P03372 (ESR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Protein existence	Evidence 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.51 Ref.62 Ref.64 Ref.69 Ref.74 Ref.76 Ref.77 Ref.79
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 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. 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.47 Ref.49 Ref.50 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.75
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.47 Ref.58 Ref.63 Ref.76 Ref.78 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.47 Ref.58 Ref.63 Ref.76 Ref.78 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.47 Ref.58 Ref.63 Ref.76 Ref.78
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. Ref.10 Ref.14 Ref.16 Ref.26 Ref.71 Glycosylated; contains N-acetylglucosamine, probably O-linked. Ref.23 Ubiquitinated. Deubiquitinated by OTUB1. Ref.70 Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization. Ref.63 Palmitoylated (isoform 3). Not biotinylated (isoform 3). Ref.22 Ref.78 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.78
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.
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 process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Domain	Transmembrane Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Activator Receptor
PTM	Glycoprotein Lipoprotein Methylation Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	androgen metabolic process Inferred from electronic annotation. Source: Compara antral ovarian follicle growth Inferred from electronic annotation. Source: Compara cellular response to estrogen stimulus Inferred from electronic annotation. Source: Compara epithelial cell development Inferred from electronic annotation. Source: Compara epithelial cell proliferation involved in mammary gland duct elongation Inferred from electronic annotation. Source: Compara male gonad development Inferred from electronic annotation. Source: Compara mammary gland alveolus development Inferred from electronic annotation. Source: Compara mammary gland branching involved in pregnancy Inferred from electronic annotation. Source: Compara negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.46Ref.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 positive regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from direct assay Ref.76. Source: UniProtKB positive regulation of nitric-oxide synthase activity Inferred from direct assay Ref.76. 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: Compara prostate epithelial cord elongation Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from electronic annotation. Source: Compara regulation of branching involved in prostate gland morphogenesis Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from direct assay PubMed 15304487. Source: BHF-UCL transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome uterus development Inferred from electronic annotation. Source: Compara vagina development Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 15569929. Source: UniProtKB
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara core promoter sequence-specific DNA binding Inferred from direct assay PubMed 15345745. 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 nitric-oxide synthase regulator activity Non-traceable author statement PubMed 12389206. Source: UniProtKB steroid binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		8	EBI-78473,EBI-78473
AKAP13	Q12802	3	EBI-78473,EBI-1373806
ASF1A	Q9Y294	2	EBI-78473,EBI-749553
ASXL1	Q8IXJ9	2	EBI-78473,EBI-1646500
Asxl1	P59598	2	EBI-78473,EBI-5743705	From a different organism.
BLCAP	P62952	2	EBI-78473,EBI-3895726
BRCA1	P38398	12	EBI-78473,EBI-349905
BTF3	P20290-2	5	EBI-78473,EBI-1054703
CITED1	Q99966	3	EBI-78473,EBI-2624951
CUEDC2	Q9H467	2	EBI-78473,EBI-1248228
DDX17	Q92841	7	EBI-78473,EBI-746012
DDX5	P17844	8	EBI-78473,EBI-351962
DNM1L	O00429	2	EBI-78473,EBI-724571
EGFR	P00533	4	EBI-4309277,EBI-297353
FOXO1	Q12778	2	EBI-78473,EBI-1108782
HAX1	O00165	2	EBI-78473,EBI-357001
Jun	P05627	6	EBI-78473,EBI-764369	From a different organism.
MACROD1	Q9BQ69	4	EBI-78473,EBI-5324932
MDM2	Q00987	2	EBI-78473,EBI-389668
MLL2	O14686	3	EBI-78473,EBI-996065
MYL6	P60660	3	EBI-78473,EBI-300817
NCOA1	Q15788	5	EBI-78473,EBI-455189
NCOA2	Q15596	8	EBI-78473,EBI-81236
NCOA3	Q9Y6Q9	2	EBI-78473,EBI-81196
Ncoa6	Q9JLI4	2	EBI-78473,EBI-286271	From a different organism.
NDRG2	Q9UN36	2	EBI-78473,EBI-3895741
NFKB1	P19838	3	EBI-78473,EBI-697771
PBXIP1	Q96AQ6	9	EBI-78473,EBI-740845
PHB2	Q99623	4	EBI-78473,EBI-358348
PPP5C	P53041	4	EBI-78473,EBI-716663
PRMT2	P55345	5	EBI-78473,EBI-78458
RAC3	P60763	5	EBI-78473,EBI-767084
RBFOX2	O43251	4	EBI-78473,EBI-746056
RELA	Q04206	7	EBI-78473,EBI-73886
SAFB2	Q14151	2	EBI-78473,EBI-352869
SENP5	Q96HI0	2	EBI-78473,EBI-3895753
SHC1	P29353	2	EBI-4309277,EBI-78835
SP1	P08047	2	EBI-78473,EBI-298336
SP3	Q02447	2	EBI-78473,EBI-348158
SRC	P12931	2	EBI-4309277,EBI-621482
ZNF366	Q8N895	6	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 595

595

Estrogen receptor

PRO_0000053618

Regions

DNA binding

185 – 250

66

Nuclear receptor

Zinc finger

185 – 205

21

NR C4-type

Zinc finger

221 – 245

25

NR C4-type

Region

1 – 184

184

Modulating (transactivation AF-1); mediates interaction with MACROD1

Region

35 – 174

140

Interaction with DDX5; self-association

Region

35 – 47

13

Required for interaction with NCOA1

Region

185 – 310

126

Mediates interaction with DNTTIP2

Region

251 – 310

60

Hinge

Region

262 – 595

334

Interaction with AKAP13

Region

264 – 595

332

Self-association

Region

311 – 595

285

Transactivation AF-2

Region

311 – 551

241

Steroid-binding

Amino acid modifications

Modified residue

104

1

Phosphoserine; by CDK2 Ref.26

Modified residue

106

1

Phosphoserine; by CDK2 Ref.26

Modified residue

118

1

Phosphoserine

Modified residue

167

1

Phosphoserine; by CK2

Modified residue

260

1

Asymmetric dimethylarginine; by PRMT1 Ref.63

Modified residue

537

1

Phosphotyrosine; by Tyr-kinases

Lipidation

447

1

S-palmitoyl cysteine By similarity

Glycosylation

10

1

O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence

1 – 173

173

Missing in isoform 3 and isoform 4.

VSP_042460

Alternative sequence

255 – 366

112

Missing in isoform 2.

VSP_003680

Alternative sequence

458 – 595

138

VYTFL…FPATV → FTISHVEAKKRILNLHPKIF GNKWFPRV in isoform 4.

VSP_042461

Natural variant

6

1

H → Y in a breast cancer sample; somatic mutation. Ref.90

VAR_033028

Natural variant

77

1

G → S. Ref.4
Corresponds to variant rs9340773 [ dbSNP | Ensembl ].

VAR_018905

Natural variant

160

1

G → C. Ref.88

VAR_004671

Natural variant

264

1

M → I in a breast cancer sample; somatic mutation. Ref.90

VAR_033029

Natural variant

364

1

V → E in estrogen resistance; dominant-negative inhibitor of the wild-type ESR. Ref.87

VAR_004672

Natural variant

400

1

G → V Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius. Ref.86

VAR_004673

Natural variant

411

1

D → 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

Mutagenesis

39

1

L → P: Impairs AF-1 transactivation. Ref.20

Mutagenesis

43

1

Y → P: Impairs AF-1 transactivation. Ref.20

Mutagenesis

104

1

S → A: Loss of cyclin A-dependent induction of transcriptional activation.

Mutagenesis

106

1

S → A: Loss of cyclin A-dependent induction of transcriptional activation.

Mutagenesis

118

1

S → A: Decrease in phosphorylation, abolishes AF-1 transactivation. Ref.18

Mutagenesis

118

1

S → E: Enhances interaction with DDX5. Ref.18

Mutagenesis

260

1

R → A or K: Loss of methylation. Ref.63

Mutagenesis

386

1

I → 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.76

Mutagenesis

447

1

C → A: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding. Ref.15

Mutagenesis

539

1

L → A: Abolishes interaction with NCOA1, NCOA2 and NCOA3. Ref.21

Sequence conflict

452

1

I → L in CAE45969. Ref.5

Secondary structure

1

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595

Helix Strand Turn

Details...

Turn

186 – 188

3

Beta strand

189 – 191

3

Beta strand

194 – 196

3

Beta strand

199 – 201

3

Helix

203 – 213

11

Beta strand

222 – 225

4

Turn

231 – 236

6

Helix

238 – 248

11

Helix

288 – 291

4

Helix

293 – 304

12

Helix

306 – 309

4

Helix

312 – 321

10

Beta strand

330 – 332

3

Beta strand

333 – 335

3

Helix

337 – 339

3

Helix

342 – 363

22

Helix

367 – 369

3

Helix

372 – 395

24

Beta strand

396 – 398

3

Beta strand

401 – 405

5

Beta strand

408 – 411

4

Helix

412 – 415

4

Beta strand

417 – 420

4

Helix

421 – 438

18

Helix

442 – 455

14

Turn

456 – 459

4

Helix

466 – 492

27

Helix

497 – 525

29

Beta strand

528 – 530

3

Beta strand

531 – 533

3

Helix

536 – 544

9

Turn

546 – 548

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) (hER-alpha66) (ER66) [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 5455C57AB0CCCAA7	FASTA	595	66,216
	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
	Isoform 2 (Short) [UniParc]. Checksum: 449BC03EF22E80A5	FASTA	483	53,687
	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 MKGGFVDLTL HDQVHLLECA WLEILMIGLV WRSMEHPGKL LFAPNLLLDR 310 320 330 340 350 360 NQGKCVEGMV EIFDMLLATS SRFRMMNLQG EEFVCLKSII LLNSGVYTFL SSTLKSLEEK 370 380 390 400 410 420 DHIHRVLDKI TDTLIHLMAK AGLTLQQQHQ RLAQLLLILS HIRHMSNKGM EHLYSMKCKN 430 440 450 460 470 480 VVPLYDLLLE MLDAHRLHAP TSRGGASVEE TDQSHLATAG STSSHSLQKY YITGEAEGFP ATV
	Isoform 3 (hER-alpha46) (ER46) [UniParc]. Checksum: C51DF9A9644127C0	FASTA	422	47,629
	10 20 30 40 50 60 MAMESAKETR YCAVCNDYAS GYHYGVWSCE GCKAFFKRSI QGHNDYMCPA TNQCTIDKNR 70 80 90 100 110 120 RKSCQACRLR KCYEVGMMKG GIRKDRRGGR MLKHKRQRDD GEGRGEVGSA GDMRAANLWP 130 140 150 160 170 180 SPLMIKRSKK NSLALSLTAD QMVSALLDAE PPILYSEYDP TRPFSEASMM GLLTNLADRE 190 200 210 220 230 240 LVHMINWAKR VPGFVDLTLH DQVHLLECAW LEILMIGLVW RSMEHPGKLL FAPNLLLDRN 250 260 270 280 290 300 QGKCVEGMVE IFDMLLATSS RFRMMNLQGE EFVCLKSIIL LNSGVYTFLS STLKSLEEKD 310 320 330 340 350 360 HIHRVLDKIT DTLIHLMAKA GLTLQQQHQR LAQLLLILSH IRHMSNKGME HLYSMKCKNV 370 380 390 400 410 420 VPLYDLLLEM LDAHRLHAPT SRGGASVEET DQSHLATAGS TSSHSLQKYY ITGEAEGFPA TV
	Isoform 4 (hER-alpha36) (ER36) [UniParc]. Checksum: 85C8DEAD873F9AEC	FASTA	312	35,547
	10 20 30 40 50 60 MAMESAKETR YCAVCNDYAS GYHYGVWSCE GCKAFFKRSI QGHNDYMCPA TNQCTIDKNR 70 80 90 100 110 120 RKSCQACRLR KCYEVGMMKG GIRKDRRGGR MLKHKRQRDD GEGRGEVGSA GDMRAANLWP 130 140 150 160 170 180 SPLMIKRSKK NSLALSLTAD QMVSALLDAE PPILYSEYDP TRPFSEASMM GLLTNLADRE 190 200 210 220 230 240 LVHMINWAKR VPGFVDLTLH DQVHLLECAW LEILMIGLVW RSMEHPGKLL FAPNLLLDRN 250 260 270 280 290 300 QGKCVEGMVE IFDMLLATSS RFRMMNLQGE EFVCLKSIIL LNSGFTISHV EAKKRILNLH 310 PKIFGNKWFP RV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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.
[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]	"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.
[47]	"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.
[48]	Erratum Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R., Kumar R. EMBO Rep. 6:1101-1101(2005)
[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 MLL2.
[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]	"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.
[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]	"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.
[81]	"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.
[82]	"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.
[83]	"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.
[84]	"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.
[85]	"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.
[86]	"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.
[87]	"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 ESTROGEN RESISTANCE GLU-364.
[88]	"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.
[89]	"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.
[90]	"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.
+	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 , 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.

IPI

IPI00218352.
IPI00294982.
IPI00914643.
IPI01018719.

PIR

S64737.

RefSeq

NP_000116.2. NM_000125.3.
NP_001116212.1. NM_001122740.1.
NP_001116213.1. NM_001122741.1.
NP_001116214.1. NM_001122742.1.

UniGene

Hs.208124.

3D structure databases

PDBe
RCSB PDB
PDBj

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	304-533	[»]
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	[»]

DisProt

DP00074.

ProteinModelPortal

P03372.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5965N.

IntAct

P03372. 353 interactions.

MINT

MINT-129047.

STRING

9606.ENSP00000206249.

PTM databases

GlycoSuiteDB

P03372.

PhosphoSite

P03372.

Polymorphism databases

DMDM

544257.

Proteomic databases

PaxDb

P03372.

PRIDE

P03372.

Protocols and materials databases

DNASU

2099.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000206249; ENSP00000206249; ENSG00000091831.
ENST00000338799; ENSP00000342630; ENSG00000091831.
ENST00000440973; ENSP00000405330; ENSG00000091831.
ENST00000443427; ENSP00000387500; ENSG00000091831.
ENST00000456483; ENSP00000415934; ENSG00000091831.

GeneID

2099.

KEGG

hsa:2099.

UCSC

uc003qom.4. human.

Organism-specific databases

CTD

2099.

GeneCards

GC06P151980.

HGNC

HGNC:3467. ESR1.

HPA

CAB000037.
HPA000449.
HPA000450.

MIM

133430. gene.

neXtProt

NX_P03372.

Orphanet

785. Estrogen resistance syndrome.

PharmGKB

PA156.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG320746.

HOVERGEN

HBG108344.

InParanoid

P03372.

KO

K08550.

OrthoDB

EOG4JM7PP.

PhylomeDB

P03372.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.
foxm1pathway. FOXM1 transcription factor network.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P03372.

Bgee

P03372.

CleanEx

HS_ESR1.

Genevestigator

P03372.

GermOnline

ENSG00000091831. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

InterPro

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]

Pfam

PF12743. ESR1_C. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF02159. Oest_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PIRSF

PIRSF500101. ER-a. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.

PRINTS

PR00543. OESTROGENR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P03372.

ChEMBL

CHEMBL206.

ChiTaRS

ESR1. human.

DrugBank

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.

EvolutionaryTrace

P03372.

GenomeRNAi

2099.

NextBio

8491.

SOURCE

Search...

Entry information

Entry name

ESR1_HUMAN

Accession

Primary (citable) accession number: P03372
Secondary accession number(s): Q13511 , Q14276, Q5T5H7, Q6MZQ9, Q9NU51, Q9UDZ7, Q9UIS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 195 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.