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Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)

 ESR2_HUMAN              Reviewed;         530 AA.
Q92731; A8K8K5; G3V5M5; O60608; O60685; O60702; O60703; O75583;
O75584; Q0MWT5; Q0MWT6; Q86Z31; Q9UEV6; Q9UHD3; Q9UQK9;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
25-OCT-2017, entry version 205.
RecName: Full=Estrogen receptor beta;
Short=ER-beta;
AltName: Full=Nuclear receptor subfamily 3 group A member 2;
Name=ESR2; Synonyms=ESTRB, NR3A2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9473491; DOI=10.1006/bbrc.1997.7893;
Ogawa S., Inoue S., Watanabe T., Hiroi H., Orimo A., Hosoi T.,
Ouchi Y., Muramatsu M.;
"The complete primary structure of human estrogen receptor beta
(hERbeta) and its heterodimerization with ER alpha in vivo and in
vitro.";
Biochem. Biophys. Res. Commun. 243:122-126(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), NUCLEOTIDE SEQUENCE
[MRNA] OF 409-482 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE [MRNA] OF
409-472 (ISOFORM 6).
TISSUE=Mammary gland, and Testis;
PubMed=9636657; DOI=10.1006/bbrc.1998.8738;
Moore J.T., McKee D.D., Slentz-Kesler K., Moore L.B., Jones S.A.,
Horne E.L., Su J.-L., Kliewer S.A., Lehmann J.M., Willson T.M.;
"Cloning and characterization of human estrogen receptor beta
isoforms.";
Biochem. Biophys. Res. Commun. 247:75-78(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Ovary;
PubMed=9685228; DOI=10.1016/S0303-7207(98)00050-1;
Lu B., Leygue E., Dotzlaw H., Murphy L.J., Murphy L.C., Watson P.H.;
"Estrogen receptor-beta mRNA variants in human and murine tissues.";
Mol. Cell. Endocrinol. 138:199-203(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
TISSUE=Testis;
PubMed=9671811; DOI=10.1093/nar/26.15.3505;
Ogawa S., Inoue S., Watanabe T., Orimo A., Hosoi T., Ouchi Y.,
Muramatsu M.;
"Molecular cloning and characterization of human estrogen receptor
beta cx: a potential inhibitor of estrogen action in human.";
Nucleic Acids Res. 26:3505-3512(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
TISSUE=Prostate;
PubMed=16938840; DOI=10.1073/pnas.0605676103;
Leung Y.K., Mak P., Hassan S., Ho S.M.;
"Estrogen receptor (ER)-beta isoforms: a key to understanding ER-beta
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:13162-13167(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
PubMed=10964723; DOI=10.1006/bbrc.2000.3363;
Li L.C., Yeh C.C., Nojima D., Dahiya R.;
"Cloning and characterization of human estrogen receptor beta
promoter.";
Biochem. Biophys. Res. Commun. 275:682-689(2000).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-530 (ISOFORM 1), AND
CHARACTERIZATION.
TISSUE=Testis;
PubMed=8769313; DOI=10.1016/0014-5793(96)00782-X;
Mosselman S., Polman J., Dijkema R.;
"ER beta: identification and characterization of a novel human
estrogen receptor.";
FEBS Lett. 392:49-53(1996).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-530 (ISOFORMS 7 AND 8).
TISSUE=Endometrium;
Brandenberger A.W., Lebovic D., Taylor R.N., Jaffe R.B.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[14]
INTERACTION WITH NCOA3.
PubMed=9267036; DOI=10.1016/S0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone
acetyltransferase and forms a multimeric activation complex with P/CAF
and CBP/p300.";
Cell 90:569-580(1997).
[15]
CHARACTERIZATION.
PubMed=9325313; DOI=10.1074/jbc.272.41.25832;
Pace P., Taylor J., Suntharalingam S., Coombes R.C., Ali S.;
"Human estrogen receptor beta binds DNA in a manner similar to and
dimerizes with estrogen receptor alpha.";
J. Biol. Chem. 272:25832-25838(1997).
[16]
INTERACTION WITH NCOA6.
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor
coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[17]
INTERACTION WITH NCOA5.
PubMed=11113208; DOI=10.1128/MCB.21.1.343-353.2001;
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F.,
Giguere V.;
"CIA, a novel estrogen receptor coactivator with a bifunctional
nuclear receptor interacting determinant.";
Mol. Cell. Biol. 21:343-353(2001).
[18]
INTERACTION WITH AKAP13.
PubMed=11579095; DOI=10.1074/jbc.M106927200;
Driggers P.H., Segars J.H., Rubino D.M.;
"The proto-oncoprotein Brx activates estrogen receptor beta by a p38
mitogen-activated protein kinase pathway.";
J. Biol. Chem. 276:46792-46797(2001).
[19]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[20]
INTERACTION WITH PELP1.
PubMed=12415108; DOI=10.1073/pnas.192569699;
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic
activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[21]
INTERACTION WITH DNTTIP2.
PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W.,
Rao S.M., Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the
activity of estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[22]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[23]
INTERACTION WITH TXNRD1.
PubMed=15199063; DOI=10.1074/jbc.M402753200;
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
Spyrou G.;
"An alternative splicing variant of the selenoprotein thioredoxin
reductase is a modulator of estrogen signaling.";
J. Biol. Chem. 279:38721-38729(2004).
[24]
PHOSPHORYLATION AT SER-87 AND SER-105, AND MUTAGENESIS OF SER-87 AND
SER-105.
PubMed=15862947; DOI=10.1016/j.jsbmb.2005.02.001;
St-Laurent V., Sanchez M., Charbonneau C., Tremblay A.;
"Selective hormone-dependent repression of estrogen receptor beta by a
p38-activated ErbB2/ErbB3 pathway.";
J. Steroid Biochem. Mol. Biol. 94:23-37(2005).
[25]
INTERACTION WITH CCDC62, AND SUBCELLULAR LOCATION.
PubMed=19126643; DOI=10.1093/carcin/bgn288;
Chen M., Ni J., Chang H.C., Lin C.Y., Muyan M., Yeh S.;
"CCDC62/ERAP75 functions as a coactivator to enhance estrogen receptor
beta-mediated transactivation and target gene expression in prostate
cancer cells.";
Carcinogenesis 30:841-850(2009).
[26]
FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S.,
Yano T., Taketani Y.;
"Repression of estrogen receptor beta function by putative tumor
suppressor DBC1.";
Biochem. Biophys. Res. Commun. 392:357-362(2010).
-!- FUNCTION: 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 (PubMed:20074560). 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.
{ECO:0000269|PubMed:20074560}.
-!- 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 PELP1 and UBE1C. Isoform 2 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 DNAAF4 (By similarity). Interacts with PRMT2.
Interacts with CCAR2 (via N-terminus) in a ligand-independent
manner. {ECO:0000250|UniProtKB:Q62986,
ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:11113208,
ECO:0000269|PubMed:11579095, ECO:0000269|PubMed:12039952,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:15047147,
ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:19126643,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:9267036}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-78505, EBI-78505;
O95273:CCNDBP1; NbExp=3; IntAct=EBI-12259414, EBI-748961;
P03372-1:ESR1; NbExp=5; IntAct=EBI-78505, EBI-15606245;
Q99750:MDFI; NbExp=3; IntAct=EBI-12259414, EBI-724076;
O15162:PLSCR1; NbExp=3; IntAct=EBI-78505, EBI-740019;
P53041:PPP5C; NbExp=4; IntAct=EBI-78505, EBI-716663;
Q12800:TFCP2; NbExp=3; IntAct=EBI-12259414, EBI-717422;
Q16881-4:TXNRD1; NbExp=3; IntAct=EBI-78505, EBI-9080335;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:19126643,
ECO:0000269|PubMed:20074560}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1; Synonyms=Beta-1;
IsoId=Q92731-1; Sequence=Displayed;
Name=2; Synonyms=Beta-2, CX;
IsoId=Q92731-2; Sequence=VSP_003689;
Name=3; Synonyms=Beta-2A;
IsoId=Q92731-3; Sequence=VSP_003684, VSP_003686;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4; Synonyms=Beta-3;
IsoId=Q92731-4; Sequence=VSP_003690;
Name=5; Synonyms=Beta-4;
IsoId=Q92731-5; Sequence=VSP_003691;
Note=Does not form homodimers.;
Name=6; Synonyms=Beta-5;
IsoId=Q92731-6; Sequence=VSP_003692;
Note=Does not form homodimers.;
Name=7; Synonyms=Beta-5A;
IsoId=Q92731-7; Sequence=VSP_003685;
Name=8; Synonyms=Beta-6;
IsoId=Q92731-8; Sequence=VSP_003687, VSP_003688;
Name=9;
IsoId=Q92731-9; Sequence=VSP_055746, VSP_055747;
-!- TISSUE SPECIFICITY: Isoform 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 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 4 is found in
testis. Isoform 5 is expressed in testis, and at a lower level in
spleen, thymus, ovary, mammary gland and uterus. Isoform 6 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.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.
{ECO:0000269|PubMed:15862947}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA67555.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ESR2ID40500ch14q23.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Estrogen receptor entry;
URL="https://en.wikipedia.org/wiki/Estrogen_receptor";
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EMBL; AB006590; BAA24953.1; -; mRNA.
EMBL; AF051427; AAC05985.1; -; mRNA.
EMBL; AF051428; AAC05751.1; -; mRNA.
EMBL; AF061054; AAC39784.1; -; mRNA.
EMBL; AF061055; AAC39785.1; -; mRNA.
EMBL; AF060555; AAC15234.1; -; mRNA.
EMBL; AF124790; AAD32580.1; -; mRNA.
EMBL; AF047463; AAC03786.1; -; mRNA.
EMBL; AB006589; BAA31966.1; -; mRNA.
EMBL; DQ838582; ABH09189.1; -; mRNA.
EMBL; DQ838583; ABH09190.1; -; mRNA.
EMBL; AY785359; AAV31779.1; -; Genomic_DNA.
EMBL; AK292370; BAF85059.1; -; mRNA.
EMBL; AL161756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW80850.1; -; Genomic_DNA.
EMBL; BC024181; AAH24181.1; -; mRNA.
EMBL; AF191544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X99101; CAA67555.1; ALT_INIT; mRNA.
EMBL; AF074598; AAC25602.1; -; mRNA.
EMBL; AF074599; AAC25603.1; -; mRNA.
CCDS; CCDS32096.1; -. [Q92731-2]
CCDS; CCDS55920.1; -. [Q92731-5]
CCDS; CCDS61469.1; -. [Q92731-7]
CCDS; CCDS61470.1; -. [Q92731-9]
CCDS; CCDS9762.1; -. [Q92731-1]
PIR; JC5939; JC5939.
PIR; PW0044; PW0044.
PIR; S71400; S71400.
RefSeq; NP_001035365.1; NM_001040275.1. [Q92731-2]
RefSeq; NP_001201831.1; NM_001214902.1. [Q92731-5]
RefSeq; NP_001258805.1; NM_001271876.1. [Q92731-9]
RefSeq; NP_001258806.1; NM_001271877.1. [Q92731-7]
RefSeq; NP_001278641.1; NM_001291712.1. [Q92731-2]
RefSeq; NP_001278652.1; NM_001291723.1. [Q92731-2]
RefSeq; NP_001428.1; NM_001437.2. [Q92731-1]
RefSeq; XP_016876568.1; XM_017021079.1. [Q92731-1]
RefSeq; XP_016876569.1; XM_017021080.1. [Q92731-1]
RefSeq; XP_016876570.1; XM_017021081.1. [Q92731-1]
RefSeq; XP_016876571.1; XM_017021082.1. [Q92731-1]
RefSeq; XP_016876572.1; XM_017021083.1. [Q92731-1]
RefSeq; XP_016876573.1; XM_017021084.1. [Q92731-2]
UniGene; Hs.660607; -.
UniGene; Hs.734038; -.
UniGene; Hs.734416; -.
PDB; 1L2J; X-ray; 2.95 A; A/B=256-505.
PDB; 1NDE; X-ray; 3.00 A; A=256-501.
PDB; 1QKM; X-ray; 1.80 A; A=255-509.
PDB; 1U3Q; X-ray; 2.40 A; A/B/C/D=261-500.
PDB; 1U3R; X-ray; 2.21 A; A/B=261-501.
PDB; 1U3S; X-ray; 2.50 A; A/B=261-500.
PDB; 1U9E; X-ray; 2.40 A; A/B=261-501.
PDB; 1X76; X-ray; 2.20 A; A/B=261-500.
PDB; 1X78; X-ray; 2.30 A; A/B=261-500.
PDB; 1X7B; X-ray; 2.30 A; A/B=261-500.
PDB; 1X7J; X-ray; 2.30 A; A/B=261-500.
PDB; 1YY4; X-ray; 2.70 A; A/B=263-530.
PDB; 1YYE; X-ray; 2.03 A; A/B=263-530.
PDB; 1ZAF; X-ray; 2.20 A; A/B=263-500.
PDB; 2FSZ; X-ray; 2.20 A; A/B=257-502.
PDB; 2GIU; X-ray; 2.20 A; A=260-500.
PDB; 2I0G; X-ray; 2.50 A; A/B=256-505.
PDB; 2JJ3; X-ray; 2.28 A; A/B=256-505.
PDB; 2NV7; X-ray; 2.10 A; A/B=263-500.
PDB; 2QTU; X-ray; 2.53 A; A/B=256-505.
PDB; 2YJD; X-ray; 1.93 A; A/B=261-500.
PDB; 2YLY; X-ray; 3.20 A; A/B=260-500.
PDB; 2Z4B; X-ray; 2.34 A; A/B=256-505.
PDB; 3OLL; X-ray; 1.50 A; A/B=261-500.
PDB; 3OLS; X-ray; 2.20 A; A/B=261-500.
PDB; 3OMO; X-ray; 2.21 A; A/B=261-500.
PDB; 3OMP; X-ray; 2.05 A; A/B=261-500.
PDB; 3OMQ; X-ray; 1.97 A; A/B=261-500.
PDB; 4J24; X-ray; 2.10 A; A/B/C/D=261-500.
PDB; 4J26; X-ray; 2.30 A; A/B=261-500.
PDB; 4ZI1; X-ray; 2.10 A; A=262-509.
PDB; 5TOA; X-ray; 2.50 A; A/B=262-509.
PDBsum; 1L2J; -.
PDBsum; 1NDE; -.
PDBsum; 1QKM; -.
PDBsum; 1U3Q; -.
PDBsum; 1U3R; -.
PDBsum; 1U3S; -.
PDBsum; 1U9E; -.
PDBsum; 1X76; -.
PDBsum; 1X78; -.
PDBsum; 1X7B; -.
PDBsum; 1X7J; -.
PDBsum; 1YY4; -.
PDBsum; 1YYE; -.
PDBsum; 1ZAF; -.
PDBsum; 2FSZ; -.
PDBsum; 2GIU; -.
PDBsum; 2I0G; -.
PDBsum; 2JJ3; -.
PDBsum; 2NV7; -.
PDBsum; 2QTU; -.
PDBsum; 2YJD; -.
PDBsum; 2YLY; -.
PDBsum; 2Z4B; -.
PDBsum; 3OLL; -.
PDBsum; 3OLS; -.
PDBsum; 3OMO; -.
PDBsum; 3OMP; -.
PDBsum; 3OMQ; -.
PDBsum; 4J24; -.
PDBsum; 4J26; -.
PDBsum; 4ZI1; -.
PDBsum; 5TOA; -.
DisProt; DP00079; -.
ProteinModelPortal; Q92731; -.
SMR; Q92731; -.
BioGrid; 108404; 100.
CORUM; Q92731; -.
DIP; DIP-5966N; -.
ELM; Q92731; -.
IntAct; Q92731; 431.
STRING; 9606.ENSP00000343925; -.
BindingDB; Q92731; -.
ChEMBL; CHEMBL242; -.
DrugBank; DB07119; 1-CHLORO-6-(4-HYDROXYPHENYL)-2-NAPHTHOL.
DrugBank; DB07032; 2-(4-HYDROXY-PHENYL)BENZOFURAN-5-OL.
DrugBank; DB06875; 3-(3-FLUORO-4-HYDROXYPHENYL)-7-HYDROXY-1-NAPHTHONITRILE.
DrugBank; DB07236; 3-(6-HYDROXY-NAPHTHALEN-2-YL)-BENZO[D]ISOOXAZOL-6-OL.
DrugBank; DB07230; 3-BROMO-6-HYDROXY-2-(4-HYDROXYPHENYL)-1H-INDEN-1-ONE.
DrugBank; DB07150; 4-(4-HYDROXYPHENYL)-1-NAPHTHALDEHYDE OXIME.
DrugBank; DB07198; 5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-CARBONITRILE.
DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DrugBank; DB04468; Afimoxifene.
DrugBank; DB05882; CHF 4227.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00783; Estradiol.
DrugBank; DB01196; Estramustine.
DrugBank; DB04573; Estriol.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB01645; Genistein.
DrugBank; DB06202; Lasofoxifene.
DrugBank; DB05052; MF101.
DrugBank; DB02983; Para-Mercury-Benzenesulfonic Acid.
DrugBank; DB01708; Prasterone.
DrugBank; DB00481; Raloxifene.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB01108; Trilostane.
GuidetoPHARMACOLOGY; 621; -.
iPTMnet; Q92731; -.
PhosphoSitePlus; Q92731; -.
SwissPalm; Q92731; -.
BioMuta; ESR2; -.
DMDM; 6166154; -.
PaxDb; Q92731; -.
PeptideAtlas; Q92731; -.
PRIDE; Q92731; -.
Ensembl; ENST00000267525; ENSP00000267525; ENSG00000140009. [Q92731-7]
Ensembl; ENST00000341099; ENSP00000343925; ENSG00000140009. [Q92731-1]
Ensembl; ENST00000344288; ENSP00000345616; ENSG00000140009. [Q92731-3]
Ensembl; ENST00000353772; ENSP00000335551; ENSG00000140009. [Q92731-2]
Ensembl; ENST00000358599; ENSP00000351412; ENSG00000140009. [Q92731-2]
Ensembl; ENST00000553796; ENSP00000452426; ENSG00000140009. [Q92731-9]
Ensembl; ENST00000554572; ENSP00000450699; ENSG00000140009. [Q92731-2]
Ensembl; ENST00000555278; ENSP00000450488; ENSG00000140009. [Q92731-5]
Ensembl; ENST00000557772; ENSP00000451582; ENSG00000140009. [Q92731-6]
GeneID; 2100; -.
KEGG; hsa:2100; -.
UCSC; uc001xgu.4; human. [Q92731-1]
CTD; 2100; -.
DisGeNET; 2100; -.
EuPathDB; HostDB:ENSG00000140009.18; -.
GeneCards; ESR2; -.
HGNC; HGNC:3468; ESR2.
HPA; CAB022544; -.
MalaCards; ESR2; -.
MIM; 601663; gene.
neXtProt; NX_Q92731; -.
OpenTargets; ENSG00000140009; -.
PharmGKB; PA27886; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOVERGEN; HBG108344; -.
InParanoid; Q92731; -.
KO; K08551; -.
OMA; VKCGSRR; -.
OrthoDB; EOG091G03V4; -.
PhylomeDB; Q92731; -.
TreeFam; TF323751; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; Q92731; -.
SIGNOR; Q92731; -.
EvolutionaryTrace; Q92731; -.
GeneWiki; Estrogen_receptor_beta; -.
GenomeRNAi; 2100; -.
PMAP-CutDB; A8K8K5; -.
PRO; PR:Q92731; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000140009; -.
ExpressionAtlas; Q92731; baseline and differential.
Genevisible; Q92731; HS.
GO; GO:0005576; C:extracellular region; IEA:GOC.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030284; F:estrogen receptor activity; IDA:CAFA.
GO; GO:0034056; F:estrogen response element binding; IDA:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0048019; F:receptor antagonist activity; NAS:UniProtKB.
GO; GO:0038052; F:RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; NAS:UniProtKB.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:CAFA.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:CAFA.
GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR028355; ER-beta/gamma.
InterPro; IPR021064; Estrogen_rcpt_beta_N.
InterPro; IPR035500; NHR_like_domain.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF12497; ERbeta_N; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF500102; ER-b; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Lipid-binding; Metal-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 530 Estrogen receptor beta.
/FTId=PRO_0000053642.
DNA_BIND 149 214 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 149 169 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 185 209 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 148 Modulating.
REGION 215 530 Steroid-binding.
MOD_RES 87 87 Phosphoserine.
{ECO:0000269|PubMed:15862947}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000269|PubMed:15862947}.
VAR_SEQ 319 409 Missing (in isoform 7).
{ECO:0000303|Ref.13}.
/FTId=VSP_003685.
VAR_SEQ 319 323 FVELS -> MRGNA (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9685228}.
/FTId=VSP_003684.
VAR_SEQ 324 530 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9685228}.
/FTId=VSP_003686.
VAR_SEQ 365 375 DEGKCVEGILE -> YVPSGHSDPGC (in isoform
8). {ECO:0000303|Ref.13}.
/FTId=VSP_003687.
VAR_SEQ 376 530 Missing (in isoform 8).
{ECO:0000303|Ref.13}.
/FTId=VSP_003688.
VAR_SEQ 469 530 SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITG
SECSPAEDSKSKEGSQNPQSQ -> RAEKASQTLTSFGMKM
ETLLPEATMEQ (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9636657,
ECO:0000303|PubMed:9671811}.
/FTId=VSP_003689.
VAR_SEQ 469 530 SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITG
SECSPAEDSKSKEGSQNPQSQ -> SSLSLSWRLFMLREAS
CHGVRQTPGGAHMSVSRSRSFEACQQPRE (in isoform
4). {ECO:0000303|PubMed:9636657}.
/FTId=VSP_003690.
VAR_SEQ 469 530 SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITG
SECSPAEDSKSKEGSQNPQSQ -> RWGEKQFIHLKLS
(in isoform 5).
{ECO:0000303|PubMed:16938840,
ECO:0000303|PubMed:9636657}.
/FTId=VSP_003691.
VAR_SEQ 469 530 SNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITG
SECSPAEDSKSKEGSQNPQSQ -> RYAP (in isoform
6). {ECO:0000303|PubMed:16938840,
ECO:0000303|PubMed:9636657}.
/FTId=VSP_003692.
VAR_SEQ 469 474 SNKGME -> RSCVYK (in isoform 9).
{ECO:0000305}.
/FTId=VSP_055746.
VAR_SEQ 475 530 Missing (in isoform 9). {ECO:0000305}.
/FTId=VSP_055747.
MUTAGEN 87 87 S->A: Enhances repression by activated
ErbB2/ErbB3; when associated with A-105.
{ECO:0000269|PubMed:15862947}.
MUTAGEN 87 87 S->D: Abolishes repression by activated
ErbB2/ErbB3; when associated with D-105.
{ECO:0000269|PubMed:15862947}.
MUTAGEN 105 105 S->A: Enhances repression by activated
ErbB2/ErbB3; when associated with A-87.
{ECO:0000269|PubMed:15862947}.
MUTAGEN 105 105 S->D: Abolishes repression by activated
ErbB2/ErbB3; when associated with D-87.
{ECO:0000269|PubMed:15862947}.
HELIX 257 260 {ECO:0000244|PDB:1L2J}.
HELIX 261 263 {ECO:0000244|PDB:2FSZ}.
HELIX 265 275 {ECO:0000244|PDB:3OLL}.
STRAND 286 288 {ECO:0000244|PDB:2FSZ}.
HELIX 291 314 {ECO:0000244|PDB:3OLL}.
HELIX 319 321 {ECO:0000244|PDB:3OLL}.
HELIX 324 347 {ECO:0000244|PDB:3OLL}.
STRAND 348 350 {ECO:0000244|PDB:1L2J}.
STRAND 353 357 {ECO:0000244|PDB:3OLL}.
STRAND 359 363 {ECO:0000244|PDB:3OLL}.
HELIX 364 369 {ECO:0000244|PDB:3OLL}.
HELIX 373 389 {ECO:0000244|PDB:3OLL}.
HELIX 394 406 {ECO:0000244|PDB:3OLL}.
STRAND 407 409 {ECO:0000244|PDB:1NDE}.
HELIX 411 413 {ECO:0000244|PDB:1QKM}.
HELIX 417 419 {ECO:0000244|PDB:1L2J}.
HELIX 421 442 {ECO:0000244|PDB:3OLL}.
TURN 443 445 {ECO:0000244|PDB:1U3Q}.
HELIX 448 481 {ECO:0000244|PDB:3OLL}.
STRAND 482 484 {ECO:0000244|PDB:1L2J}.
HELIX 489 497 {ECO:0000244|PDB:3OLL}.
HELIX 498 501 {ECO:0000244|PDB:4ZI1}.
SEQUENCE 530 AA; 59216 MW; 8CAE34215992418A CRC64;
MDIKNSPSSL NSPSSYNCSQ SILPLEHGSI YIPSSYVDSH HEYPAMTFYS PAVMNYSIPS
NVTNLEGGPG RQTTSPNVLW PTPGHLSPLV VHRQLSHLYA EPQKSPWCEA RSLEHTLPVN
RETLKRKVSG NRCASPVTGP GSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQRSADEQLH
CAGKAKRSGG HAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFT EASMMMSLTK
LADKELVHMI SWAKKIPGFV ELSLFDQVRL LESCWMEVLM MGLMWRSIDH PGKLIFAPDL
VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLVTATQDA
DSSRKLAHLL NAVTDALVWV IAKSGISSQQ QSMRLANLLM LLSHVRHASN KGMEHLLNMK
CKNVVPVYDL LLEMLNAHVL RGCKSSITGS ECSPAEDSKS KEGSQNPQSQ


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