Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08537 (ESR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 (ER-alpha), and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. May play a role in ovarian follicular growth and maturation.

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, UBE1C and AKAP13. Interacts with DNTTIP2 By similarity. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes. Interacts with DYX1C1. Interacts with PRMT2 By similarity. Ref.9 Ref.14

Subcellular location

Nucleus.

Tissue specificity

Expressed in prostate, ovary, Leydig cells and in epithelium of the efferent ductules and of the initial segment of the epididymis. Ref.10

Induction

Isoforms 1 and 2 are down-regulated by 17-beta-estradiol. Ref.6

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 AAC17919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAI41076.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAI45330.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAL15175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC35719.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC35770.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from mutant phenotype PubMed 12515851. Source: MGI

epithelial cell maturation involved in prostate gland development

Inferred from mutant phenotype PubMed 15187231. Source: MGI

hormone-mediated apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15187231. Source: MGI

intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 12370428. Source: MGI

negative regulation of androgen receptor signaling pathway

Inferred from mutant phenotype PubMed 12370428. Source: MGI

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 18464259. Source: MGI

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 12370428PubMed 15187231. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from mutant phenotype PubMed 12515851. Source: MGI

ovarian follicle development

Inferred from mutant phenotype PubMed 10976058PubMed 9861029. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

prostate gland epithelium morphogenesis

Inferred from mutant phenotype PubMed 12370428PubMed 15187231. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 9697695. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

uterus development

Inferred from genetic interaction PubMed 10976058. Source: MGI

vagina development

Inferred from genetic interaction PubMed 10976058. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 14552897. Source: MGI

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 12801993PubMed 14502087PubMed 14552897. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.4. Source: MGI

core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

estrogen receptor activity

Inferred from electronic annotation. Source: InterPro

estrogen response element binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 21565615. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

steroid binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FosP011012EBI-2526214,EBI-4288185

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O08537-1)

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: O08537-2)

Also known as: Beta-2;

The sequence of this isoform differs from the canonical sequence as follows:
     364-364: R → RSSEDPHWHVAQTKSAVPR
Isoform 3 (identifier: O08537-4)

Also known as: Beta-5A;

The sequence of this isoform differs from the canonical sequence as follows:
     319-409: Missing.
Note: Corresponds to exons 5 and 6 deletion (PubMed:9685228).
Isoform 4 (identifier: O08537-6)

The sequence of this isoform differs from the canonical sequence as follows:
     319-343: FVELSLLDQVRLLESCWMEVLMVGL → MRGSAWKGFWKSLTCSWRRRHGSVS
     344-530: Missing.
Note: Corresponds to exon 5 deletion (PubMed:9685228). May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Isoform 5 (identifier: O08537-7)

The sequence of this isoform differs from the canonical sequence as follows:
     365-377: DEGKCVEGILEIF → YVPLGYRKPGSRE
     378-530: Missing.
Note: Corresponds to exon 6 deletion (PubMed:9685228). May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Estrogen receptor beta
PRO_0000053644

Regions

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

Amino acid modifications

Modified residue611Phosphoserine; alternate Ref.13
Modified residue871Phosphoserine; by MAPK Ref.12
Modified residue1051Phosphoserine; by MAPK Ref.12
Glycosylation611O-linked (GlcNAc); alternate Ref.13
CAR_000201

Natural variations

Alternative sequence319 – 40991Missing in isoform 3.
VSP_003696
Alternative sequence319 – 34325FVELS…LMVGL → MRGSAWKGFWKSLTCSWRRR HGSVS in isoform 4.
VSP_042429
Alternative sequence344 – 530187Missing in isoform 4.
VSP_042430
Alternative sequence3641R → RSSEDPHWHVAQTKSAVPR in isoform 2.
VSP_003693
Alternative sequence365 – 37713DEGKC…ILEIF → YVPLGYRKPGSRE in isoform 5.
VSP_042431
Alternative sequence378 – 530153Missing in isoform 5.
VSP_042432

Experimental info

Mutagenesis1051S → A: Abolishes stimulatory effect of Ras.
Mutagenesis1391S → A: No loss of the stimulatory effect of Ras.
Sequence conflict471T → A in CAA03949. Ref.5
Sequence conflict1421A → T in CAA03949. Ref.5
Sequence conflict2001S → N in CAA03949. Ref.5
Sequence conflict3781D → G in AAB51132. Ref.1
Sequence conflict3781D → G in AAL15175. Ref.6
Sequence conflict4121P → H in CAA03949. Ref.5
Sequence conflict4451G → R in CAA03949. Ref.5
Sequence conflict5111E → G in CAA03949. Ref.5

Sequences

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

Last modified March 21, 2012. Version 3.
Checksum: BEFA25F62650A8D4

FASTA53059,070
        10         20         30         40         50         60 
MEIKNSPSSL TSPASYNCSQ SILPLEHGPI YIPSSYVESR HEYSAMTFYS PAVMNYSVPS 

        70         80         90        100        110        120 
STGNLEGGPV RQTASPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN 

       130        140        150        160        170        180 
RETLKRKLGG SGCASPVTSP SAKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH 

       190        200        210        220        230        240 
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSASEQVH 

       250        260        270        280        290        300 
CLNKAKRTSG HTPRVKELLL NSLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK 

       310        320        330        340        350        360 
LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL 

       370        380        390        400        410        420 
VLDRDEGKCV EGILEIFDML LATTARFREL KLQHKEYLCV KAMILLNSSM YPLATASQEA 

       430        440        450        460        470        480 
ESSRKLTHLL NAVTDALVWV ISKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK 

       490        500        510        520        530 
CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECCSTEDSKS KEGSQNLQSQ 

« Hide

Isoform 2 (Beta-2) [UniParc].

Checksum: 5A3BFF5FCD158E7C
Show »

FASTA54861,084
Isoform 3 (Beta-5A) [UniParc].

Checksum: FCA85E5235E368D2
Show »

FASTA43948,550
Isoform 4 [UniParc].

Checksum: 0073C2E153F493D3
Show »

FASTA34338,185
Isoform 5 [UniParc].

Checksum: 59314206E084E413
Show »

FASTA37742,107

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Ovary.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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 1).
Tissue: Brain.
[4]"Cloning, chromosomal localization, and functional analysis of the murine estrogen receptor beta."
Tremblay G.B., Tremblay A., Copeland N.G., Gilbert D.J., Jenkins N.A., Labrie F., Giguere V.
Mol. Endocrinol. 11:353-365(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-530, MUTAGENESIS.
Strain: 129/Sv.
Tissue: Ovary.
[5]"Mouse estrogen receptor beta forms estrogen response element-binding heterodimers with estrogen receptor alpha."
Pettersson K., Grandien K., Kuiper G.G.J.M., Gustafsson J.-A.
Mol. Endocrinol. 11:1486-1496(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-530, CHARACTERIZATION.
Tissue: Ovary.
[6]"Exposure of KS483 cells to estrogen enhances osteogenesis and inhibits adipogenesis."
Dang Z.C., van Bezooijen R.L., Karperien M., Papapoulos S.E., Lowik C.W.
J. Bone Miner. Res. 17:394-405(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), INDUCTION.
Strain: ddY.
Tissue: Calvaria.
[7]Leygue E., Lu B., Dotzlaw H., Glor C., Watson P.H., Murphy L.C.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
Tissue: Ovary.
[8]Rosenfeld C.S., Lubahn D.B.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
Tissue: Ovary.
[9]"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA3.
[10]"Transcription and translation of estrogen receptor-beta in the male reproductive tract of estrogen receptor-alpha knock-out and wild-type mice."
Rosenfeld C.S., Ganjam V.K., Taylor J.A., Yuan X., Stiehr J.R., Hardy M.P., Lubahn D.B.
Endocrinology 139:2982-2987(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"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: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
Tissue: Ovary.
[12]"Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1."
Tremblay A., Tremblay G.B., Labrie F., Giguere V.
Mol. Cell 3:513-519(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-87 AND SER-105.
[13]"Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta."
Cheng X., Cole R.N., Zaia J., Hart G.W.
Biochemistry 39:11609-11620(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-61, PHOSPHORYLATION AT SER-61.
[14]"Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK054290 mRNA. Translation: BAC35719.1. Different initiation.
AK054413 mRNA. Translation: BAC35770.1. Different initiation.
AC164121 Genomic DNA. No translation available.
BC141075 mRNA. Translation: AAI41076.1. Different initiation.
BC145329 mRNA. Translation: AAI45330.1. Different initiation.
U81451 mRNA. Translation: AAB51132.1.
AJ000220 Genomic DNA. Translation: CAA03949.1.
AY054413 mRNA. Translation: AAL15175.1. Different initiation.
AF067422 mRNA. Translation: AAC17919.1. Different initiation.
AF063853 mRNA. Translation: AAC16656.1.
RefSeqNP_034287.3. NM_010157.3.
NP_997590.1. NM_207707.1.
UniGeneMm.2561.

3D structure databases

ProteinModelPortalO08537.
SMRO08537. Positions 147-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08537. 2 interactions.

Chemistry

BindingDBO08537.
ChEMBLCHEMBL2995.
GuidetoPHARMACOLOGY621.

PTM databases

PhosphoSiteO08537.
UniCarbKBO08537.

Proteomic databases

PRIDEO08537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076634; ENSMUSP00000075932; ENSMUSG00000021055.
ENSMUST00000101291; ENSMUSP00000098849; ENSMUSG00000021055.
ENSMUST00000110421; ENSMUSP00000106051; ENSMUSG00000021055.
GeneID13983.
KEGGmmu:13983.
UCSCuc007nxu.1. mouse. [O08537-2]
uc007nxv.1. mouse. [O08537-1]

Organism-specific databases

CTD2100.
MGIMGI:109392. Esr2.

Phylogenomic databases

eggNOGNOG271979.
GeneTreeENSGT00730000110346.
HOGENOMHOG000233468.
HOVERGENHBG108344.
KOK08551.
OrthoDBEOG7288S1.
TreeFamTF323751.

Gene expression databases

ArrayExpressO08537.
BgeeO08537.
CleanExMM_ESR2.
GenevestigatorO08537.

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. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284858.
PROO08537.
SOURCESearch...

Entry information

Entry nameESR2_MOUSE
AccessionPrimary (citable) accession number: O08537
Secondary accession number(s): B2RUC6 expand/collapse secondary AC list , E9QKX7, O35635, O70519, Q8BG65, Q91Z86
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 21, 2012
Last modified: June 11, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot