686(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UIMC1.
  61. "ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification."
    Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.
    Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATAD2.
  62. "ERalpha and AP-1 interact in vivo with a specific sequence of the F promoter of the human ERalpha gene in osteoblasts."
    Lambertini E., Tavanti E., Torreggiani E., Penolazzi L., Gambari R., Piva R.
    J. Cell. Physiol. 216:101-110(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ASSOCIATION WITH AP-1.
  63. Cited for: METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULAR LOCATION, INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
  64. "CBP Is a dosage-dependent regulator of nuclear factor-kappaB suppression by the estrogen receptor."
    Nettles K.W., Gil G., Nowak J., Metivier R., Sharma V.B., Greene G.L.
    Mol. Endocrinol. 22:263-272(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NF-KAPPA-B TRANSREPRESSION, INTERACTION WITH RELA.
  65. "ERAP75 functions as a coactivator to enhance estrogen receptor alpha transactivation in prostate stromal cells."
    Chen M., Ni J., Zhang Y., Muyan M., Yeh S.
    Prostate 68:1273-1282(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC62.
  66. "SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC pathway."
    Li T., Li W., Lu J., Liu H., Li Y., Zhao Y.
    BMB Rep. 42:516-522(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D4A AND PLCG.
  67. "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer."
    Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L., Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G., Scheffner M., Pantel K., Gannon F., Bach I.
    Cancer Res. 69:128-136(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LDB1 AND RLIM.
  68. "Functional interaction of DYX1C1 with estrogen receptors suggests involvement of hormonal pathways in dyslexia."
    Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E., Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E., Kere J.
    Hum. Mol. Genet. 18:2802-2812(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYX1C1.
  69. "NF-kappaB and estrogen receptor alpha interactions: Differential function in estrogen receptor-negative and -positive hormone-independent breast cancer cells."
    Gionet N., Jansson D., Mader S., Pratt M.A.
    J. Cell. Biochem. 107:448-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MUTUAL TRANSREPRESSION WITH NF-KAPPA-B, INTERACTION WITH NFKB1 AND RELA.
  70. "OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity."
    Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.
    J. Biol. Chem. 284:16135-16145(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH OTUB1.
  71. "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 interactions."
    Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.
    Nucleic Acids Res. 37:3110-3123(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
  72. "The DEAD-box protein p72 regulates ERalpha-/oestrogen-dependent transcription and cell growth, and is associated with improved survival in ERalpha-positive breast cancer."
    Wortham N.C., Ahamed E., Nicol S.M., Thomas R.S., Periyasamy M., Jiang J., Ochocka A.M., Shousha S., Huson L., Bray S.E., Coombes R.C., Ali S., Fuller-Pace F.V.
    Oncogene 28:4053-4064(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX17.
  73. "The regulation of MS-KIF18A expression and cross talk with estrogen receptor."
    Zusev M., Benayahu D.
    PLoS ONE 4:E6407-E6407(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF18A.
  74. "Proinflammatory cytokines enhance estrogen-dependent expression of the multidrug transporter gene ABCG2 through estrogen receptor and NF{kappa}B cooperativity at adjacent response elements."
    Pradhan M., Bembinster L.A., Baumgarten S.C., Frasor J.
    J. Biol. Chem. 285:31100-31106(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
  75. "Mammalian MST2 kinase and human Salvador activate and reduce estrogen receptor alpha in the absence of ligand."
    Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.
    J. Mol. Med. 89:181-191(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAV1 AND STK3/MST2.
  76. "Splice isoform estrogen receptors as integral transmembrane proteins."
    Kim K.H., Toomre D., Bender J.R.
    Mol. Biol. Cell 22:4415-4423(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), TOPOLOGY (ISOFORM 3), MUTAGENESIS OF ILE-386.
  77. "Multiple sequence-specific DNA-binding proteins mediate estrogen receptor signaling through a tethering pathway."
    Heldring N., Isaacs G.D., Diehl A.G., Sun M., Cheung E., Ranish J.A., Kraus W.L.
    Mol. Endocrinol. 25:564-574(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ERE-INDEPENDENT SIGNALING.
  78. "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
    Pedram A., Razandi M., Deschenes R.J., Levin E.R.
    Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PALMITOYLATION.
  79. "CBP mediates NF-kappaB-dependent histone acetylation and estrogen receptor recruitment to an estrogen response element in the BIRC3 promoter."
    Pradhan M., Baumgarten S.C., Bembinster L.A., Frasor J.
    Mol. Cell. Biol. 32:569-575(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNERGISM WITH NF-KAPPA-B.
  80. "CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-alpha."
    Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y., Xiao L., Wu H.
    Oncogene 32:4883-4891(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CLOCK.
  81. "Solution structure of the DNA-binding domain of the oestrogen receptor."
    Schwabe J.W.E., Neuhaus D., Rhodes D.
    Nature 348:458-461(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 180-262.
  82. "The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements."
    Schwabe J.W.E., Chapman L., Finch J.T., Rhodes D.
    Cell 75:567-578(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262.
  83. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
  84. "Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains."
    Tanenbaum D.M., Wang Y., Williams S.P., Sigler P.B.
    Proc. Natl. Acad. Sci. U.S.A. 95:5998-6003(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-544.
  85. "The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen."
    Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L.
    Cell 95:927-937(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 294-554.
  86. "Homology model for the ligand-binding domain of the human estrogen receptor."
    Maalouf G.J., Xu W., Smith T., Mohr S.C.
    J. Biomol. Struct. Dyn. 15:841-850(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 311-547.
  87. "The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties."
    Tora L., Mullick A., Metzger D., Ponglikitmongkol M., Park I., Chambon P.
    EMBO J. 8:1981-1986(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-400.
  88. "A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action."
    McInerney E.M., Ince B.A., Shapiro D.J., Katzenellenbogen B.S.
    Mol. Endocrinol. 10:1519-1526(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ESTRR GLU-364.
  89. Cited for: VARIANT CYS-160.
  90. "Evidence of a linkage disequilibrium between polymorphisms in the human estrogen receptor alpha gene and their relationship to bone mass variation in postmenopausal Italian women."
    Becherini L., Gennari L., Masi L., Mansani R., Massart F., Morelli A., Falchetti A., Gonnelli S., Fiorelli G., Tanini A., Brandi M.L.
    Hum. Mol. Genet. 9:2043-2050(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN BMD.
  91. "G protein-coupled receptor 30 expression is up-regulated by EGF and TGF alpha in estrogen receptor alpha-positive cancer cells."
    Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., Fuqua S.A., Ando S., Maggiolini M.
    Mol. Endocrinol. 23:1815-1826(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPER1.
  92. "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
    Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.
    Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYR-6 AND ILE-264.
  93. "Delayed puberty and estrogen resistance in a woman with estrogen receptor alpha variant."
    Quaynor S.D., Stradtman E.W. Jr., Kim H.G., Shen Y., Chorich L.P., Schreihofer D.A., Layman L.C.
    N. Engl. J. Med. 369:164-171(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ESTRR HIS-375, CHARACTERIZATION OF VARIANT ESTRR HIS-375.

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: September 3, 2014
This is version 210 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

External Data

Dasty 3

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