Q9XSW2 · ESR2_PIG

  • Protein
    Estrogen receptor beta
  • Gene
    ESR2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner.

Features

Showing features for dna binding.

152650100150200250300350400450500
TypeIDPosition(s)Description
DNA binding146-211Nuclear receptor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Molecular Functionestrogen response element binding
Molecular Functionnuclear estrogen receptor activity
Molecular Functionnuclear receptor activity
Molecular Functionsteroid binding
Molecular Functionzinc ion binding
Biological Processcellular response to estradiol stimulus
Biological Processcellular response to estrogen stimulus
Biological Processestrogen receptor signaling pathway
Biological Processpositive regulation of DNA-binding transcription factor activity
Biological Processpositive regulation of DNA-templated transcription
Biological Processregulation of transcription by RNA polymerase II

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Estrogen receptor beta
  • Short names
    ER-beta
  • Alternative names
    • Nuclear receptor subfamily 3 group A member 2

Gene names

    • Name
      ESR2
    • Synonyms
      NR3A2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    Q9XSW2
  • Secondary accessions
    • Q9BDW5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000536451-526Estrogen receptor beta
Modified residue84Phosphoserine; by MAPK
Modified residue102Phosphoserine; by MAPK

Post-translational modification

Phosphorylation at Ser-84 and Ser-102 recruits NCOA1.

Keywords

Proteomic databases

Interaction

Subunit

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 UBE1C and AKAP13. Interacts with DNTTIP2. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with DNAAF4. Interacts with PRMT2. Interacts with CCAR2 (via N-terminus) in a ligand-independent manner. Interacts with RBM39, in the presence of estradiol (E2). Interacts with STUB1/CHIP (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, zinc finger, domain.

Type
IDPosition(s)Description
Region1-145Modulating
Zinc finger146-166NR C4-type
Zinc finger182-206NR C4-type
Domain261-494NR LBD
Region502-526Disordered

Domain

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

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    526
  • Mass (Da)
    58,850
  • Last updated
    2001-12-19 v2
  • Checksum
    35CE2DF661078BF6
MDIKNSPSNLNSPVSYNCSQSVLPLEPGPIYIPSSYVESCHEYSAMTFYSPAVVNYSISSNSEVGPGRQATSPNVLWPTPGHLSPLAIHCQPSLLYAEPQKSPWCDTRSLEHTLPVNRETLKRKASGSSCASPVTSPSSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRIVRKQRNSEGHLHCLSRAKKNGDHTTRVKELLLSTLSPEQLVLTLLEAEPPHVLVSRPSTPFTEASMMMSLTKLADKELVHMISWAKKIPGFMELSLYDQVRLLESCWLEVLMVGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPSAAAQEAESSRKLTHLLNAVTDALVWVIARSGISSQQQSVRLANLLMLLSHVRHASNKGTEHLLNMKCKNVVPVYDLLLEMLNAHTLRGNKSLVTGSERSRMEESESKEGSQKPQAQ

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict317in Ref. 2; AAK15151
Sequence conflict469in Ref. 2; AAK15151

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF164957
EMBL· GenBank· DDBJ
AAD45381.2
EMBL· GenBank· DDBJ
mRNA
AF267736
EMBL· GenBank· DDBJ
AAK15151.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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