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Q92731 (ESR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen receptor beta

Short name=ER-beta
Alternative name(s):
Nuclear receptor subfamily 3 group A member 2
Gene names
Name:ESR2
Synonyms:ESTRB, NR3A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence 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-cxlacks 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/cxpreferentially 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-1is 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-2is 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-3is found in testis. Isoform beta-4is expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. Isoform beta-5is 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionReceptor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Traceable author statement Ref.12. Source: ProtInc

epithelial cell maturation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

extracellular negative regulation of signal transduction

Non-traceable author statement Ref.4. Source: GOC

gene expression

Traceable author statement. Source: Reactome

hormone-mediated apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

intracellular estrogen receptor signaling pathway

Traceable author statement PubMed 11181953. Source: UniProtKB

negative regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Non-traceable author statement PubMed 11181953. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15345745. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

regulation of transcription, DNA-templated

Traceable author statement PubMed 11181953. Source: UniProtKB

signal transduction

Traceable author statement PubMed 10749889Ref.12. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

uterus development

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Non-traceable author statement Ref.4. Source: GOC

mitochondrion

Inferred from direct assay PubMed 15024130. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 11181953. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 15345745. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.19. 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

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.12. Source: ProtInc

steroid binding

Inferred from sequence or structural similarity. Source: UniProtKB

steroid hormone receptor activity

Traceable author statement PubMed 10749889. Source: ProtInc

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

PPP5CP530414EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Estrogen receptor beta
PRO_0000053642

Regions

DNA binding149 – 21466Nuclear receptor
Zinc finger149 – 16921NR C4-type
Zinc finger185 – 20925NR C4-type
Region1 – 148148Modulating
Region215 – 530316Steroid-binding

Amino acid modifications

Modified residue871Phosphoserine Ref.24
Modified residue1051Phosphoserine Ref.24

Natural variations

Alternative sequence319 – 40991Missing in isoform 7.
VSP_003685
Alternative sequence319 – 3235FVELS → MRGNA in isoform 3.
VSP_003684
Alternative sequence324 – 530207Missing in isoform 3.
VSP_003686
Alternative sequence365 – 37511DEGKCVEGILE → YVPSGHSDPGC in isoform 8.
VSP_003687
Alternative sequence376 – 530155Missing in isoform 8.
VSP_003688
Alternative sequence469 – 53062SNKGM…NPQSQ → RAEKASQTLTSFGMKMETLL PEATMEQ in isoform 2.
VSP_003689
Alternative sequence469 – 53062SNKGM…NPQSQ → SSLSLSWRLFMLREASCHGV RQTPGGAHMSVSRSRSFEAC QQPRE in isoform 4.
VSP_003690
Alternative sequence469 – 53062SNKGM…NPQSQ → RWGEKQFIHLKLS in isoform 5.
VSP_003691
Alternative sequence469 – 53062SNKGM…NPQSQ → RYAP in isoform 6.
VSP_003692

Experimental info

Mutagenesis871S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-105. Ref.24
Mutagenesis871S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-105. Ref.24
Mutagenesis1051S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-87. Ref.24
Mutagenesis1051S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-87. Ref.24

Secondary structure

.................................... 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta-1) [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 8CAE34215992418A

FASTA53059,216
        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 

« Hide

Isoform 2 (Beta-2) (CX) [UniParc].

Checksum: F068DBC63DC838A6
Show »

FASTA49555,483
Isoform 3 (Beta-2A) [UniParc].

Checksum: 158D376C56D3CA12
Show »

FASTA32335,944
Isoform 4 (Beta-3) [UniParc].

Checksum: EE88C42CBB24775E
Show »

FASTA51357,518
Isoform 5 (Beta-4) [UniParc].

Checksum: 9B6017FE950720F0
Show »

FASTA48154,096
Isoform 6 (Beta-5) [UniParc].

Checksum: 673B0DB5FAF03C26
Show »

FASTA47252,959
Isoform 7 (Beta-5A) [UniParc].

Checksum: 35B686E3C0D32D0F
Show »

FASTA43948,614
Isoform 8 (Beta-6) [UniParc].

Checksum: E2FA83EE3C519EE5
Show »

FASTA37541,948

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (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.

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.
PIRJC5939.
PW0044.
S71400.
RefSeqNP_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.
UniGeneHs.660607.
Hs.734038.
Hs.734416.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L2JX-ray2.95A/B256-505[»]
1NDEX-ray3.00A256-501[»]
1QKMX-ray1.80A255-509[»]
1U3QX-ray2.40A/B/C/D261-500[»]
1U3RX-ray2.21A/B261-501[»]
1U3SX-ray2.50A/B261-500[»]
1U9EX-ray2.40A/B261-501[»]
1X76X-ray2.20A/B261-500[»]
1X78X-ray2.30A/B261-500[»]
1X7BX-ray2.30A/B261-500[»]
1X7JX-ray2.30A/B261-500[»]
1YY4X-ray2.70A/B263-530[»]
1YYEX-ray2.03A/B263-530[»]
1ZAFX-ray2.20A/B263-500[»]
2FSZX-ray2.20A/B257-502[»]
2GIUX-ray2.20A260-500[»]
2I0GX-ray2.50A/B256-505[»]
2JJ3X-ray2.28A/B256-505[»]
2NV7X-ray2.10A/B263-500[»]
2QTUX-ray2.53A/B256-505[»]
2YJDX-ray1.93A/B261-500[»]
2YLYX-ray3.20A/B260-500[»]
2Z4BX-ray2.34A/B256-505[»]
3OLLX-ray1.50A/B261-500[»]
3OLSX-ray2.20A/B261-500[»]
3OMOX-ray2.21A/B261-500[»]
3OMPX-ray2.05A/B261-500[»]
3OMQX-ray1.97A/B261-500[»]
4J24X-ray2.10A/B/C/D261-500[»]
4J26X-ray2.30A/B261-500[»]
DisProtDP00079.
ProteinModelPortalQ92731.
SMRQ92731. Positions 147-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108404. 88 interactions.
DIPDIP-5966N.
IntActQ92731. 287 interactions.

Chemistry

BindingDBQ92731.
ChEMBLCHEMBL242.
DrugBankDB01128. Bicalutamide.
DB00783. Estradiol.
DB01196. Estramustine.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB01108. Trilostane.
GuidetoPHARMACOLOGY621.

PTM databases

PhosphoSiteQ92731.

Polymorphism databases

DMDM6166154.

Proteomic databases

PaxDbQ92731.
PRIDEQ92731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267525; ENSP00000267525; ENSG00000140009. [Q92731-7]
ENST00000341099; ENSP00000343925; ENSG00000140009. [Q92731-1]
ENST00000344288; ENSP00000345616; ENSG00000140009. [Q92731-3]
ENST00000353772; ENSP00000335551; ENSG00000140009. [Q92731-2]
ENST00000357782; ENSP00000350427; ENSG00000140009. [Q92731-5]
ENST00000358599; ENSP00000351412; ENSG00000140009. [Q92731-2]
ENST00000554572; ENSP00000450699; ENSG00000140009. [Q92731-2]
ENST00000555278; ENSP00000450488; ENSG00000140009. [Q92731-5]
ENST00000557772; ENSP00000451582; ENSG00000140009. [Q92731-6]
GeneID2100.
KEGGhsa:2100.
UCSCuc001xgy.2. human. [Q92731-5]
uc001xgz.2. human. [Q92731-6]
uc001xha.1. human. [Q92731-1]
uc010aqc.1. human. [Q92731-7]

Organism-specific databases

CTD2100.
GeneCardsGC14M064550.
HGNCHGNC:3468. ESR2.
HPACAB022544.
MIM601663. gene.
neXtProtNX_Q92731.
PharmGKBPA27886.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271979.
HOVERGENHBG108344.
InParanoidQ92731.
KOK08551.
OMAEPQKSPW.
PhylomeDBQ92731.
TreeFamTF323751.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ92731.

Gene expression databases

ArrayExpressQ92731.
BgeeQ92731.
GenevestigatorQ92731.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR028355. ER-beta/gamma.
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]
PfamPF12497. ERbeta_N. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF500102. ER-b. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92731.
GeneWikiEstrogen_receptor_beta.
GenomeRNAi2100.
NextBio8495.
PMAP-CutDBA8K8K5.
PROQ92731.
SOURCESearch...

Entry information

Entry nameESR2_HUMAN
AccessionPrimary (citable) accession number: Q92731
Secondary accession number(s): A8K8K5 expand/collapse secondary AC list , 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: April 16, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM