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P03372 (ESR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 209. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen receptor

Short name=ER
Alternative name(s):
ER-alpha
Estradiol receptor
Nuclear receptor subfamily 3 group A member 1
Gene names
Name:ESR1
Synonyms:ESR, NR3A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.17 Ref.19 Ref.24 Ref.30 Ref.31 Ref.33 Ref.36 Ref.44 Ref.46 Ref.47 Ref.48 Ref.52 Ref.63 Ref.65 Ref.70 Ref.75 Ref.77 Ref.78 Ref.80

Subunit structure

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. Ref.18 Ref.19 Ref.21 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.45 Ref.48 Ref.50 Ref.51 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.76 Ref.81 Ref.92

Subcellular location

Isoform 1: Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: A minor fraction is associated with the inner membrane. Ref.6 Ref.22 Ref.48 Ref.59 Ref.64 Ref.77 Ref.79 Ref.81

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 Probable. At least a subset exists as a transmembrane protein with a N-terminal extracellular domain. Ref.6 Ref.22 Ref.48 Ref.59 Ref.64 Ref.77 Ref.79 Ref.81

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. Ref.6 Ref.22 Ref.48 Ref.59 Ref.64 Ref.77 Ref.79 Ref.81

Tissue specificity

Widely expressed. Isoform 3 is not expressed in the pituitary gland. Ref.19

Domain

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.

Post-translational modification

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. Ref.10 Ref.14 Ref.16 Ref.26 Ref.46 Ref.72

Glycosylated; contains N-acetylglucosamine, probably O-linked. Ref.23

Ubiquitinated. Deubiquitinated by OTUB1. Ref.71

Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization. Ref.64

Palmitoylated (isoform 3) Not biotinylated (isoform 3) Ref.22 Ref.79

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. Ref.22 Ref.79

Polymorphism

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.

Involvement in disease

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. Ref.89 Ref.94

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.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransmembrane
Zinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionActivator
Receptor
   PTMGlycoprotein
Lipoprotein
Methylation
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen metabolic process

Inferred from electronic annotation. Source: Ensembl

antral ovarian follicle growth

Inferred from electronic annotation. Source: Ensembl

cellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin remodeling

Non-traceable author statement PubMed 12351687. Source: UniProtKB

epithelial cell development

Inferred from electronic annotation. Source: Ensembl

epithelial cell proliferation involved in mammary gland duct elongation

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

intracellular estrogen receptor signaling pathway

Non-traceable author statement Ref.2. Source: UniProtKB

intracellular steroid hormone receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

male gonad development

Inferred from electronic annotation. Source: Ensembl

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.47Ref.17. Source: UniProtKB

negative regulation of gene expression

Inferred from direct assay PubMed 21695196. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.31. Source: UniProtKB

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay Ref.77. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from direct assay Ref.77. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of retinoic acid receptor signaling pathway

Inferred from direct assay PubMed 15831516. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.30Ref.24. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15345745. Source: UniProtKB

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from electronic annotation. Source: Ensembl

prostate epithelial cord elongation

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in prostate gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

response to estradiol

Inferred from direct assay PubMed 15304487. Source: BHF-UCL

response to estrogen

Inferred from direct assay Ref.32. Source: UniProtKB

signal transduction

Traceable author statement PubMed 10749889Ref.19. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement PubMed 2040605. Source: ProtInc

uterus development

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Non-traceable author statement PubMed 11960618. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15569929PubMed 20080953. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 15569929. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 15304487. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 15345745. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.37. Source: UniProtKB

estrogen receptor activity

Non-traceable author statement Ref.2. Source: UniProtKB

estrogen response element binding

Inferred from direct assay PubMed 15345745PubMed 17975005. Source: UniProtKB

estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from genetic interaction PubMed 18722177. Source: MGI

identical protein binding

Inferred from physical interaction Ref.29Ref.36PubMed 21182205PubMed 23065768. Source: IntAct

nitric-oxide synthase regulator activity

Non-traceable author statement PubMed 12389206. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20935677. Source: IntAct

sequence-specific DNA binding transcription factor activity

Non-traceable author statement PubMed 12552091. Source: BHF-UCL

steroid binding

Inferred from sequence or structural similarity. Source: UniProtKB

steroid hormone receptor activity

Traceable author statement PubMed 10749889. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P03372-1)

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.
Isoform 2 (identifier: P03372-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     255-366: Missing.
Isoform 3 (identifier: P03372-3)

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.
Isoform 4 (identifier: P03372-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595Estrogen receptor
PRO_0000053618

Regions

DNA binding185 – 25066Nuclear receptor
Zinc finger185 – 20521NR C4-type
Zinc finger221 – 24525NR C4-type
Region1 – 184184Modulating (transactivation AF-1); mediates interaction with MACROD1
Region35 – 174140Interaction with DDX5; self-association
Region35 – 4713Required for interaction with NCOA1
Region185 – 310126Mediates interaction with DNTTIP2
Region251 – 31060Hinge
Region262 – 595334Interaction with AKAP13
Region264 – 595332Self-association
Region311 – 595285Transactivation AF-2
Region311 – 551241Steroid-binding

Amino acid modifications

Modified residue1041Phosphoserine; by CDK2 Ref.26
Modified residue1061Phosphoserine; by CDK2 Ref.26
Modified residue1181Phosphoserine Ref.46
Modified residue1671Phosphoserine; by CK2 Ref.16
Modified residue2601Asymmetric dimethylarginine; by PRMT1 Ref.64
Modified residue5371Phosphotyrosine; by Tyr-kinases Ref.14
Lipidation4471S-palmitoyl cysteine By similarity
Glycosylation101O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence1 – 173173Missing in isoform 3 and isoform 4.
VSP_042460
Alternative sequence255 – 366112Missing in isoform 2.
VSP_003680
Alternative sequence458 – 595138VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4.
VSP_042461
Natural variant61H → Y in a breast cancer sample; somatic mutation. Ref.93
Corresponds to variant rs139960913 [ dbSNP | Ensembl ].
VAR_033028
Natural variant771G → S. Ref.4
Corresponds to variant rs9340773 [ dbSNP | Ensembl ].
VAR_018905
Natural variant1601G → C. Ref.90
Corresponds to variant rs149308960 [ dbSNP | Ensembl ].
VAR_004671
Natural variant2641M → I in a breast cancer sample; somatic mutation. Ref.93
VAR_033029
Natural variant3641V → E in ESTRR; dominant-negative inhibitor of the wild-type ESR. Ref.89
VAR_004672
Natural variant3751Q → H in ESTRR; results in highly reduced activity. Ref.94
VAR_070072
Natural variant4001G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. Ref.88
VAR_004673
Natural variant4111D → 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

Experimental info

Mutagenesis391L → P: Impairs AF-1 transactivation. Ref.20
Mutagenesis431Y → P: Impairs AF-1 transactivation. Ref.20
Mutagenesis1041S → A: Loss of cyclin A-dependent induction of transcriptional activation.
Mutagenesis1061S → A: Loss of cyclin A-dependent induction of transcriptional activation.
Mutagenesis1181S → A: Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity. Ref.18 Ref.46
Mutagenesis1181S → E: Enhances transactivation activity. Enhances interaction with DDX5. Insensitive to PPP5C inhibition of transactivation activity. Ref.18 Ref.46
Mutagenesis2601R → A or K: Loss of methylation. Ref.64
Mutagenesis3861I → 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. Ref.77
Mutagenesis4471C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. Ref.15
Mutagenesis5391L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. Ref.21
Sequence conflict4521I → L in CAE45969. Ref.5

Secondary structure

.......................................................... 595
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (hER-alpha66) (ER66) [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 5455C57AB0CCCAA7

FASTA59566,216
        10         20         30         40         50         60 
MTMTLHTKAS GMALLHQIQG NELEPLNRPQ LKIPLERPLG EVYLDSSKPA VYNYPEGAAY 

        70         80         90        100        110        120 
EFNAAAAANA QVYGQTGLPY GPGSEAAAFG SNGLGGFPPL NSVSPSPLML LHPPPQLSPF 

       130        140        150        160        170        180 
LQPHGQQVPY YLENEPSGYT VREAGPPAFY RPNSDNRRQG GRERLASTND KGSMAMESAK 

       190        200        210        220        230        240 
ETRYCAVCND YASGYHYGVW SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC 

       250        260        270        280        290        300 
RLRKCYEVGM MKGGIRKDRR GGRMLKHKRQ RDDGEGRGEV GSAGDMRAAN LWPSPLMIKR 

       310        320        330        340        350        360 
SKKNSLALSL TADQMVSALL DAEPPILYSE YDPTRPFSEA SMMGLLTNLA DRELVHMINW 

       370        380        390        400        410        420 
AKRVPGFVDL TLHDQVHLLE CAWLEILMIG LVWRSMEHPG KLLFAPNLLL DRNQGKCVEG 

       430        440        450        460        470        480 
MVEIFDMLLA TSSRFRMMNL QGEEFVCLKS IILLNSGVYT FLSSTLKSLE EKDHIHRVLD 

       490        500        510        520        530        540 
KITDTLIHLM AKAGLTLQQQ HQRLAQLLLI LSHIRHMSNK GMEHLYSMKC KNVVPLYDLL 

       550        560        570        580        590 
LEMLDAHRLH APTSRGGASV EETDQSHLAT AGSTSSHSLQ KYYITGEAEG FPATV 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 449BC03EF22E80A5
Show »

FASTA48353,687
Isoform 3 (hER-alpha46) (ER46) [UniParc].

