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Q92731

- ESR2_HUMAN

UniProt

Q92731 - ESR2_HUMAN

Protein

Estrogen receptor beta

Gene

ESR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    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 receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri149 – 16921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri185 – 20925NR C4-typePROSITE-ProRule annotationAdd
    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 Source: InterPro
    10. sequence-specific DNA binding transcription factor activity Source: ProtInc
    11. steroid binding Source: UniProtKB
    12. steroid hormone receptor activity Source: ProtInc
    13. transcription coactivator activity Source: ProtInc
    14. 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, DNA-templated Source: UniProtKB-KW
    19. transcription initiation from RNA polymerase II promoter Source: Reactome
    20. uterus development Source: Ensembl
    21. vagina development Source: Ensembl

    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 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    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 NCOA1.1 Publication

    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.By similarity9 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri149 – 16921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri185 – 20925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    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. 1 PublicationVSP_003685Add
    BLAST
    Alternative sequencei319 – 3235FVELS → MRGNA in isoform 3. 2 PublicationsVSP_003684
    Alternative sequencei324 – 530207Missing in isoform 3. 2 PublicationsVSP_003686Add
    BLAST
    Alternative sequencei365 – 37511DEGKCVEGILE → YVPSGHSDPGC in isoform 8. 1 PublicationVSP_003687Add
    BLAST
    Alternative sequencei376 – 530155Missing in isoform 8. 1 PublicationVSP_003688Add
    BLAST
    Alternative sequencei469 – 53062SNKGM…NPQSQ → RAEKASQTLTSFGMKMETLL PEATMEQ in isoform 2. 3 PublicationsVSP_003689Add
    BLAST
    Alternative sequencei469 – 53062SNKGM…NPQSQ → SSLSLSWRLFMLREASCHGV RQTPGGAHMSVSRSRSFEAC QQPRE in isoform 4. 1 PublicationVSP_003690Add
    BLAST
    Alternative sequencei469 – 53062SNKGM…NPQSQ → RWGEKQFIHLKLS in isoform 5. 2 PublicationsVSP_003691Add
    BLAST
    Alternative sequencei469 – 53062SNKGM…NPQSQ → RYAP in isoform 6. 2 PublicationsVSP_003692Add
    BLAST
    Alternative sequencei469 – 4746SNKGME → RSCVYK in isoform 9. CuratedVSP_055746
    Alternative sequencei475 – 53056Missing in isoform 9. CuratedVSP_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]
    ENST00000358599; ENSP00000351412; ENSG00000140009. [Q92731-2]
    ENST00000553796; ENSP00000452426; ENSG00000140009. [Q92731-9]
    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 ]
    ENST00000358599 ; ENSP00000351412 ; ENSG00000140009 . [Q92731-2 ]
    ENST00000553796 ; ENSP00000452426 ; ENSG00000140009 . [Q92731-9 ]
    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

    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: October 1, 2014
    This is version 178 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