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Estrogen-related receptor gamma (ERR gamma-2) (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3)

 ERR3_HUMAN              Reviewed;         458 AA.
P62508; A8K4I0; A8K6I2; B3KY84; E9PGB7; F8W8J3; O75454; O96021;
Q68DA0; Q6P274; Q6PK28; Q6TS38; Q9R1F3; Q9UNJ4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
23-MAY-2018, entry version 165.
RecName: Full=Estrogen-related receptor gamma;
AltName: Full=ERR gamma-2;
AltName: Full=Estrogen receptor-related protein 3;
AltName: Full=Nuclear receptor subfamily 3 group B member 3;
Name=ESRRG; Synonyms=ERR3, ERRG2, KIAA0832, NR3B3;
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).
TISSUE=Brain;
PubMed=10072763; DOI=10.1016/S0378-1119(98)00619-2;
Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C.,
Liu Q., Caskey C.T.;
"Identification of two hERR2-related novel nuclear receptors utilizing
bioinformatics and inverse PCR.";
Gene 228:101-109(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=9676434; DOI=10.1006/geno.1998.5345;
Eudy J.D., Yao S.F., Weston M.D., Ma-Edmonds M., Talmadge C.B.,
Cheng J.J., Kimberling W.J., Sumegi J.;
"Isolation of a gene encoding a novel member of the nuclear receptor
superfamily from the critical region of Usher syndrome type IIa at
1q41.";
Genomics 50:382-384(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, Retina, and Skeletal muscle;
PubMed=10707956; DOI=10.1210/mend.14.3.0431;
Heard D.J., Norby P.L., Holloway J., Vissing H.;
"Human ERRgamma, a third member of the estrogen receptor-related
receptor (ERR) subfamily of orphan nuclear receptors: tissue-specific
isoforms are expressed during development and in the adult.";
Mol. Endocrinol. 14:382-392(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Brain, and Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-50.
NIEHS SNPs program;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Eye, and Placenta;
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 [MRNA] OF 1-129 (ISOFORM 1).
TISSUE=Brain;
PubMed=10428842; DOI=10.1074/jbc.274.32.22618;
Hong H., Yang L., Stallcup M.R.;
"Hormone-independent transcriptional activation and coactivator
binding by novel orphan nuclear receptor ERR3.";
J. Biol. Chem. 274:22618-22626(1999).
[12]
INTERACTION WITH TLE1 AND PNRC2, AND TISSUE SPECIFICITY.
PubMed=14651967; DOI=10.1016/j.bbrc.2003.11.025;
Hentschke M., Borgmeyer U.;
"Identification of PNRC2 and TLE1 as activation function-1 cofactors
of the orphan nuclear receptor ERRgamma.";
Biochem. Biophys. Res. Commun. 312:975-982(2003).
[13]
SUMOYLATION AT LYS-40, AND MUTAGENESIS OF LYS-40.
PubMed=16371476; DOI=10.1073/pnas.0503698102;
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,
Nakai A., Sistonen L.;
"PDSM, a motif for phosphorylation-dependent SUMO modification.";
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
[14]
SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, AND
MUTAGENESIS OF PHE-38; ILE-39; LYS-40; THR-41; GLU-42; SER-44 AND
SER-45.
PubMed=19067653; DOI=10.1042/BJ20081556;
Hentschke M., Suesens U., Borgmeyer U.;
"Transcriptional ERRgamma2-mediated activation is regulated by
sentrin-specific proteases.";
Biochem. J. 419:167-176(2009).
[15]
SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, AND
MUTAGENESIS OF LYS-40 AND SER-45.
PubMed=18063693; DOI=10.1210/me.2007-0357;
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
"Phosphorylation-dependent sumoylation regulates estrogen-related
receptor-alpha and -gamma transcriptional activity through a synergy
control motif.";
Mol. Endocrinol. 22:570-584(2008).
[16]
ACETYLATION BY PCAF/KAT2B.
PubMed=20484414; DOI=10.1210/me.2009-0441;
Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.;
"An acetylation switch modulates the transcriptional activity of
estrogen-related receptor alpha.";
Mol. Endocrinol. 24:1349-1358(2010).