Checksum: C51DF9A9644127C0
Show »

FASTA42247,629
Isoform 4 (hER-alpha36) (ER36) [UniParc].

Checksum: 85C8DEAD873F9AEC
Show »

FASTA31235,547

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A negative coregulator for the human ER."
Norris J.D., Fan D., Sherk A., McDonnell D.P.
Mol. Endocrinol. 16:459-468(2002) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R., Kumar R.
EMBO Rep. 6:1101-1101(2005)
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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.
[62]"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.
[63]"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.
[64]"Regulation of estrogen rapid signaling through arginine methylation by PRMT1."
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.
Mol. Cell 31:212-221(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-260 BY PRMT1, MUTAGENESIS OF ARG-260, SUBCELLULAR LOCATION, INTERACTION WITH PI3KR1/2; SRC AND PTK2/FAK1.
[65]"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.
[66]"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.
[67]"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.
[68]"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.
[69]"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.
[70]"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.
[71]"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.
[72]"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.
[73]"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.
[74]"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.
[75]"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.
[76]"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.
[77]"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.
[78]"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.
[79]"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.
[80]"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.
[81]"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.
[82]"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.
[83]"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.
[84]"Molecular basis of agonism and antagonism in the oestrogen receptor."
Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T., Engstroem O., Oehman L., Greene G.L., Gustafsson J.-A., Carlquist M.
Nature 389:753-758(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 305-548.
[85]"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.
[86]"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.
[87]"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.
[88]"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.
[89]"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.
[90]"Screening for ESR mutations in breast and ovarian cancer patients."
Anderson T.I., Wooster R., Laake K., Collins N., Warren W., Skrede M., Eeles R., Tveit K.M., Johnston S.R.D., Dowsett M., Olsen A.O., Moeller P., Stratton M.R., Boerresen-Dale A.-L.
Hum. Mutat. 9:531-536(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-160.
[91]"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.
[92]"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.
[93]"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.
[94]"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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Estrogen receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AL049821, AL078582, AL590993 Genomic DNA. Translation: CAI21012.1.
AL049821 expand/collapse EMBL AC list , AL078582, AL356311, AL590993 Genomic DNA. Translation: CAI22123.1.
AL590993 expand/collapse EMBL AC list , 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.
CCDSCCDS5234.1. [P03372-1]
PIRS64737.
RefSeqNP_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]
UniGeneHs.208124.
Hs.744830.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00074.
ProteinModelPortalP03372.
SMRP03372. Positions 180-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108403. 528 interactions.
DIPDIP-5965N.
IntActP03372. 376 interactions.
MINTMINT-129047.
STRING9606.ENSP00000206249.

Chemistry

BindingDBP03372.
ChEMBLCHEMBL2093866.
DrugBankDB00269. 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.
GuidetoPHARMACOLOGY620.

PTM databases

PhosphoSiteP03372.
UniCarbKBP03372.

Polymorphism databases

DMDM544257.

Proteomic databases

PaxDbP03372.
PRIDEP03372.

Protocols and materials databases

DNASU2099.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000206249; ENSP00000206249; ENSG00000091831. [P03372-1]
ENST00000338799; ENSP00000342630; ENSG00000091831. [P03372-1]
ENST00000440973; ENSP00000405330; ENSG00000091831. [P03372-1]
ENST00000443427; ENSP00000387500; ENSG00000091831. [P03372-1]
ENST00000456483; ENSP00000415934; ENSG00000091831. [P03372-2]
GeneID2099.
KEGGhsa:2099.
UCSCuc003qom.4. human. [P03372-1]

Organism-specific databases

CTD2099.
GeneCardsGC06P151985.
HGNCHGNC:3467. ESR1.
HPACAB000037.
CAB055099.
HPA000449.
HPA000450.
MIM133430. gene.
615363. phenotype.
neXtProtNX_P03372.
Orphanet785. Estrogen resistance syndrome.
PharmGKBPA156.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320746.
HOVERGENHBG108344.
InParanoidP03372.
KOK08550.
OrthoDBEOG7288S1.
PhylomeDBP03372.
TreeFamTF323751.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_71. Gene Expression.
SignaLinkP03372.

Gene expression databases

ArrayExpressP03372.
BgeeP03372.
CleanExHS_ESR1.
GenevestigatorP03372.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSPR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSESR1. human.
EvolutionaryTraceP03372.
GeneWikiEstrogen_receptor_alpha.
GenomeRNAi2099.
NextBio8491.
PROP03372.
SOURCESearch...

Entry information

Entry nameESR1_HUMAN
AccessionPrimary (citable) accession number: P03372
Secondary accession number(s): Q13511 expand/collapse secondary AC list , Q14276, Q5T5H7, Q6MZQ9, Q9NU51, Q9UDZ7, Q9UIS7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 209 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM