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O08537

- ESR2_MOUSE

UniProt

O08537 - ESR2_MOUSE

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Protein

Estrogen receptor beta

Gene

Esr2

Organism
Mus musculus (Mouse)
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 (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.

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: Ensembl
  2. DNA binding Source: MGI
  3. estrogen receptor activity Source: InterPro
  4. estrogen response element binding Source: Ensembl
  5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
  6. steroid binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. brain development Source: MGI
  2. epithelial cell maturation involved in prostate gland development Source: MGI
  3. hormone-mediated apoptotic signaling pathway Source: MGI
  4. intracellular estrogen receptor signaling pathway Source: MGI
  5. negative regulation of androgen receptor signaling pathway Source: MGI
  6. negative regulation of cell proliferation Source: MGI
  7. negative regulation of epithelial cell proliferation Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. neuron migration Source: MGI
  10. ovarian follicle development Source: MGI
  11. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  12. prostate gland epithelium morphogenesis Source: MGI
  13. regulation of cell proliferation Source: MGI
  14. uterus development Source: MGI
  15. vagina development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:109392. Esr2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. mitochondrion Source: Ensembl
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051S → A: Abolishes stimulatory effect of Ras. 1 Publication
Mutagenesisi139 – 1391S → A: No loss of the stimulatory effect of Ras. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Estrogen receptor betaPRO_0000053644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine; alternate1 Publication
Glycosylationi61 – 611O-linked (GlcNAc); alternate1 PublicationCAR_000201
Modified residuei87 – 871Phosphoserine; by MAPK1 Publication
Modified residuei105 – 1051Phosphoserine; by MAPK1 Publication

Post-translational modificationi

Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO08537.

PTM databases

PhosphoSiteiO08537.
UniCarbKBiO08537.

Expressioni

Tissue specificityi

Expressed in prostate, ovary, Leydig cells and in epithelium of the efferent ductules and of the initial segment of the epididymis.1 Publication

Inductioni

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

Gene expression databases

BgeeiO08537.
CleanExiMM_ESR2.
ExpressionAtlasiO08537. baseline and differential.
GenevestigatoriO08537.

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, 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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FosP011012EBI-2526214,EBI-4288185

Protein-protein interaction databases

IntActiO08537. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliO08537.
SMRiO08537. Positions 147-498.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233468.
HOVERGENiHBG108344.
InParanoidiO08537.
KOiK08551.
OrthoDBiEOG7288S1.
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. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O08537-1) [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

        10         20         30         40         50
MEIKNSPSSL TSPASYNCSQ SILPLEHGPI YIPSSYVESR HEYSAMTFYS
60 70 80 90 100
PAVMNYSVPS STGNLEGGPV RQTASPNVLW PTSGHLSPLA THCQSSLLYA
110 120 130 140 150
EPQKSPWCEA RSLEHTLPVN RETLKRKLGG SGCASPVTSP SAKRDAHFCA
160 170 180 190 200
VCSDYASGYH YGVWSCEGCK AFFKRSIQGH NDYICPATNQ CTIDKNRRKS
210 220 230 240 250
CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSASEQVH CLNKAKRTSG
260 270 280 290 300
HTPRVKELLL NSLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK
310 320 330 340 350
LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH
360 370 380 390 400
PGKLIFAPDL VLDRDEGKCV EGILEIFDML LATTARFREL KLQHKEYLCV
410 420 430 440 450
KAMILLNSSM YPLATASQEA ESSRKLTHLL NAVTDALVWV ISKSGISSQQ
460 470 480 490 500
QSVRLANLLM LLSHVRHISN KGMEHLLSMK CKNVVPVYDL LLEMLNAHTL
510 520 530
RGYKSSISGS ECCSTEDSKS KEGSQNLQSQ
Length:530
Mass (Da):59,070
Last modified:March 21, 2012 - v3
Checksum:iBEFA25F62650A8D4
GO
Isoform 2 (identifier: O08537-2) [UniParc]FASTAAdd to Basket

Also known as: Beta-2

The sequence of this isoform differs from the canonical sequence as follows:
     364-364: R → RSSEDPHWHVAQTKSAVPR

Show »
Length:548
Mass (Da):61,084
Checksum:i5A3BFF5FCD158E7C
GO
Isoform 3 (identifier: O08537-4) [UniParc]FASTAAdd to Basket

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.1 Publication

Show »
Length:439
Mass (Da):48,550
Checksum:iFCA85E5235E368D2
GO
Isoform 4 (identifier: O08537-6) [UniParc]FASTAAdd to Basket

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.1 Publication

Show »
Length:343
Mass (Da):38,185
Checksum:i0073C2E153F493D3
GO
Isoform 5 (identifier: O08537-7) [UniParc]FASTAAdd to Basket

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.1 Publication

Show »
Length:377
Mass (Da):42,107
Checksum:i59314206E084E413
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471T → A in CAA03949. (PubMed:9280064)Curated
Sequence conflicti142 – 1421A → T in CAA03949. (PubMed:9280064)Curated
Sequence conflicti200 – 2001S → N in CAA03949. (PubMed:9280064)Curated
Sequence conflicti378 – 3781D → G in AAB51132. (PubMed:16141072)Curated
Sequence conflicti378 – 3781D → G in AAL15175. (PubMed:11878304)Curated
Sequence conflicti412 – 4121P → H in CAA03949. (PubMed:9280064)Curated
Sequence conflicti445 – 4451G → R in CAA03949. (PubMed:9280064)Curated
Sequence conflicti511 – 5111E → G in CAA03949. (PubMed:9280064)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei319 – 40991Missing in isoform 3. CuratedVSP_003696Add
BLAST
Alternative sequencei319 – 34325FVELS…LMVGL → MRGSAWKGFWKSLTCSWRRR HGSVS in isoform 4. CuratedVSP_042429Add
BLAST
Alternative sequencei344 – 530187Missing in isoform 4. CuratedVSP_042430Add
BLAST
Alternative sequencei364 – 3641R → RSSEDPHWHVAQTKSAVPR in isoform 2. 2 PublicationsVSP_003693
Alternative sequencei365 – 37713DEGKC…ILEIF → YVPLGYRKPGSRE in isoform 5. CuratedVSP_042431Add
BLAST
Alternative sequencei378 – 530153Missing in isoform 5. CuratedVSP_042432Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_034287.3. NM_010157.3.
NP_997590.1. NM_207707.1.
UniGeneiMm.2561.

Genome annotation databases

EnsembliENSMUST00000076634; ENSMUSP00000075932; ENSMUSG00000021055.
ENSMUST00000101291; ENSMUSP00000098849; ENSMUSG00000021055.
ENSMUST00000110421; ENSMUSP00000106051; ENSMUSG00000021055.
GeneIDi13983.
KEGGimmu:13983.
UCSCiuc007nxu.1. mouse. [O08537-2]
uc007nxv.1. mouse. [O08537-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_034287.3. NM_010157.3.
NP_997590.1. NM_207707.1.
UniGenei Mm.2561.

3D structure databases

ProteinModelPortali O08537.
SMRi O08537. Positions 147-498.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O08537. 2 interactions.

Chemistry

BindingDBi O08537.
ChEMBLi CHEMBL2995.
GuidetoPHARMACOLOGYi 621.

PTM databases

PhosphoSitei O08537.
UniCarbKBi O08537.

Proteomic databases

PRIDEi O08537.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000076634 ; ENSMUSP00000075932 ; ENSMUSG00000021055 .
ENSMUST00000101291 ; ENSMUSP00000098849 ; ENSMUSG00000021055 .
ENSMUST00000110421 ; ENSMUSP00000106051 ; ENSMUSG00000021055 .
GeneIDi 13983.
KEGGi mmu:13983.
UCSCi uc007nxu.1. mouse. [O08537-2 ]
uc007nxv.1. mouse. [O08537-1 ]

Organism-specific databases

CTDi 2100.
MGIi MGI:109392. Esr2.

Phylogenomic databases

eggNOGi NOG271979.
GeneTreei ENSGT00760000118887.
HOGENOMi HOG000233468.
HOVERGENi HBG108344.
InParanoidi O08537.
KOi K08551.
OrthoDBi EOG7288S1.
TreeFami TF323751.

Miscellaneous databases

NextBioi 284858.
PROi O08537.
SOURCEi Search...

Gene expression databases

Bgeei O08537.
CleanExi MM_ESR2.
ExpressionAtlasi O08537. baseline and differential.
Genevestigatori O08537.

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. 2 hits.
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 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.
    , 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. 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.

Entry informationi

Entry nameiESR2_MOUSE
AccessioniPrimary (citable) accession number: O08537
Secondary accession number(s): B2RUC6
, E9QKX7, O35635, O70519, Q8BG65, Q91Z86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 21, 2012
Last modified: October 29, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3