Q92731 (ESR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Estrogen receptor beta
Short name=ER-beta

Alternative name(s):
Nuclear receptor subfamily 3 group A member 2

Gene names

Name:	ESR2
Synonyms:	ESTRB, NR3A2

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	530 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.
Subunit structure	Binds DNA as a homodimer. Can form a heterodimer with ESR1. Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with PELP1 and UBE1C. Isoform beta-2/cx preferentially forms a heterodimer with ESR1 rather than ESR2 and inhibits DNA-binding by ESR1. Interacts with AKAP13. Interacts with DNTTIP2. Interacts with isoform 4 of TXNRD1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes, including cyclin-D1/CCND1 AP-1 promoter. Interacts with DYX1C1 By similarity. Interacts with PRMT2. Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25
Subcellular location	Nucleus Ref.25.
Tissue specificity	Isoform beta-1 is expressed in testis and ovary, and at a lower level in heart, brain, placenta, liver, skeletal muscle, spleen, thymus, prostate, colon, bone marrow, mammary gland and uterus. Also found in uterine bone, breast, and ovarian tumor cell lines, but not in colon and liver tumors. Isoform beta-2 is expressed in spleen, thymus, testis and ovary and at a lower level in skeletal muscle, prostate, colon, small intestine, leukocytes, bone marrow, mammary gland and uterus. Isoform beta-3 is found in testis. Isoform beta-4 is expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. Isoform beta-5 is expressed in testis, placenta, skeletal muscle, spleen and leukocytes, and at a lower level in heart, lung, liver, kidney, pancreas, thymus, prostate, colon, small intestine, bone marrow, mammary gland and uterus. Not expressed in brain.
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Post-translational modification	Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR3 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Sequence caution	The sequence CAA67555.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Receptor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from electronic annotation. Source: Compara cell-cell signaling Traceable author statement Ref.12. Source: ProtInc epithelial cell maturation involved in prostate gland development Inferred from electronic annotation. Source: Compara intracellular estrogen receptor signaling pathway Traceable author statement PubMed 11181953. Source: UniProtKB negative regulation of androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of cell growth Non-traceable author statement PubMed 11181953. Source: UniProtKB negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15345745. Source: UniProtKB neuron migration Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10681512. Source: UniProtKB prostate gland epithelium morphogenesis Inferred from electronic annotation. Source: Compara 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	extracellular region Non-traceable author statement Ref.4. Source: GOC mitochondrion Inferred from direct assay PubMed 15024130. Source: MGI nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	core promoter sequence-specific DNA binding Inferred from direct assay PubMed 15345745. Source: UniProtKB estrogen receptor activity Traceable author statement PubMed 11181953. Source: UniProtKB estrogen response element binding Inferred from direct assay PubMed 15345745. Source: UniProtKB ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Non-traceable author statement Ref.4. Source: UniProtKB receptor antagonist activity Non-traceable author statement Ref.4. Source: UniProtKB steroid binding Traceable author statement PubMed 11181953. Source: UniProtKB transcription coactivator activity Traceable author statement Ref.12. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP5C	P53041	4	EBI-78505,EBI-716663

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92731-1)

Also known as: Beta-1;

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: Q92731-2)

Also known as: Beta-2; CX;

The sequence of this isoform differs from the canonical sequence as follows:
     469-530: SNKGMEHLLN...KEGSQNPQSQ → RAEKASQTLTSFGMKMETLLPEATMEQ

Isoform 3 (identifier: Q92731-3)

Also known as: Beta-2A;

The sequence of this isoform differs from the canonical sequence as follows:
     319-323: FVELS → MRGNA
     324-530: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: Q92731-4)

Also known as: Beta-3;

The sequence of this isoform differs from the canonical sequence as follows:
     469-530: SNKGMEHLLN...KEGSQNPQSQ → SSLSLSWRLF...SFEACQQPRE

Isoform 5 (identifier: Q92731-5)

Also known as: Beta-4;

The sequence of this isoform differs from the canonical sequence as follows:
     469-530: SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ → RWGEKQFIHLKLS

Note: Does not form homodimers.

Isoform 6 (identifier: Q92731-6)

Also known as: Beta-5;

The sequence of this isoform differs from the canonical sequence as follows:
     469-530: SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ → RYAP

Note: Does not form homodimers.

Isoform 7 (identifier: Q92731-7)

Also known as: Beta-5A;

The sequence of this isoform differs from the canonical sequence as follows:
     319-409: Missing.

Isoform 8 (identifier: Q92731-8)

Also known as: Beta-6;

The sequence of this isoform differs from the canonical sequence as follows:
     365-375: DEGKCVEGILE → YVPSGHSDPGC
     376-530: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 530

530

Estrogen receptor beta

PRO_0000053642

Regions

DNA binding

149 – 214

66

Nuclear receptor

Zinc finger

149 – 169

21

NR C4-type

Zinc finger

185 – 209

25

NR C4-type

Region

1 – 148

148

Modulating

Region

215 – 530

316

Steroid-binding

Amino acid modifications

Modified residue

87

1

Phosphoserine Ref.24

Modified residue

105

1

Phosphoserine Ref.24

Natural variations

Alternative sequence

319 – 409

91

Missing in isoform 7.

VSP_003685

Alternative sequence

319 – 323

5

FVELS → MRGNA in isoform 3.

VSP_003684

Alternative sequence

324 – 530

207

Missing in isoform 3.

VSP_003686

Alternative sequence

365 – 375

11

DEGKCVEGILE → YVPSGHSDPGC in isoform 8.

VSP_003687

Alternative sequence

376 – 530

155

Missing in isoform 8.

VSP_003688

Alternative sequence

469 – 530

62

SNKGM…NPQSQ → RAEKASQTLTSFGMKMETLL PEATMEQ in isoform 2.

VSP_003689

Alternative sequence

469 – 530

62

SNKGM…NPQSQ → SSLSLSWRLFMLREASCHGV RQTPGGAHMSVSRSRSFEAC QQPRE in isoform 4.

VSP_003690

Alternative sequence

469 – 530

62

SNKGM…NPQSQ → RWGEKQFIHLKLS in isoform 5.

VSP_003691

Alternative sequence

469 – 530

62

SNKGM…NPQSQ → RYAP in isoform 6.

VSP_003692

Experimental info

Mutagenesis

87

1

S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-105. Ref.24

Mutagenesis

87

1

S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-105. Ref.24

Mutagenesis

105

1

S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-87. Ref.24

Mutagenesis

105

1

S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-87. Ref.24

Secondary structure

1

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530

Helix Strand Turn

Details...

Helix

261 – 263

3

Helix

265 – 275

11

Beta strand

286 – 288

3

Helix

291 – 314

24

Helix

319 – 321

3

Helix

324 – 347

24

Beta strand

348 – 350

3

Beta strand

353 – 357

5

Beta strand

359 – 363

5

Helix

364 – 369

6

Helix

373 – 389

17

Helix

394 – 406

13

Beta strand

407 – 409

3

Helix

411 – 413

3

Helix

417 – 419

3

Helix

421 – 442

22

Turn

443 – 445

3

Helix

448 – 481

34

Beta strand

482 – 484

3

Helix

489 – 497

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Beta-1) [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 8CAE34215992418A	FASTA	530	59,216
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 380 390 400 410 420 VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA 430 440 450 460 470 480 DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHASN KGMEHLLNMK 490 500 510 520 530 CKNVVPVYDL LLEMLNAHVL RGCKSSITGS ECSPAEDSKS KEGSQNPQSQ
	Isoform 2 (Beta-2) (CX) [UniParc]. Checksum: F068DBC63DC838A6	FASTA	495	55,483
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 380 390 400 410 420 VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA 430 440 450 460 470 480 DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHARA EKASQTLTSF 490 GMKMETLLPE ATMEQ
	Isoform 3 (Beta-2A) [UniParc]. Checksum: 158D376C56D3CA12	FASTA	323	35,944
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 LADKELVHMI SWAKKIPGMR GNA
	Isoform 4 (Beta-3) [UniParc]. Checksum: EE88C42CBB24775E	FASTA	513	57,518
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 380 390 400 410 420 VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA 430 440 450 460 470 480 DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHASS LSLSWRLFML 490 500 510 REASCHGVRQ TPGGAHMSVS RSRSFEACQQ PRE
	Isoform 5 (Beta-4) [UniParc]. Checksum: 9B6017FE950720F0	FASTA	481	54,096
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 380 390 400 410 420 VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA 430 440 450 460 470 480 DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHARW GEKQFIHLKL S
	Isoform 6 (Beta-5) [UniParc]. Checksum: 673B0DB5FAF03C26	FASTA	472	52,959
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 380 390 400 410 420 VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA 430 440 450 460 470 DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHARY AP
	Isoform 7 (Beta-5A) [UniParc]. Checksum: 35B686E3C0D32D0F	FASTA	439	48,614
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGMY PLVTATQDAD SSRKLAHLLN AVTDALVWVI AKSGISSQQQ 370 380 390 400 410 420 SMRLANLLML LSHVRHASNK GMEHLLNMKC KNVVPVYDLL LEMLNAHVLR GCKSSITGSE 430 CSPAEDSKSK EGSQNPQSQ
	Isoform 8 (Beta-6) [UniParc]. Checksum: E2FA83EE3C519EE5	FASTA	375	41,948
	10 20 30 40 50 60 MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS 70 80 90 100 110 120 NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN 130 140 150 160 170 180 RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 190 200 210 220 230 240 NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH 250 260 270 280 290 300 CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 310 320 330 340 350 360 LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL 370 VLDRYVPSGH SDPGC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete primary structure of human estrogen receptor beta (hERbeta) and its heterodimerization with ER alpha in vivo and in vitro." Ogawa S., Inoue S., Watanabe T., Hiroi H., Orimo A., Hosoi T., Ouchi Y., Muramatsu M. Biochem. Biophys. Res. Commun. 243:122-126(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and characterization of human estrogen receptor beta isoforms." Moore J.T., McKee D.D., Slentz-Kesler K., Moore L.B., Jones S.A., Horne E.L., Su J.-L., Kliewer S.A., Lehmann J.M., Willson T.M. Biochem. Biophys. Res. Commun. 247:75-78(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 409-482 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 409-472 (ISOFORM 6). Tissue: Mammary gland and Testis.
[3]	"Estrogen receptor-beta mRNA variants in human and murine tissues." Lu B., Leygue E., Dotzlaw H., Murphy L.J., Murphy L.C., Watson P.H. Mol. Cell. Endocrinol. 138:199-203(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Ovary.
[4]	"Molecular cloning and characterization of human estrogen receptor beta cx: a potential inhibitor of estrogen action in human." Ogawa S., Inoue S., Watanabe T., Orimo A., Hosoi T., Ouchi Y., Muramatsu M. Nucleic Acids Res. 26:3505-3512(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION. Tissue: Testis.
[5]	"Estrogen receptor (ER)-beta isoforms: a key to understanding ER-beta signaling." Leung Y.K., Mak P., Hassan S., Ho S.M. Proc. Natl. Acad. Sci. U.S.A. 103:13162-13167(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). Tissue: Prostate.
[6]	SeattleSNPs variation discovery resource Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[8]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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 3). Tissue: Testis.
[11]	"Cloning and characterization of human estrogen receptor beta promoter." Li L.C., Yeh C.C., Nojima D., Dahiya R. Biochem. Biophys. Res. Commun. 275:682-689(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
[12]	"ER beta: identification and characterization of a novel human estrogen receptor." Mosselman S., Polman J., Dijkema R. FEBS Lett. 392:49-53(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-530 (ISOFORM 1), CHARACTERIZATION. Tissue: Testis.
[13]	Brandenberger A.W., Lebovic D., Taylor R.N., Jaffe R.B. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-530 (ISOFORMS 7 AND 8). Tissue: Endometrium.
[14]	"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300." Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M. Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA3.
[15]	"Human estrogen receptor beta binds DNA in a manner similar to and dimerizes with estrogen receptor alpha." Pace P., Taylor J., Suntharalingam S., Coombes R.C., Ali S. J. Biol. Chem. 272:25832-25838(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[16]	"Cloning and characterization of RAP250, a nuclear receptor coactivator." Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A. J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA6.
[17]	"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.
[18]	"The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway." Driggers P.H., Segars J.H., Rubino D.M. J. Biol. Chem. 276:46792-46797(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKAP13.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[23]	"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.
[24]	"Selective hormone-dependent repression of estrogen receptor beta by a p38-activated ErbB2/ErbB3 pathway." St-Laurent V., Sanchez M., Charbonneau C., Tremblay A. J. Steroid Biochem. Mol. Biol. 94:23-37(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-87 AND SER-105, MUTAGENESIS OF SER-87 AND SER-105.
[25]	"CCDC62/ERAP75 functions as a coactivator to enhance estrogen receptor beta-mediated transactivation and target gene expression in prostate cancer cells." Chen M., Ni J., Chang H.C., Lin C.Y., Muyan M., Yeh S. Carcinogenesis 30:841-850(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCDC62, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Estrogen receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB006590 mRNA. Translation: BAA24953.1.
AF051427 mRNA. Translation: AAC05985.1.
AF051428 mRNA. Translation: AAC05751.1.
AF061054 mRNA. Translation: AAC39784.1.
AF061055 mRNA. Translation: AAC39785.1.
AF060555 mRNA. Translation: AAC15234.1.
AF124790 mRNA. Translation: AAD32580.1.
AF047463 mRNA. Translation: AAC03786.1.
AB006589 mRNA. Translation: BAA31966.1.
DQ838582 mRNA. Translation: ABH09189.1.
DQ838583 mRNA. Translation: ABH09190.1.
AY785359 Genomic DNA. Translation: AAV31779.1.
AK292370 mRNA. Translation: BAF85059.1.
CH471061 Genomic DNA. Translation: EAW80850.1.
BC024181 mRNA. Translation: AAH24181.1.
AF191544 Genomic DNA. No translation available.
X99101 mRNA. Translation: CAA67555.1. Different initiation.
AF074598 mRNA. Translation: AAC25602.1.
AF074599 mRNA. Translation: AAC25603.1.

IPI

IPI00023212.
IPI00218153.
IPI00218155.
IPI00218156.
IPI00218157.
IPI00218158.
IPI00218159.
IPI00397583.

PIR

JC5939.
PW0044.
S71400.

RefSeq

NP_001035365.1. NM_001040275.1.
NP_001201831.1. NM_001214902.1.
NP_001201832.1. NM_001214903.1.
NP_001258805.1. NM_001271876.1.
NP_001258806.1. NM_001271877.1.
NP_001428.1. NM_001437.2.

UniGene

Hs.660607.
Hs.734038.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L2J	X-ray	2.95	A/B	256-505	[»]
1NDE	X-ray	3.00	A	256-501	[»]
1QKM	X-ray	1.80	A	255-509	[»]
1U3Q	X-ray	2.40	A/B/C/D	261-500	[»]
1U3R	X-ray	2.21	A/B	261-501	[»]
1U3S	X-ray	2.50	A/B	261-500	[»]
1U9E	X-ray	2.40	A/B	261-501	[»]
1X76	X-ray	2.20	A/B	261-500	[»]
1X78	X-ray	2.30	A/B	261-500	[»]
1X7B	X-ray	2.30	A/B	261-500	[»]
1X7J	X-ray	2.30	A/B	261-500	[»]
1YY4	X-ray	2.70	A/B	263-530	[»]
1YYE	X-ray	2.03	A/B	263-530	[»]
1ZAF	X-ray	2.20	A/B	263-500	[»]
2FSZ	X-ray	2.20	A/B	257-502	[»]
2GIU	X-ray	2.20	A	260-500	[»]
2I0G	X-ray	2.50	A/B	256-505	[»]
2JJ3	X-ray	2.28	A/B	256-505	[»]
2NV7	X-ray	2.10	A/B	263-500	[»]
2QTU	X-ray	2.53	A/B	256-505	[»]
2YJD	X-ray	1.93	A/B	261-500	[»]
2YLY	X-ray	3.20	A/B	260-500	[»]
2Z4B	X-ray	2.34	A/B	256-505	[»]
3OLL	X-ray	1.50	A/B	261-500	[»]
3OLS	X-ray	2.20	A/B	261-500	[»]
3OMO	X-ray	2.21	A/B	261-500	[»]
3OMP	X-ray	2.05	A/B	261-500	[»]
3OMQ	X-ray	1.97	A/B	261-500	[»]
4J24	X-ray	2.10	A/B/C/D	261-500	[»]
4J26	X-ray	2.30	A/B	261-500	[»]

DisProt

DP00079.

ProteinModelPortal

Q92731.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5966N.

IntAct

Q92731. 287 interactions.

PTM databases

PhosphoSite

Q92731.

Polymorphism databases

DMDM

6166154.

Proteomic databases

PaxDb

Q92731.

PRIDE

Q92731.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000267525; ENSP00000267525; ENSG00000140009.
ENST00000341099; ENSP00000343925; ENSG00000140009.
ENST00000344288; ENSP00000345616; ENSG00000140009.
ENST00000353772; ENSP00000335551; ENSG00000140009.
ENST00000357782; ENSP00000350427; ENSG00000140009.
ENST00000358599; ENSP00000351412; ENSG00000140009.
ENST00000554572; ENSP00000450699; ENSG00000140009.
ENST00000555278; ENSP00000450488; ENSG00000140009.
ENST00000557772; ENSP00000451582; ENSG00000140009.

GeneID

2100.

KEGG

hsa:2100.

UCSC

uc001xgy.2. human.
uc001xgz.2. human.
uc001xha.1. human.
uc010aqc.1. human.

Organism-specific databases

CTD

2100.

GeneCards

GC14M064550.

HGNC

HGNC:3468. ESR2.

HPA

CAB022544.

MIM

601663. gene.

neXtProt

NX_Q92731.

PharmGKB

PA27886.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG271979.

HOVERGEN

HBG108344.

InParanoid

Q92731.

KO

K08551.

OMA

LYAEPQK.

OrthoDB

EOG41RPTT.

PhylomeDB

Q92731.

Enzyme and pathway databases

Pathway_Interaction_DB

er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92731.

Bgee

Q92731.

Genevestigator

Q92731.

GermOnline

ENSG00000140009. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.
3.30.50.10. 1 hit.

InterPro

IPR021064. Estrogen_rcpt_beta_N.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Pfam

PF12497. ERbeta_N. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PIRSF

PIRSF002527. ER-like_NR. 1 hit.

PRINTS

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

Q92731.

ChEMBL

CHEMBL242.

DrugBank

DB01128. Bicalutamide.
DB00783. Estradiol.
DB01196. Estramustine.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB01108. Trilostane.

EvolutionaryTrace

Q92731.

GenomeRNAi

2100.

NextBio

8495.

PMAP-CutDB

A8K8K5.

SOURCE

Search...

Entry information

Entry name

ESR2_HUMAN

Accession

Primary (citable) accession number: Q92731
Secondary accession number(s): A8K8K5 , O60608, O60685, O60702, O60703, O75583, O75584, Q0MWT5, Q0MWT6, Q86Z31, Q9UEV6, Q9UHD3, Q9UQK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 15, 1999
Last modified:	May 1, 2013
This is version 163 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.