[17]
FUNCTION.
PubMed=23836911; DOI=10.1074/jbc.M113.489674;
Cho Y., Hazen B.C., Russell A.P., Kralli A.;
"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
(Perm1) is a tissue-specific regulator of oxidative capacity in
skeletal muscle cells.";
J. Biol. Chem. 288:25207-25218(2013).
[18]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 229-458 IN COMPLEXES WITH
INVERSE AGONISTS AND NCOA1, FUNCTION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11864604; DOI=10.1016/S1097-2765(02)00444-6;
Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A.,
Moras D., Renaud J.-P.;
"Structural and functional evidence for ligand-independent
transcriptional activation by the estrogen-related receptor 3.";
Mol. Cell 9:303-313(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 233-458 IN COMPLEX WITH
INVERSE AGONIST.
PubMed=16307879; DOI=10.1016/j.bmcl.2005.11.030;
Chao E.Y.H., Collins J.L., Gaillard S., Miller A.B., Wang L.,
Orband-Miller L.A., Nolte R.T., McDonnell D.P., Willson T.M.,
Zuercher W.J.;
"Structure-guided synthesis of tamoxifen analogs with improved
selectivity for the orphan ERRgamma.";
Bioorg. Med. Chem. Lett. 16:821-824(2006).
[20]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 229-458 IN COMPLEXES WITH
AGONIST AND INVERSE AGONIST; NRIP1 AND NCOR2, AND SUBUNIT.
PubMed=16990259; DOI=10.1074/jbc.M608410200;
Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B.,
Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.;
"X-ray crystal structures of the estrogen-related receptor-gamma
ligand binding domain in three functional states reveal the molecular
basis of small molecule regulation.";
J. Biol. Chem. 281:37773-37781(2006).
-!- FUNCTION: Orphan receptor that acts as transcription activator in
the absence of bound ligand. Binds specifically to an estrogen
response element and activates reporter genes controlled by
estrogen response elements (By similarity). Induces the expression
of PERM1 in the skeletal muscle. {ECO:0000250,
ECO:0000269|PubMed:11864604, ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:19067653, ECO:0000269|PubMed:23836911}.
-!- SUBUNIT: Homodimer. Binds TLE1, PNRC1 and PNRC2. Binds GRIP1 (By
similarity). Interacts with NRIP1, NCOA1 and NCOR2. {ECO:0000250,
ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:16307879,
ECO:0000269|PubMed:16990259}.
-!- INTERACTION:
G2XKQ0:-; NbExp=3; IntAct=EBI-2834260, EBI-10175576;
Q05D60:DEUP1; NbExp=3; IntAct=EBI-2834260, EBI-748597;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-2834260, EBI-2125614;
P50222:MEOX2; NbExp=3; IntAct=EBI-2834260, EBI-748397;
Q6IN84:MRM1; NbExp=4; IntAct=EBI-12001340, EBI-5454865;
P51843:NR0B1; NbExp=3; IntAct=EBI-2834260, EBI-946109;
Q12769:NUP160; NbExp=3; IntAct=EBI-2834260, EBI-295715;
Q9UBK2:PPARGC1A; NbExp=3; IntAct=EBI-2834260, EBI-765486;
A0MZ66:SHTN1; NbExp=3; IntAct=EBI-2834260, EBI-308778;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Long;
IsoId=P62508-1, O75454-1;
Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P62508-2, O75454-2;
Sequence=VSP_003702;
Name=3;
IsoId=P62508-3; Sequence=VSP_003702, VSP_013301;
Name=4;
IsoId=P62508-4; Sequence=VSP_003702, VSP_045980;
Note=No experimental confirmation available.;
Name=5;
IsoId=P62508-5; Sequence=VSP_047156, VSP_013301;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in the heart, kidney, brain, lung,
bone marrow, adrenal gland, trachea, spinal cord and thyroid
gland. {ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:9676434}.
-!- DEVELOPMENTAL STAGE: Expressed at high levels in fetal brain and
also in the fetal kidney, lung and liver.
{ECO:0000269|PubMed:9676434}.
-!- PTM: Acetylated by PCAF/KAT2 (in vitro).
{ECO:0000269|PubMed:20484414}.
-!- PTM: Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-
45 and represses transcriptional activity.
{ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:19067653}.
-!- PTM: Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus
repressing transcriptional activity. {ECO:0000269|PubMed:16371476,
ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:19067653}.
-!- MISCELLANEOUS: No physiological activating ligand is known for
this orphan receptor, but 4-hydroxytamoxifen and
diethylstilbestrol act as inverse agonists and deactivate ESRRG.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH08218.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA74855.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/esrrg/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ESRRGID45840ch1q41.html";
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EMBL; AF094518; AAC99410.1; -; mRNA.
EMBL; AB020639; BAA74855.2; ALT_INIT; mRNA.
EMBL; AF058291; AAC39899.1; -; mRNA.
EMBL; AY388456; AAQ93376.1; -; mRNA.
EMBL; AY388457; AAQ93377.1; -; mRNA.
EMBL; AY388458; AAQ93378.1; -; mRNA.
EMBL; AY388459; AAQ93379.1; -; mRNA.
EMBL; AY388460; AAQ93380.1; -; mRNA.
EMBL; AY388461; AAQ93381.1; -; mRNA.
EMBL; AK131193; BAG54746.1; -; mRNA.
EMBL; AK290945; BAF83634.1; -; mRNA.
EMBL; AK291028; BAF83717.1; -; mRNA.
EMBL; AK291647; BAF84336.1; -; mRNA.
EMBL; CR749497; CAH18320.1; -; mRNA.
EMBL; AY528719; AAS00098.1; -; Genomic_DNA.
EMBL; AC096635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL603752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93335.1; -; Genomic_DNA.
EMBL; BC008218; AAH08218.1; ALT_SEQ; mRNA.
EMBL; BC064700; AAH64700.1; -; mRNA.
EMBL; AF117255; AAD48370.1; -; mRNA.
CCDS; CCDS1517.1; -. [P62508-2]
CCDS; CCDS41468.1; -.
CCDS; CCDS58060.1; -. [P62508-4]
CCDS; CCDS58061.1; -. [P62508-5]
RefSeq; NP_001127757.1; NM_001134285.2. [P62508-2]
RefSeq; NP_001230434.1; NM_001243505.1.
RefSeq; NP_001230435.1; NM_001243506.1.
RefSeq; NP_001230436.1; NM_001243507.1. [P62508-4]
RefSeq; NP_001230438.1; NM_001243509.1. [P62508-2]
RefSeq; NP_001230439.1; NM_001243510.2. [P62508-2]
RefSeq; NP_001230440.1; NM_001243511.2. [P62508-2]
RefSeq; NP_001230441.1; NM_001243512.1. [P62508-2]
RefSeq; NP_001230442.1; NM_001243513.1. [P62508-2]
RefSeq; NP_001230443.1; NM_001243514.1. [P62508-2]
RefSeq; NP_001230444.1; NM_001243515.1. [P62508-2]
RefSeq; NP_001230447.1; NM_001243518.1. [P62508-5]
RefSeq; NP_001230448.1; NM_001243519.1. [P62508-2]
RefSeq; NP_001429.2; NM_001438.3. [P62508-1]
RefSeq; NP_996317.1; NM_206594.2. [P62508-2]
RefSeq; NP_996318.1; NM_206595.2. [P62508-2]
RefSeq; XP_011507569.1; XM_011509267.1. [P62508-5]
RefSeq; XP_011507570.1; XM_011509268.2. [P62508-5]
RefSeq; XP_011507571.1; XM_011509269.2. [P62508-5]
RefSeq; XP_011507576.1; XM_011509274.1. [P62508-3]
RefSeq; XP_011507577.1; XM_011509275.1. [P62508-3]
RefSeq; XP_011507578.1; XM_011509276.1. [P62508-3]
RefSeq; XP_011507579.1; XM_011509277.1. [P62508-3]
RefSeq; XP_011507580.1; XM_011509278.1. [P62508-3]
RefSeq; XP_011507581.1; XM_011509279.1. [P62508-3]
RefSeq; XP_011507582.1; XM_011509280.2. [P62508-3]
RefSeq; XP_016856120.1; XM_017000631.1. [P62508-3]
RefSeq; XP_016856121.1; XM_017000632.1. [P62508-3]
RefSeq; XP_016856122.1; XM_017000633.1. [P62508-3]
RefSeq; XP_016856123.1; XM_017000634.1. [P62508-3]
RefSeq; XP_016856124.1; XM_017000635.1. [P62508-3]
RefSeq; XP_016856125.1; XM_017000636.1. [P62508-3]
RefSeq; XP_016856126.1; XM_017000637.1. [P62508-3]
RefSeq; XP_016856127.1; XM_017000638.1. [P62508-2]
RefSeq; XP_016856128.1; XM_017000639.1. [P62508-2]
RefSeq; XP_016856129.1; XM_017000640.1. [P62508-2]
RefSeq; XP_016856130.1; XM_017000641.1. [P62508-2]
RefSeq; XP_016856131.1; XM_017000642.1.
RefSeq; XP_016856132.1; XM_017000643.1.
RefSeq; XP_016856133.1; XM_017000644.1. [P62508-2]
RefSeq; XP_016856134.1; XM_017000645.1. [P62508-2]
RefSeq; XP_016856135.1; XM_017000646.1.
RefSeq; XP_016856136.1; XM_017000647.1. [P62508-2]
RefSeq; XP_016856137.1; XM_017000648.1. [P62508-2]
RefSeq; XP_016856138.1; XM_017000649.1.
UniGene; Hs.444225; -.
UniGene; Hs.738938; -.
PDB; 1KV6; X-ray; 2.70 A; A/B=229-458.
PDB; 1TFC; X-ray; 2.40 A; A/B=229-458.
PDB; 1VJB; X-ray; 3.20 A; A/B=229-458.
PDB; 2E2R; X-ray; 1.60 A; A=222-458.
PDB; 2EWP; X-ray; 2.30 A; A/B/C/D/E=233-458.
PDB; 2GP7; X-ray; 2.45 A; A/B/C/D=229-458.
PDB; 2GPO; X-ray; 1.95 A; A=229-458.
PDB; 2GPP; X-ray; 2.60 A; A/B=229-458.
PDB; 2GPU; X-ray; 1.70 A; A=229-458.
PDB; 2GPV; X-ray; 2.85 A; A/B/C/D/E/F=229-458.
PDB; 2P7A; X-ray; 2.30 A; A=229-458.
PDB; 2P7G; X-ray; 2.10 A; A=229-458.
PDB; 2P7Z; X-ray; 2.50 A; A=229-458.
PDB; 2ZAS; X-ray; 2.00 A; A=222-458.
PDB; 2ZBS; X-ray; 1.80 A; A=222-458.
PDB; 2ZKC; X-ray; 1.70 A; A=222-458.
PDBsum; 1KV6; -.
PDBsum; 1TFC; -.
PDBsum; 1VJB; -.
PDBsum; 2E2R; -.
PDBsum; 2EWP; -.
PDBsum; 2GP7; -.
PDBsum; 2GPO; -.
PDBsum; 2GPP; -.
PDBsum; 2GPU; -.
PDBsum; 2GPV; -.
PDBsum; 2P7A; -.
PDBsum; 2P7G; -.
PDBsum; 2P7Z; -.
PDBsum; 2ZAS; -.
PDBsum; 2ZBS; -.
PDBsum; 2ZKC; -.
ProteinModelPortal; P62508; -.
SMR; P62508; -.
BioGrid; 108407; 28.
IntAct; P62508; 33.
MINT; P62508; -.
STRING; 9606.ENSP00000386171; -.
BindingDB; P62508; -.
ChEMBL; CHEMBL4245; -.
DrugBank; DB06902; 4-(1-methyl-1-phenylethyl)phenol.
DrugBank; DB06884; 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE.
DrugBank; DB04468; Afimoxifene.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00197; Troglitazone.
GuidetoPHARMACOLOGY; 624; -.
iPTMnet; P62508; -.
PhosphoSitePlus; P62508; -.
BioMuta; ESRRG; -.
DMDM; 50402102; -.
MaxQB; P62508; -.
PaxDb; P62508; -.
PeptideAtlas; P62508; -.
PRIDE; P62508; -.
DNASU; 2104; -.
Ensembl; ENST00000359162; ENSP00000352077; ENSG00000196482. [P62508-2]
Ensembl; ENST00000360012; ENSP00000353108; ENSG00000196482. [P62508-2]
Ensembl; ENST00000361395; ENSP00000354584; ENSG00000196482. [P62508-2]
Ensembl; ENST00000361525; ENSP00000355225; ENSG00000196482. [P62508-2]
Ensembl; ENST00000366937; ENSP00000355904; ENSG00000196482. [P62508-5]
Ensembl; ENST00000366938; ENSP00000355905; ENSG00000196482. [P62508-2]
Ensembl; ENST00000366940; ENSP00000355907; ENSG00000196482. [P62508-2]
Ensembl; ENST00000391890; ENSP00000375761; ENSG00000196482. [P62508-2]
Ensembl; ENST00000408911; ENSP00000386171; ENSG00000196482. [P62508-1]
Ensembl; ENST00000463665; ENSP00000418629; ENSG00000196482. [P62508-4]
Ensembl; ENST00000487276; ENSP00000419155; ENSG00000196482. [P62508-2]
Ensembl; ENST00000493603; ENSP00000419594; ENSG00000196482. [P62508-2]
Ensembl; ENST00000493748; ENSP00000417374; ENSG00000196482. [P62508-2]
Ensembl; ENST00000616180; ENSP00000481528; ENSG00000196482. [P62508-2]
GeneID; 2104; -.
KEGG; hsa:2104; -.
UCSC; uc001hkw.3; human.
CTD; 2104; -.
DisGeNET; 2104; -.
EuPathDB; HostDB:ENSG00000196482.16; -.
GeneCards; ESRRG; -.
HGNC; HGNC:3474; ESRRG.
HPA; HPA044678; -.
MIM; 602969; gene.
neXtProt; NX_P62508; -.
OpenTargets; ENSG00000196482; -.
PharmGKB; PA27891; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOGENOM; HOG000233467; -.
HOVERGEN; HBG108344; -.
InParanoid; P62508; -.
KO; K08554; -.
OMA; PRLLCRM; -.
OrthoDB; EOG091G0DYP; -.
PhylomeDB; P62508; -.
TreeFam; TF323751; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P62508; -.
SIGNOR; P62508; -.
ChiTaRS; ESRRG; human.
EvolutionaryTrace; P62508; -.
GeneWiki; Estrogen-related_receptor_gamma; -.
GenomeRNAi; 2104; -.
PRO; PR:P62508; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000196482; -.
ExpressionAtlas; P62508; baseline and differential.
Genevisible; P62508; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0050682; F:AF-2 domain binding; ISS:UniProtKB.
GO; GO:0003708; F:retinoic acid receptor activity; IEA:InterPro.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0005496; F:steroid binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR027289; Oest-rel_rcp.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR003078; Retinoic_acid_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PIRSF; PIRSF500939; ERR1-2-3; 1.
PRINTS; PR01292; RETNOICACIDR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 458 Estrogen-related receptor gamma.
/FTId=PRO_0000053665.
DOMAIN 233 457 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 125 200 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 128 148 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 164 188 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000305|PubMed:18063693,
ECO:0000305|PubMed:19067653}.
CROSSLNK 40 40 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
VAR_SEQ 1 23 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10707956,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9676434}.
/FTId=VSP_003702.
VAR_SEQ 1 19 MDSVELCLPESFSLHYEEE -> MWRECDWGLGAVKSDLAC
VPSAKR (in isoform 5). {ECO:0000305}.
/FTId=VSP_047156.
VAR_SEQ 158 196 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045980.
VAR_SEQ 234 234 Y -> LLWSDPAD (in isoform 3 and isoform
5). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_013301.
VARIANT 50 50 T -> M (in dbSNP:rs11572693).
{ECO:0000269|Ref.7}.
/FTId=VAR_019229.
MUTAGEN 38 38 F->A,E: No effect on transcriptional
activity. {ECO:0000269|PubMed:19067653}.
MUTAGEN 39 39 I->A: 4-fold increase in transcriptional
activity. {ECO:0000269|PubMed:19067653}.
MUTAGEN 40 40 K->R: Abolishes sumoylation. 7-fold
increase in transcriptional activity.
{ECO:0000269|PubMed:16371476,
ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:19067653}.
MUTAGEN 41 41 T->A: No effect on transcriptional
activity. {ECO:0000269|PubMed:19067653}.
MUTAGEN 42 42 E->A: 4-fold increase in transcriptional
activity. {ECO:0000269|PubMed:19067653}.
MUTAGEN 44 44 S->A,E: No effect on transcriptional
activity. {ECO:0000269|PubMed:19067653}.
MUTAGEN 45 45 S->A: Abolishes sumoylation. Increased
transcriptional activity.
{ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:19067653}.
MUTAGEN 45 45 S->D: No change in sumoylation nor
transcriptional activity.
{ECO:0000269|PubMed:18063693,
ECO:0000269|PubMed:19067653}.
CONFLICT 19 19 E -> K (in Ref. 4; AAQ93376).
{ECO:0000305}.
CONFLICT 151 151 F -> S (in Ref. 3; AAC39899).
{ECO:0000305}.
CONFLICT 155 155 T -> K (in Ref. 3; AAC39899).
{ECO:0000305}.
CONFLICT 158 158 G -> A (in Ref. 3; AAC39899).
{ECO:0000305}.
CONFLICT 227 227 V -> A (in Ref. 5; BAG54746).
{ECO:0000305}.
CONFLICT 271 271 L -> C (in Ref. 3; AAC39899).
{ECO:0000305}.
CONFLICT 313 313 V -> F (in Ref. 3; AAC39899).
{ECO:0000305}.
CONFLICT 449 449 L -> P (in Ref. 5; CAH18320).
{ECO:0000305}.
CONFLICT 458 458 V -> VC (in Ref. 3; AAC39899).
{ECO:0000305}.
HELIX 236 243 {ECO:0000244|PDB:2E2R}.
STRAND 255 257 {ECO:0000244|PDB:1TFC}.
HELIX 261 283 {ECO:0000244|PDB:2E2R}.
HELIX 289 291 {ECO:0000244|PDB:2E2R}.
HELIX 294 316 {ECO:0000244|PDB:2E2R}.
TURN 317 319 {ECO:0000244|PDB:2E2R}.
STRAND 320 322 {ECO:0000244|PDB:2E2R}.
STRAND 324 327 {ECO:0000244|PDB:2E2R}.
STRAND 330 332 {ECO:0000244|PDB:2E2R}.
HELIX 334 339 {ECO:0000244|PDB:2E2R}.
HELIX 343 359 {ECO:0000244|PDB:2E2R}.
HELIX 363 375 {ECO:0000244|PDB:2E2R}.
HELIX 385 406 {ECO:0000244|PDB:2E2R}.
HELIX 413 418 {ECO:0000244|PDB:2E2R}.
HELIX 421 441 {ECO:0000244|PDB:2E2R}.
HELIX 448 454 {ECO:0000244|PDB:2E2R}.
SEQUENCE 458 AA; 51306 MW; 63D36CFD37573152 CRC64;
MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT DSVNHHSPGG
SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL YDDCSSTIVE DPQTKCEYML
NSMPKRLCLV CGDIASGYHY GVASCEACKA FFKRTIQGNI EYSCPATNEC EITKRRRKSC
QACRFMKCLK VGMLKEGVRL DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH
LLVAEPEKIY AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL
LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL QLVKKYKSMK
LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ DYEAGQHMED PRRAGKMLMT
LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF LEMLEAKV


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