Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)

 GCR_RAT                 Reviewed;         795 AA.
P06536; O08624; Q8R463; Q8R5J0;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
22-NOV-2017, entry version 205.
RecName: Full=Glucocorticoid receptor;
Short=GR;
AltName: Full=Nuclear receptor subfamily 3 group C member 1;
Name=Nr3c1; Synonyms=Grl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
PubMed=3755378; DOI=10.1016/0092-8674(86)90659-8;
Miesfeld R., Rusconi S., Godowski P.J., Maler B.A., Okret S.,
Wikstroem A.-C., Gustafsson J.-A., Yamamoto K.R.;
"Genetic complementation of a glucocorticoid receptor deficiency by
expression of cloned receptor cDNA.";
Cell 46:389-399(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Heeley R.P., Gill E., van Zutphen B.;
"CAG repeat variation in the gene for rat glucocorticoid receptor: a
study of allele frequencies in inbred and wild rat populations and of
the steroid-binding properties of their polypeptides in vitro.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-226 AND ASP-260.
STRAIN=Brown Norway/Crl, and SHR/OlaIpcv;
Pravenec M., Zidek V., Kostka V., Mlejnek P., Musilova A., Kren V.,
Jansa P., Forejt J., Lezin E.S., Kurtz T.W.;
"Genetic isolation of a QTL on chromosome 18 associated with salt
sensitivity in spontaneously hypertensive rats.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-515.
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=3684608; DOI=10.1093/nar/15.22.9603;
Chang C., Kokontis J., Chang C.T., Liao S.;
"Cloning and sequence analysis of the rat ventral prostate
glucocorticoid receptor cDNA.";
Nucleic Acids Res. 15:9603-9603(1987).
[5]
MUTAGENESIS OF ZINC-FINGER.
PubMed=3191912;
Severne Y., Wieland S., Schaffner W., Rusconi S.;
"Metal binding 'finger' structures in the glucocorticoid receptor
defined by site-directed mutagenesis.";
EMBO J. 7:2503-2508(1988).
[6]
GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
PubMed=3216865; DOI=10.1210/mend-2-12-1256;
Dong Y., Poellinger L., Gustafsson J.-A., Okret S.;
"Regulation of glucocorticoid receptor expression: evidence for
transcriptional and posttranslational mechanisms.";
Mol. Endocrinol. 2:1256-1264(1988).
[7]
MUTAGENESIS OF CYS-656.
PubMed=1939229;
Chakraborti P.K., Garabedian M.J., Yamamoto K.R., Simons S.S. Jr.;
"Creation of 'super' glucocorticoid receptors by point mutations in
the steroid binding domain.";
J. Biol. Chem. 266:22075-22078(1991).
[8]
MUTAGENESIS OF ZINC-FINGER.
PubMed=8450530; DOI=10.1006/jmbi.1993.1130;
Zandi E., Galli I., Doebbeling U., Rusconi S.;
"Zinc finger mutations that alter domain interactions in the
glucocorticoid receptor.";
J. Mol. Biol. 230:124-136(1993).
[9]
REVIEW ON MUTAGENESIS.
PubMed=8191545; DOI=10.1016/0039-128X(94)90093-0;
Lanz R.B., Hug M., Gola M., Tallone T., Wieland S., Rusconi S.;
"Active, interactive, and inactive steroid receptor mutants.";
Steroids 59:148-152(1994).
[10]
HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, AND MUTAGENESIS OF
ASP-481.
PubMed=8618925; DOI=10.1073/pnas.92.26.12480;
Liu W., Wang J., Sauter N.K., Pearce D.;
"Steroid receptor heterodimerization demonstrated in vitro and in
vivo.";
Proc. Natl. Acad. Sci. U.S.A. 92:12480-12484(1995).
[11]
INTERACTION WITH NCOA2.
PubMed=9111344; DOI=10.1128/MCB.17.5.2735;
Hong H., Kohli K., Garabedian M.J., Stallcup M.R.;
"GRIP1, a transcriptional coactivator for the AF-2 transactivation
domain of steroid, thyroid, retinoid, and vitamin D receptors.";
Mol. Cell. Biol. 17:2735-2744(1997).
[12]
PHOSPHORYLATION AT THR-171; SER-224; SER-232 AND SER-246.
PubMed=9603939; DOI=10.1074/jbc.273.23.14315;
Rogatsky I., Waase C.L.M., Garabedian M.J.;
"Phosphorylation and inhibition of rat glucocorticoid receptor
transcriptional activation by glycogen synthase kinase-3 (GSK-3).
Species-specific differences between human and rat glucocorticoid
receptor signaling as revealed through GSK-3 phosphorylation.";
J. Biol. Chem. 273:14315-14321(1998).
[13]
INTERACTION WITH NRIP1.
PubMed=10364267; DOI=10.1074/jbc.274.25.18121;
Subramaniam N., Treuter E., Okret S.;
"Receptor interacting protein RIP140 inhibits both positive and
negative gene regulation by glucocorticoids.";
J. Biol. Chem. 274:18121-18127(1999).
[14]
INTERACTION WITH POU2F1 AND POU2F2, AND MUTAGENESIS OF CYS-500 AND
LEU-501.
PubMed=10480874; DOI=10.1074/jbc.274.38.26713;
Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L.,
Hache R.J.G.;
"Selective binding of steroid hormone receptors to octamer
transcription factors determines transcriptional synergism at the
mouse mammary tumor virus promoter.";
J. Biol. Chem. 274:26713-26719(1999).
[15]
INTERACTION WITH NCOA6.
PubMed=10866662; DOI=10.1128/MCB.20.14.5048-5063.2000;
Mahajan M.A., Samuels H.H.;
"A new family of nuclear receptor coregulators that integrates nuclear
receptor signaling through CBP.";
Mol. Cell. Biol. 20:5048-5063(2000).
[16]
HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, AND MUTAGENESIS OF
LEU-501.
PubMed=11278286; DOI=10.1074/jbc.M005363200;
Ou X.-M., Storring J.M., Kushwaha N., Albert P.R.;
"Heterodimerization of mineralocorticoid and glucocorticoid receptors
at a novel negative response element of the 5-HT1A receptor gene.";
J. Biol. Chem. 276:14299-14307(2001).
[17]
ALTERNATIVE INITIATION, AND MUTAGENESIS OF MET-1 AND MET-28.
PubMed=11435610; DOI=10.1210/mend.15.7.0667;
Yudt M.R., Cidlowski J.A.;
"Molecular identification and characterization of A and B forms of the
glucocorticoid receptor.";
Mol. Endocrinol. 15:1093-1103(2001).
[18]
INTERACTION WITH NCOA1, AND MUTAGENESIS OF GLU-773.
PubMed=12118039; DOI=10.1074/jbc.M204013200;
Kucera T., Waltner-Law M., Scott D.K., Prasad R., Granner D.K.;
"A point mutation of the AF2 transactivation domain of the
glucocorticoid receptor disrupts its interaction with steroid receptor
coactivator 1.";
J. Biol. Chem. 277:26098-26102(2002).
[19]
FUNCTION, INTERACTION WITH NCOA1; NCOA3; SMARCA4; SMARCC1; SMARCD1 AND
SMARCE1, AND MUTAGENESIS OF ARG-488.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[21]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=21730050; DOI=10.1074/jbc.M111.256610;
Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.;
"The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is
a mitochondrial protein that translocates to the nucleus to protect
cells against oxidative stress.";
J. Biol. Chem. 286:30152-30160(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND
SER-287, VARIANT [LARGE SCALE ANALYSIS] GLY-226, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[23]
SUMOYLATION AT LYS-297; LYS-313 AND LYS-721, INTERACTION WITH
UBE2I/UBC9 AND RWDD3, AND MUTAGENESIS OF LYS-297; LYS-313 AND LYS-721.
PubMed=23508108; DOI=10.1128/MCB.01470-12;
Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J.,
Paez-Pereda M., Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
"RSUME enhances glucocorticoid receptor SUMOylation and
transcriptional activity.";
Mol. Cell. Biol. 33:2116-2127(2013).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 434-525.
PubMed=1865905; DOI=10.1038/352497a0;
Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R.,
Sigler P.B.;
"Crystallographic analysis of the interaction of the glucocorticoid
receptor with DNA.";
Nature 352:497-505(1991).
[25]
STRUCTURE BY NMR OF 440-510.
PubMed=2115209; DOI=10.1126/science.2115209;
Haerd T., Kellenbach E., Boelens R., Maler B.A., Dahlman K.,
Freedman L.P., Carlstedt-Duke J., Yamamoto K.R., Gustafsson J.-A.,
Kaptein R.;
"Solution structure of the glucocorticoid receptor DNA-binding
domain.";
Science 249:157-160(1990).
[26]
STRUCTURE BY NMR OF 440-525.
PubMed=1751485; DOI=10.1021/bi00114a003;
Remerowski M.L., Kellenbach E., Boelens R., van der Marel A.,
van Boom J.H., Maler B.A., Yamamoto K.R., Kaptein R.;
"1H NMR studies of DNA recognition by the glucocorticoid receptor:
complex of the DNA binding domain with a half-site response element.";
Biochemistry 30:11620-11624(1991).
[27]
STRUCTURE BY NMR OF 440-525.
PubMed=1936288; DOI=10.1016/0014-5793(91)81322-Y;
Kellenbach E., Maler B.A., Yamamoto K.R., Boelens R., Kaptein R.;
"Identification of the metal coordinating residues in the DNA binding
domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR
spectroscopy.";
FEBS Lett. 291:367-370(1991).
[28]
STRUCTURE BY NMR OF 439-510.
PubMed=8257681; DOI=10.1021/bi00212a011;
Baumann H., Paulsen K., Kovacs H., Berglund H., Wright A.P.H.,
Gustafsson J.-A., Haerd T.;
"Refined solution structure of the glucocorticoid receptor DNA-binding
domain.";
Biochemistry 32:13463-13471(1993).
[29]
POLYMORPHISM OF POLY-GLN REGION.
PubMed=8493115; DOI=10.1093/nar/21.8.2014;
Gearing K.L., Gustafsson J.-A., Okret S.;
"Heterogeneity in the polyglutamine tract of the glucocorticoid
receptor from different rat strains.";
Nucleic Acids Res. 21:2014-2014(1993).
-!- FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of
action: as a transcription factor that binds to glucocorticoid
response elements (GRE), both for nuclear and mitochondrial DNA,
and as a modulator of other transcription factors. Affects
inflammatory responses, cellular proliferation and differentiation
in target tissues. Involved in chromatin remodeling
(PubMed:12917342). Plays a role in rapid mRNA degradation by
binding to the 5' UTR of target mRNAs and interacting with PNRC2
in a ligand-dependent manner which recruits the RNA helicase UPF1
and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By
similarity). Could act as a coactivator for STAT5-dependent
transcription upon growth hormone (GH) stimulation and could
reveal an essential role of hepatic GR in the control of body
growth (By similarity). {ECO:0000250|UniProtKB:P04150,
ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:12917342}.
-!- FUNCTION: Isoform A: Has transcriptional activation and repression
activity. Mediates glucocorticoid-induced apoptosis. Promotes
accurate chromosome segregation during mitosis. May act as a tumor
suppressor. May play a negative role in adipogenesis through the
regulation of lipolytic and antilipogenic gene expression.
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
-!- SUBUNIT: Interacts with GRIP1 (By similarity). Heteromultimeric
cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or
another immunophilin such as PPID, STIP1, or the immunophilin
homolog PPP5C (PubMed:21730050). Upon ligand binding FKBP5
dissociates from the complex and FKBP4 takes its place, thereby
linking the complex to dynein and mediating transport to the
nucleus, where the complex dissociates (By similarity). Directly
interacts with UNC45A (By similarity). Binds to DNA as a
homodimer, and as heterodimer with NR3C2 or the retinoid X
receptor (By similarity). Binds STAT5A and STAT5B homodimers and
heterodimers (By similarity). Interacts with NRIP1, POU2F1, POU2F2
and TRIM28 (PubMed:10364267, PubMed:10480874). Interacts with
several coactivator complexes, including the SMARCA4 complex,
CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as
NCOA2 and NCOA6 (PubMed:9111344, PubMed:10866662). Interaction
with BAG1 inhibits transactivation (By similarity). Interacts with
HEXIM1, PELP1 and TGFB1I1 (By similarity). Interacts with NCOA1
(PubMed:12917342). Interacts with NCOA3, SMARCA4, SMARCC1,
SMARCD1, and SMARCE1 (PubMed:12917342, PubMed:12118039). Interacts
with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (By
similarity). Interacts with CIART (By similarity). Interacts with
RWDD3 (PubMed:23508108). Interacts with UBE2I/UBC9 and this
interaction is enhanced in the presence of RWDD3
(PubMed:23508108). Interacts with NR4A3 (via nuclear receptor DNA-
binding domain), represses transcription activity of NR4A3 on the
POMC promoter Nur response element (NurRE) (By similarity).
Directly interacts with PNRC2 to attract and form a complex with
UPF1 and DCP1A; the interaction leads to rapid mRNA degradation
(By similarity). Interacts with GSK3B (By similarity). Interacts
with FNIP1 and FNIP2 (By similarity). Interacts (via C-terminus)
with HNRNPU (via C-terminus) (By similarity).
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537,
ECO:0000269|PubMed:10364267, ECO:0000269|PubMed:10480874,
ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:12118039,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:21730050,
ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:9111344}.
-!- INTERACTION:
Q62667:Mvp; NbExp=2; IntAct=EBI-1187143, EBI-918333;
Q15788:NCOA1 (xeno); NbExp=2; IntAct=EBI-1187143, EBI-455189;
Q63604:Ntrk2; NbExp=2; IntAct=EBI-1187143, EBI-7287667;
Q9BTK6:PAGR1 (xeno); NbExp=2; IntAct=EBI-1187143, EBI-2372223;
P51532:SMARCA4 (xeno); NbExp=3; IntAct=EBI-1187143, EBI-302489;
Q96GM5:SMARCD1 (xeno); NbExp=2; IntAct=EBI-1187143, EBI-358489;
-!- SUBCELLULAR LOCATION: Isoform A: Cytoplasm
{ECO:0000250|UniProtKB:P04150}. Nucleus
{ECO:0000250|UniProtKB:P04150}. Mitochondrion
{ECO:0000269|PubMed:21730050}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P04150}. Note=After ligand activation,
translocates from the cytoplasm to the nucleus.
{ECO:0000250|UniProtKB:P04150}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=A;
IsoId=P06536-1; Sequence=Displayed;
Name=B;
IsoId=P06536-2; Sequence=VSP_018969;
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain. The
ligand-binding domain is required for correct chromosome
segregation during mitosis although ligand binding is not
required. {ECO:0000250|UniProtKB:P04150}.
-!- PTM: Acetylation by CLOCK reduces its binding to glucocorticoid
response elements and its transcriptional activity. {ECO:0000250}.
-!- PTM: Increased proteasome-mediated degradation in response to
glucocorticoids. {ECO:0000250|UniProtKB:P04150}.
-!- PTM: Phosphorylated in the absence of hormone; becomes
hyperphosphorylated in the presence of glucocorticoids. The Ser-
224, Ser-246 and Ser-424-phosphorylated forms are mainly
cytoplasmic, and the Ser-232-phosphorylated form is nuclear.
Phosphorylation at Ser-232 increases transcriptional activity.
Phosphorylation at Ser-224, Ser-246 and Ser-424 decreases
signaling capacity. Phosphorylation at Ser-424 may protect from
glucocorticoid-induced apoptosis. Phosphorylation at Ser-224 and
Ser-232 is not required in regulation of chromosome segregation.
May be dephosphorylated by PPP5C, attenuates NR3C1 action.
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
-!- PTM: Sumoylation at Lys-297 and Lys-313 negatively regulates its
transcriptional activity. Sumoylation at Lys-721 positively
regulates its transcriptional activity in the presence of RWDD3.
Sumoylation at Lys-297 and Lys-313 is dispensable whereas
sumoylation at Lys-721 is critical for the stimulatory effect of
RWDD3 on its transcriptional activity. Heat shock increases
sumoylation in a RWDD3-dependent manner.
{ECO:0000269|PubMed:23508108}.
-!- PTM: Ubiquitinated; restricts glucocorticoid-mediated
transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M14053; AAA41203.1; -; mRNA.
EMBL; Y12264; CAA72938.1; -; mRNA.
EMBL; AY066016; AAL66772.2; -; mRNA.
EMBL; AF455050; AAL78956.1; -; mRNA.
EMBL; Y00489; CAA68545.1; -; mRNA.
EMBL; X69666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X69667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X69668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X69669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X69670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A24194; QRRTG.
RefSeq; NP_036708.2; NM_012576.2.
UniGene; Rn.90070; -.
PDB; 1GDC; NMR; -; A=439-510.
PDB; 1GLU; X-ray; 2.90 A; A/B=440-514.
PDB; 1LAT; X-ray; 1.90 A; A/B=440-515.
PDB; 1R4O; X-ray; 2.50 A; A/B=440-525.
PDB; 1R4R; X-ray; 3.00 A; A/B=440-525.
PDB; 1RGD; NMR; -; A=440-510.
PDB; 2GDA; NMR; -; A=439-510.
PDB; 3FYL; X-ray; 1.63 A; A/B=440-525.
PDB; 3G6P; X-ray; 1.99 A; A/B=440-525.
PDB; 3G6Q; X-ray; 2.26 A; A/B=440-525.
PDB; 3G6R; X-ray; 2.30 A; A/B=440-525.
PDB; 3G6T; X-ray; 1.90 A; A/B=440-525.
PDB; 3G6U; X-ray; 1.90 A; A/B=440-525.
PDB; 3G8U; X-ray; 1.90 A; A/B=440-525.
PDB; 3G8X; X-ray; 2.05 A; A/B=440-525.
PDB; 3G97; X-ray; 2.08 A; A/B=440-525.
PDB; 3G99; X-ray; 1.81 A; A/B=440-525.
PDB; 3G9I; X-ray; 1.85 A; A/B=440-525.
PDB; 3G9J; X-ray; 2.32 A; A/B=440-525.
PDB; 3G9M; X-ray; 1.61 A; A/B=440-525.
PDB; 3G9O; X-ray; 1.65 A; A/B=440-525.
PDB; 3G9P; X-ray; 1.65 A; A/B=440-525.
PDBsum; 1GDC; -.
PDBsum; 1GLU; -.
PDBsum; 1LAT; -.
PDBsum; 1R4O; -.
PDBsum; 1R4R; -.
PDBsum; 1RGD; -.
PDBsum; 2GDA; -.
PDBsum; 3FYL; -.
PDBsum; 3G6P; -.
PDBsum; 3G6Q; -.
PDBsum; 3G6R; -.
PDBsum; 3G6T; -.
PDBsum; 3G6U; -.
PDBsum; 3G8U; -.
PDBsum; 3G8X; -.
PDBsum; 3G97; -.
PDBsum; 3G99; -.
PDBsum; 3G9I; -.
PDBsum; 3G9J; -.
PDBsum; 3G9M; -.
PDBsum; 3G9O; -.
PDBsum; 3G9P; -.
ProteinModelPortal; P06536; -.
SMR; P06536; -.
BioGrid; 246578; 15.
CORUM; P06536; -.
DIP; DIP-38940N; -.
ELM; P06536; -.
IntAct; P06536; 34.
MINT; MINT-194828; -.
STRING; 10116.ENSRNOP00000044335; -.
BindingDB; P06536; -.
ChEMBL; CHEMBL3368; -.
iPTMnet; P06536; -.
PhosphoSitePlus; P06536; -.
PaxDb; P06536; -.
PeptideAtlas; P06536; -.
PRIDE; P06536; -.
GeneID; 24413; -.
KEGG; rno:24413; -.
UCSC; RGD:2741; rat. [P06536-1]
CTD; 2908; -.
RGD; 2741; Nr3c1.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000037950; -.
HOVERGEN; HBG007583; -.
InParanoid; P06536; -.
KO; K05771; -.
PhylomeDB; P06536; -.
EvolutionaryTrace; P06536; -.
PRO; PR:P06536; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0001047; F:core promoter binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0004883; F:glucocorticoid receptor activity; ISO:RGD.
GO; GO:0038051; F:glucocorticoid-activated RNA polymerase II transcription factor binding transcription factor activity; ISS:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IDA:RGD.
GO; GO:0042562; F:hormone binding; IPI:RGD.
GO; GO:0030544; F:Hsp70 protein binding; IDA:RGD.
GO; GO:0051879; F:Hsp90 protein binding; IDA:RGD.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; ISO:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:RGD.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0005496; F:steroid binding; IPI:RGD.
GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
GO; GO:0032183; F:SUMO binding; ISO:RGD.
GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; TAS:RGD.
GO; GO:0030325; P:adrenal gland development; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0008209; P:androgen metabolic process; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IMP:RGD.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; IEP:RGD.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0008211; P:glucocorticoid metabolic process; ISO:RGD.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0060603; P:mammary gland duct morphogenesis; ISO:RGD.
GO; GO:0042711; P:maternal behavior; ISO:RGD.
GO; GO:0014889; P:muscle atrophy; IEP:RGD.
GO; GO:1900170; P:negative regulation of glucocorticoid mediated signaling pathway; ISO:RGD.
GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0043116; P:negative regulation of vascular permeability; IMP:RGD.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; IDA:RGD.
GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IDA:RGD.
GO; GO:0031946; P:regulation of glucocorticoid biosynthetic process; ISO:RGD.
GO; GO:0006111; P:regulation of gluconeogenesis; ISO:RGD.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0046685; P:response to arsenic-containing substance; IDA:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0014854; P:response to inactivity; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0046689; P:response to mercury ion; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; ISO:RGD.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR001409; Glcrtcd_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF02155; GCR; 2.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00528; GLCORTICOIDR.
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; Acetylation; Alternative initiation;
Chromatin regulator; Complete proteome; Cytoplasm; Cytoskeleton;
DNA-binding; Isopeptide bond; Lipid-binding; Metal-binding;
Methylation; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Steroid-binding; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 795 Glucocorticoid receptor.
/FTId=PRO_0000019941.
DNA_BIND 440 505 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 440 460 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 476 500 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 439 Modulating.
REGION 504 795 Interaction with CLOCK. {ECO:0000250}.
REGION 506 546 Hinge.
REGION 547 795 Steroid-binding.
REGION 550 715 Interaction with CRY1. {ECO:0000250}.
COMPBIAS 75 97 Poly-Gln.
COMPBIAS 419 438 Glu/Pro/Ser/Thr-rich (PEST region).
MOD_RES 24 24 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 171 171 Phosphothreonine.
{ECO:0000269|PubMed:9603939}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:9603939}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:9603939}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000269|PubMed:9603939}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 511 511 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 513 513 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 514 514 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:23508108}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:23508108}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 721 721 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:23508108}.
VAR_SEQ 1 27 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_018969.
VARIANT 77 77 Missing (in strain: Brown Norway/Crl).
VARIANT 78 79 Missing (in strain: SHR/OlaIpcv).
VARIANT 83 96 Missing (in strain: Sprague-Dawley).
VARIANT 226 226 S -> G (in strain: SHR/OlaIpcv and Brown
Norway/Crl).
{ECO:0000244|PubMed:22673903,
ECO:0000269|Ref.3}.
VARIANT 260 260 N -> D (in strain: SHR/OlaIpcv and Brown
Norway/Crl). {ECO:0000269|Ref.3}.
MUTAGEN 1 1 M->T: Abolishes expression of A-type
isoforms. {ECO:0000269|PubMed:11435610}.
MUTAGEN 28 28 M->T: Abolishes expression of B-type
isoforms. {ECO:0000269|PubMed:11435610}.
MUTAGEN 297 297 K->R: Enhances transcriptional activity;
when associated with R-313.
{ECO:0000269|PubMed:23508108}.
MUTAGEN 313 313 K->R: Enhances transcriptional activity;
when associated with R-297.
{ECO:0000269|PubMed:23508108}.
MUTAGEN 481 481 D->R: Disrupts dimerization and decreases
transcription transactivation.
{ECO:0000269|PubMed:8618925}.
MUTAGEN 488 488 R->Q: Loss of chromatin specific function
and reduces chromatin remodeling.
Abolishes interaction with SMARD1.
{ECO:0000269|PubMed:12917342}.
MUTAGEN 500 500 C->Y: Abolishes interaction with POU2F2.
{ECO:0000269|PubMed:10480874}.
MUTAGEN 501 501 L->P: Abrogates DNA-binding and
transcription transactivation. Abolishes
interaction with POU2F1 and POU2F2.
{ECO:0000269|PubMed:10480874,
ECO:0000269|PubMed:11278286}.
MUTAGEN 656 656 C->S: Strongly increases affinity for
dexamethasone.
{ECO:0000269|PubMed:1939229}.
MUTAGEN 721 721 K->R: Abolishes the stimulatory effect of
RWDD3 on its transcriptional activity.
Diminishes NCOA2 coactivator activity.
{ECO:0000269|PubMed:23508108}.
MUTAGEN 773 773 E->A: Abolishes interaction with NCOA1
and reduces transcription
transactivation; when associated with S-
656. {ECO:0000269|PubMed:12118039}.
CONFLICT 95 96 Missing (in Ref. 3; AAL78956).
{ECO:0000305}.
CONFLICT 98 98 D -> G (in Ref. 1; AAA41203).
{ECO:0000305}.
CONFLICT 345 345 S -> T (in Ref. 4; CAA68545).
{ECO:0000305}.
CONFLICT 600 600 L -> P (in Ref. 2; CAA72938 and 3;
AAL66772/AAL78956). {ECO:0000305}.
CONFLICT 602 602 L -> F (in Ref. 3; AAL66772/AAL78956).
{ECO:0000305}.
TURN 441 443 {ECO:0000244|PDB:3G9M}.
STRAND 444 446 {ECO:0000244|PDB:3G97}.
STRAND 449 451 {ECO:0000244|PDB:3G9M}.
STRAND 454 456 {ECO:0000244|PDB:3G9M}.
HELIX 458 469 {ECO:0000244|PDB:3G9M}.
STRAND 477 480 {ECO:0000244|PDB:3G9M}.
HELIX 488 490 {ECO:0000244|PDB:3G9M}.
HELIX 493 503 {ECO:0000244|PDB:3G9M}.
HELIX 509 513 {ECO:0000244|PDB:3G9M}.
SEQUENCE 795 AA; 87556 MW; 9C9DE0B1D6724845 CRC64;
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ
RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS KAVSLSMGLY MGETETKVMG
NDLGYPQQGQ LGLSSGETDF RLLEESIANL NRSTSVPENP KSSTSATGCA TPTEKEFPKT
HSDASSEQQN RKSQTGTNGG SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI
DENLLSPLAG EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK
DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS
LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA LNFPGRSVFS NGYSSPGMRP
DVSSPPSSSS AATGPPPKLC LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN
DCIIDKIRRK NCPACRYRKC LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP
AALPQLTPTL VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL
GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ RMSLPCMYDQ
CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS QELFDEIRMT YIKELGKAIV
KREGNSSQNW QRFYQLTKLL DSMHEVVENL LTYCFQTFLD KTMSIEFPEM LAEIITNQIP
KYSNGNIKKL LFHQK


Related products :

Catalog number Product name Quantity
NR4A1 NR3C1 Gene nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)
E1608p ELISA Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Pig,Sus scrofa 96T
E1608p ELISA kit Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Pig,Sus scrofa 96T
U1608p CLIA Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Pig,Sus scrofa 96T
U1608r CLIA Glucocorticoid receptor,GR,Grl,Nr3c1,Nuclear receptor subfamily 3 group C member 1,Rat,Rattus norvegicus 96T
E1608r ELISA Glucocorticoid receptor,GR,Grl,Nr3c1,Nuclear receptor subfamily 3 group C member 1,Rat,Rattus norvegicus 96T
18-783-77657 SHEEP ANTI HUMAN GLUCOCORTICOID RECEPTOR - GR; Nuclear receptor subfamily 3 group C member 1 Polyclonal 1 ml
18-783-77656 SHEEP ANTI HUMAN GLUCOCORTICOID RECEPTOR - GR; Nuclear receptor subfamily 3 group C member 1 Polyclonal 1 ml
E1608r ELISA kit Glucocorticoid receptor,GR,Grl,Nr3c1,Nuclear receptor subfamily 3 group C member 1,Rat,Rattus norvegicus 96T
E1608Rb ELISA kit Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Oryctolagus cuniculus,Rabbit 96T
E1608h ELISA kit Glucocorticoid receptor,GR,GRL,Homo sapiens,Human,NR3C1,Nuclear receptor subfamily 3 group C member 1 96T
E1608m ELISA kit Glucocorticoid receptor,GR,Grl,Grl1,Mouse,Mus musculus,Nr3c1,Nuclear receptor subfamily 3 group C member 1 96T
U1608Rb CLIA Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Oryctolagus cuniculus,Rabbit 96T
E1608Rb ELISA Glucocorticoid receptor,GR,GRL,NR3C1,Nuclear receptor subfamily 3 group C member 1,Oryctolagus cuniculus,Rabbit 96T
U1608m CLIA Glucocorticoid receptor,GR,Grl,Grl1,Mouse,Mus musculus,Nr3c1,Nuclear receptor subfamily 3 group C member 1 96T
E1608m ELISA Glucocorticoid receptor,GR,Grl,Grl1,Mouse,Mus musculus,Nr3c1,Nuclear receptor subfamily 3 group C member 1 96T
E1608h ELISA Glucocorticoid receptor,GR,GRL,Homo sapiens,Human,NR3C1,Nuclear receptor subfamily 3 group C member 1 96T
U1608h CLIA Glucocorticoid receptor,GR,GRL,Homo sapiens,Human,NR3C1,Nuclear receptor subfamily 3 group C member 1 96T
CSB-EL016059PI Pig nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) (NR3C1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL016059SH Sheep nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) (NR3C1) ELISA kit, Species Sheep, Sample Type serum, plasma 96T
CSB-EL016059RB Rabbit nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) (NR3C1) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL016059GU Guinea pig nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) (NR3C1) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
CSB-EL016059HU Human nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) (NR3C1) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB27810 Gfrp,Hmr,Mouse,Mus musculus,N10,Nr4a1,Nuclear hormone receptor NUR_77,Nuclear protein N10,Nuclear receptor subfamily 4 group A member 1,Nur77,Orphan nuclear receptor HMR
EIAAB27782 Liver X receptor beta,Lxrb,Nr1h2,Nuclear receptor subfamily 1 group H member 2,Orphan nuclear receptor OR-1,Oxysterols receptor LXR-beta,Rat,Rattus norvegicus,Ubiquitously-expressed nuclear receptor,U


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur