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Q92731

- ESR2_HUMAN

UniProt

Q92731 - ESR2_HUMAN

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Protein

Estrogen receptor beta

Gene
ESR2, ESTRB, NR3A2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi149 – 21466Nuclear receptorAdd
BLAST
Zinc fingeri149 – 16921NR C4-typeAdd
BLAST
Zinc fingeri185 – 20925NR C4-typeAdd
BLAST

GO - Molecular functioni

  1. core promoter sequence-specific DNA binding Source: UniProtKB
  2. DNA binding Source: ProtInc
  3. enzyme binding Source: UniProtKB
  4. estrogen receptor activity Source: UniProtKB
  5. estrogen response element binding Source: UniProtKB
  6. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. receptor antagonist activity Source: UniProtKB
  9. sequence-specific DNA binding transcription factor activity Source: ProtInc
  10. steroid binding Source: UniProtKB
  11. steroid hormone receptor activity Source: ProtInc
  12. transcription coactivator activity Source: ProtInc
  13. zinc ion binding Source: InterPro

GO - Biological processi

  1. brain development Source: Ensembl
  2. cell-cell signaling Source: ProtInc
  3. epithelial cell maturation involved in prostate gland development Source: Ensembl
  4. extracellular negative regulation of signal transduction Source: GOC
  5. gene expression Source: Reactome
  6. hormone-mediated apoptotic signaling pathway Source: Ensembl
  7. intracellular estrogen receptor signaling pathway Source: UniProtKB
  8. negative regulation of androgen receptor signaling pathway Source: Ensembl
  9. negative regulation of cell growth Source: UniProtKB
  10. negative regulation of epithelial cell proliferation Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. neuron migration Source: Ensembl
  13. ovarian follicle development Source: Ensembl
  14. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  15. prostate gland epithelium morphogenesis Source: Ensembl
  16. regulation of transcription, DNA-templated Source: UniProtKB
  17. signal transduction Source: ProtInc
  18. transcription initiation from RNA polymerase II promoter Source: Reactome
  19. uterus development Source: Ensembl
  20. vagina development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiQ92731.

Names & Taxonomyi

Protein namesi
Recommended name:
Estrogen receptor beta
Short name:
ER-beta
Alternative name(s):
Nuclear receptor subfamily 3 group A member 2
Gene namesi
Name:ESR2
Synonyms:ESTRB, NR3A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:3468. ESR2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. extracellular region Source: GOC
  2. mitochondrion Source: MGI
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-105. 1 Publication
Mutagenesisi87 – 871S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-105. 1 Publication
Mutagenesisi105 – 1051S → A: Enhances repression by activated ErbB2/ErbB3; when associated with A-87. 1 Publication
Mutagenesisi105 – 1051S → D: Abolishes repression by activated ErbB2/ErbB3; when associated with D-87. 1 Publication

Organism-specific databases

PharmGKBiPA27886.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Estrogen receptor betaPRO_0000053642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei105 – 1051Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ92731.
PRIDEiQ92731.

PTM databases

PhosphoSiteiQ92731.

Miscellaneous databases

PMAP-CutDBA8K8K5.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiQ92731.
BgeeiQ92731.
GenevestigatoriQ92731.

Organism-specific databases

HPAiCAB022544.

Interactioni

Subunit structurei

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 PRMT2.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP5CP530414EBI-78505,EBI-716663
TXNRD1Q16881-43EBI-78505,EBI-9080335

Protein-protein interaction databases

BioGridi108404. 88 interactions.
DIPiDIP-5966N.
IntActiQ92731. 288 interactions.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi261 – 2633
Helixi265 – 27511
Beta strandi286 – 2883
Helixi291 – 31424
Helixi319 – 3213
Helixi324 – 34724
Beta strandi348 – 3503
Beta strandi353 – 3575
Beta strandi359 – 3635
Helixi364 – 3696
Helixi373 – 38917
Helixi394 – 40613
Beta strandi407 – 4093
Helixi411 – 4133
Helixi417 – 4193
Helixi421 – 44222
Turni443 – 4453
Helixi448 – 48134
Beta strandi482 – 4843
Helixi489 – 4979

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00079.
ProteinModelPortaliQ92731.
SMRiQ92731. Positions 147-498.

Miscellaneous databases

EvolutionaryTraceiQ92731.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 148148ModulatingAdd
BLAST
Regioni215 – 530316Steroid-bindingAdd
BLAST

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG271979.
HOVERGENiHBG108344.
InParanoidiQ92731.
KOiK08551.
OMAiEPQKSPW.
PhylomeDBiQ92731.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR028355. 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]
PfamiPF12497. ERbeta_N. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF500102. ER-b. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92731-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS    50
PAVMNYSIPS NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA 100
EPQKSPWCEA RSLEHTLPVN RETLKRKVSG NRCASPVTGP GSKRDAHFCA 150
VCSDYASGYH YGVWSCEGCK AFFKRSIQGH NDYICPATNQ CTIDKNRRKS 200
CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH CAGKAKRSGG 250
HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK 300
LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH 350
PGKLIFAPDL VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV 400
KAMILLNSSM YPLVTATQDA DSSRKLAHLL NAVTDALVWV IAKSGISSQQ 450
QSMRLANLLM LLSHVRHASN KGMEHLLNMK CKNVVPVYDL LLEMLNAHVL 500
RGCKSSITGS ECSPAEDSKS KEGSQNPQSQ 530
Length:530
Mass (Da):59,216
Last modified:July 15, 1999 - v2
Checksum:i8CAE34215992418A
GO
Isoform 2 (identifier: Q92731-2) [UniParc]FASTAAdd to Basket

Also known as: Beta-2, CX

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

Show »
Length:495
Mass (Da):55,483
Checksum:iF068DBC63DC838A6
GO
Isoform 3 (identifier: Q92731-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:323
Mass (Da):35,944
Checksum:i158D376C56D3CA12
GO
Isoform 4 (identifier: Q92731-4) [UniParc]FASTAAdd to Basket

Also known as: Beta-3

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

Show »
Length:513
Mass (Da):57,518
Checksum:iEE88C42CBB24775E
GO
Isoform 5 (identifier: Q92731-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:481
Mass (Da):54,096
Checksum:i9B6017FE950720F0
GO
Isoform 6 (identifier: Q92731-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:472
Mass (Da):52,959
Checksum:i673B0DB5FAF03C26
GO
Isoform 7 (identifier: Q92731-7) [UniParc]FASTAAdd to Basket

Also known as: Beta-5A

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

Show »
Length:439
Mass (Da):48,614
Checksum:i35B686E3C0D32D0F
GO
Isoform 8 (identifier: Q92731-8) [UniParc]FASTAAdd to Basket

Also known as: Beta-6

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

Show »
Length:375
Mass (Da):41,948
Checksum:iE2FA83EE3C519EE5
GO
Isoform 9 (identifier: Q92731-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     469-474: SNKGME → RSCVYK
     475-530: Missing.

Show »
Length:474
Mass (Da):53,209
Checksum:i4558F2986355FAF0
GO

Sequence cautioni

The sequence CAA67555.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei319 – 40991Missing in isoform 7. VSP_003685Add
BLAST
Alternative sequencei319 – 3235FVELS → MRGNA in isoform 3. VSP_003684
Alternative sequencei324 – 530207Missing in isoform 3. VSP_003686Add
BLAST
Alternative sequencei365 – 37511DEGKCVEGILE → YVPSGHSDPGC in isoform 8. VSP_003687Add
BLAST
Alternative sequencei376 – 530155Missing in isoform 8. VSP_003688Add
BLAST
Alternative sequencei469 – 53062SNKGM…NPQSQ → RAEKASQTLTSFGMKMETLL PEATMEQ in isoform 2. VSP_003689Add
BLAST
Alternative sequencei469 – 53062SNKGM…NPQSQ → SSLSLSWRLFMLREASCHGV RQTPGGAHMSVSRSRSFEAC QQPRE in isoform 4. VSP_003690Add
BLAST
Alternative sequencei469 – 53062SNKGM…NPQSQ → RWGEKQFIHLKLS in isoform 5. VSP_003691Add
BLAST
Alternative sequencei469 – 53062SNKGM…NPQSQ → RYAP in isoform 6. VSP_003692Add
BLAST
Alternative sequencei469 – 4746SNKGME → RSCVYK in isoform 9. VSP_055746
Alternative sequencei475 – 53056Missing in isoform 9. VSP_055747Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
AL161756 Genomic DNA. No translation available.
AL355094 Genomic DNA. No translation available.
AL359235 Genomic DNA. No translation available.
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.
CCDSiCCDS32096.1. [Q92731-2]
CCDS55920.1. [Q92731-5]
CCDS61469.1. [Q92731-7]
CCDS9762.1. [Q92731-1]
PIRiJC5939.
PW0044.
S71400.
RefSeqiNP_001035365.1. NM_001040275.1. [Q92731-2]
NP_001201831.1. NM_001214902.1. [Q92731-5]
NP_001258805.1. NM_001271876.1.
NP_001258806.1. NM_001271877.1. [Q92731-7]
NP_001278641.1. NM_001291712.1. [Q92731-2]
NP_001278652.1. NM_001291723.1. [Q92731-2]
NP_001428.1. NM_001437.2. [Q92731-1]
XP_006720139.1. XM_006720076.1. [Q92731-2]
UniGeneiHs.660607.
Hs.734038.
Hs.734416.

Genome annotation databases

EnsembliENST00000267525; 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]
ENST00000553796; ENSP00000452426; ENSG00000140009.
ENST00000554572; ENSP00000450699; ENSG00000140009. [Q92731-2]
ENST00000555278; ENSP00000450488; ENSG00000140009. [Q92731-5]
ENST00000557772; ENSP00000451582; ENSG00000140009. [Q92731-6]
GeneIDi2100.
KEGGihsa:2100.
UCSCiuc001xgy.2. human. [Q92731-5]
uc001xgz.2. human. [Q92731-6]
uc001xha.1. human. [Q92731-1]
uc010aqc.1. human. [Q92731-7]

Polymorphism databases

DMDMi6166154.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Estrogen receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
AL161756 Genomic DNA. No translation available.
AL355094 Genomic DNA. No translation available.
AL359235 Genomic DNA. No translation available.
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 .
CCDSi CCDS32096.1. [Q92731-2 ]
CCDS55920.1. [Q92731-5 ]
CCDS61469.1. [Q92731-7 ]
CCDS9762.1. [Q92731-1 ]
PIRi JC5939.
PW0044.
S71400.
RefSeqi NP_001035365.1. NM_001040275.1. [Q92731-2 ]
NP_001201831.1. NM_001214902.1. [Q92731-5 ]
NP_001258805.1. NM_001271876.1.
NP_001258806.1. NM_001271877.1. [Q92731-7 ]
NP_001278641.1. NM_001291712.1. [Q92731-2 ]
NP_001278652.1. NM_001291723.1. [Q92731-2 ]
NP_001428.1. NM_001437.2. [Q92731-1 ]
XP_006720139.1. XM_006720076.1. [Q92731-2 ]
UniGenei Hs.660607.
Hs.734038.
Hs.734416.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00079.
ProteinModelPortali Q92731.
SMRi Q92731. Positions 147-498.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108404. 88 interactions.
DIPi DIP-5966N.
IntActi Q92731. 288 interactions.

Chemistry

BindingDBi Q92731.
ChEMBLi CHEMBL242.
DrugBanki DB01128. Bicalutamide.
DB00783. Estradiol.
DB01196. Estramustine.
DB00481. Raloxifene.
DB00675. Tamoxifen.
DB01108. Trilostane.
GuidetoPHARMACOLOGYi 621.

PTM databases

PhosphoSitei Q92731.

Polymorphism databases

DMDMi 6166154.

Proteomic databases

PaxDbi Q92731.
PRIDEi Q92731.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000267525 ; 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 ]
ENST00000553796 ; ENSP00000452426 ; ENSG00000140009 .
ENST00000554572 ; ENSP00000450699 ; ENSG00000140009 . [Q92731-2 ]
ENST00000555278 ; ENSP00000450488 ; ENSG00000140009 . [Q92731-5 ]
ENST00000557772 ; ENSP00000451582 ; ENSG00000140009 . [Q92731-6 ]
GeneIDi 2100.
KEGGi hsa:2100.
UCSCi uc001xgy.2. human. [Q92731-5 ]
uc001xgz.2. human. [Q92731-6 ]
uc001xha.1. human. [Q92731-1 ]
uc010aqc.1. human. [Q92731-7 ]

Organism-specific databases

CTDi 2100.
GeneCardsi GC14M064550.
HGNCi HGNC:3468. ESR2.
HPAi CAB022544.
MIMi 601663. gene.
neXtProti NX_Q92731.
PharmGKBi PA27886.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271979.
HOVERGENi HBG108344.
InParanoidi Q92731.
KOi K08551.
OMAi EPQKSPW.
PhylomeDBi Q92731.
TreeFami TF323751.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki Q92731.

Miscellaneous databases

EvolutionaryTracei Q92731.
GeneWikii Estrogen_receptor_beta.
GenomeRNAii 2100.
NextBioi 8495.
PMAP-CutDB A8K8K5.
PROi Q92731.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92731.
Bgeei Q92731.
Genevestigatori Q92731.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR028355. 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 ]
Pfami PF12497. ERbeta_N. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PIRSFi PIRSF500102. ER-b. 1 hit.
PIRSF002527. ER-like_NR. 1 hit.
PRINTSi PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. 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. 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.

Entry informationi

Entry nameiESR2_HUMAN
AccessioniPrimary (citable) accession number: Q92731
Secondary accession number(s): A8K8K5
, G3V5M5, O60608, O60685, O60702, O60703, O75583, O75584, Q0MWT5, Q0MWT6, Q86Z31, Q9UEV6, Q9UHD3, Q9UQK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: September 3, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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