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

 GCR_HUMAN               Reviewed;         777 AA.
P04150; A0ZXF9; B0LPG8; D3DQF4; F5ATB7; P04151; Q53EP5; Q6N0A4;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1986, sequence version 1.
12-SEP-2018, entry version 252.
RecName: Full=Glucocorticoid receptor;
Short=GR;
AltName: Full=Nuclear receptor subfamily 3 group C member 1;
Name=NR3C1; Synonyms=GRL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Fibroblast;
PubMed=2867473; DOI=10.1038/318635a0;
Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R.,
Thompson E.B., Rosenfeld M.G., Evans R.M.;
"Primary structure and expression of a functional human glucocorticoid
receptor cDNA.";
Nature 318:635-641(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA AND BETA).
PubMed=1707881;
Encio I.J., Detera-Wadleigh S.D.;
"The genomic structure of the human glucocorticoid receptor.";
J. Biol. Chem. 266:7182-7188(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=20843780; DOI=10.1093/nar/gkq750;
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W.,
Mindrinos M., Speed T.P., Scharfe C.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
PubMed=17404046; DOI=10.1196/annals.1397.037;
Turner J.D., Schote A.B., Keipes M., Muller C.P.;
"A new transcript splice variant of the human glucocorticoid receptor:
identification and tissue distribution of hGR Delta 313-338, an
alternative exon 2 transactivation domain isoform.";
Ann. N. Y. Acad. Sci. 1095:334-341(2007).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANTS ASP-72; ALA-321
AND SER-766, AND CHARACTERIZATION OF VARIANTS ASP-72; ALA-321 AND
SER-766.
PubMed=21701417; DOI=10.1097/SHK.0b013e318228eca7;
Tung K., Baker A.C., Amini A., Green T.L., Chew V.W., Lim D.,
Nguyen S.T., Yee K.S., Cho K., Greenhalgh D.G.;
"Novel hyperactive glucocorticoid receptor isoform identified within a
human population.";
Shock 36:339-344(2011).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
TISSUE=Osteosarcoma;
Munroe D.G., Pang J., Taylor G.R., Lau C., Plante R.K., Zhou L.;
"Alternative splicing within the DNA binding domain creates a novel
isoform of the human glucocorticoid receptor.";
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Uterine endothelium;
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-23 AND VAL-65.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[12]
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.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=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).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
PubMed=2026589;
Leclerc S., Xie B.X., Roy R., Govindan M.V.;
"Purification of a human glucocorticoid receptor gene promoter-binding
protein. Production of polyclonal antibodies against the purified
factor.";
J. Biol. Chem. 266:8711-8719(1991).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
PubMed=1958537; DOI=10.1016/0960-0760(91)90197-D;
Govindan M.V., Pothier F., Leclerc S., Palaniswami R., Xie B.;
"Human glucocorticoid receptor gene promotor-homologous down
regulation.";
J. Steroid Biochem. Mol. Biol. 40:317-323(1991).
[16]
DOMAINS.
PubMed=3841189; DOI=10.1038/318670a0;
Weinberger C., Hollenberg S.M., Rosenfeld M.G., Evans R.M.;
"Domain structure of human glucocorticoid receptor and its
relationship to the v-erb-A oncogene product.";
Nature 318:670-672(1985).
[17]
ALTERNATIVE SPLICING (ISOFORMS GR-P; GR-A ALPHA AND GR-A BETA).
PubMed=8358712;
Moalli P.A., Pillay S., Krett N.L., Rosen S.T.;
"Alternatively spliced glucocorticoid receptor messenger RNAs in
glucocorticoid-resistant human multiple myeloma cells.";
Cancer Res. 53:3877-3879(1993).
[18]
FUNCTION (ISOFORM BETA), AND TISSUE SPECIFICITY (ISOFORM BETA).
PubMed=7769088; DOI=10.1172/JCI117943;
Bamberger C.M., Bamberger A.M., de Castro M., Chrousos G.P.;
"Glucocorticoid receptor beta, a potential endogenous inhibitor of
glucocorticoid action in humans.";
J. Clin. Invest. 95:2435-2441(1995).
[19]
FUNCTION (ISOFORM BETA), SUBCELLULAR LOCATION (ISOFORMS ALPHA AND
BETA), AND TISSUE SPECIFICITY (ISOFORM BETA).
PubMed=8621628; DOI=10.1074/jbc.271.16.9550;
Oakley R.H., Sar M., Cidlowski J.A.;
"The human glucocorticoid receptor beta isoform. Expression,
biochemical properties, and putative function.";
J. Biol. Chem. 271:9550-9559(1996).
[20]
INTERACTION WITH HNRNPU.
PubMed=9353307;
Eggert M., Michel J., Schneider S., Bornfleth H., Baniahmad A.,
Fackelmayer F.O., Schmidt S., Renkawitz R.;
"The glucocorticoid receptor is associated with the RNA-binding
nuclear matrix protein hnRNP U.";
J. Biol. Chem. 272:28471-28478(1997).
[21]
INTERACTION WITH TADA2L AND THE ADA COMPLEX, AND MUTAGENESIS OF
PHE-191; ILE-193; LEU-194; LEU-197; TRP-213; LEU-224; LEU-225; PHE-235
AND LEU-236.
PubMed=9154805; DOI=10.1128/MCB.17.6.3065;
Henriksson A., Almloef T., Ford J., McEwan I.J., Gustafsson J.-A.,
Wright A.P.H.;
"Role of the Ada adaptor complex in gene activation by the
glucocorticoid receptor.";
Mol. Cell. Biol. 17:3065-3073(1997).
[22]
FUNCTION, AND INTERACTION WITH THE SMARCA4 COMPLEX; NCOA1; NCOA2 AND
THE CREBBP/EP300 COMPLEX.
PubMed=9590696; DOI=10.1038/30032;
Fryer C.J., Archer T.K.;
"Chromatin remodelling by the glucocorticoid receptor requires the
BRG1 complex.";
Nature 393:88-91(1998).
[23]
INTERACTION WITH BAG1.
PubMed=10477749; DOI=10.1083/jcb.146.5.929;
Schneikert J., Huebner S., Martin E., Cato A.B.C.;
"A nuclear action of the eukaryotic cochaperone RAP46 in
downregulation of glucocorticoid receptor activity.";
J. Cell Biol. 146:929-940(1999).
[24]
ALTERNATIVE SPLICING (ISOFORMS ALPHA-2 AND BETA-2).
PubMed=10566686; DOI=10.1210/jcem.84.11.6235;
Rivers C., Levy A., Hancock J., Lightman S., Norman M.;
"Insertion of an amino acid in the DNA-binding domain of the
glucocorticoid receptor as a result of alternative splicing.";
J. Clin. Endocrinol. Metab. 84:4283-4286(1999).
[25]
TISSUE SPECIFICITY.
PubMed=10902803; DOI=10.1210/jcem.85.7.6663;
Kayes-Wandover K.M., White P.C.;
"Steroidogenic enzyme gene expression in the human heart.";
J. Clin. Endocrinol. Metab. 85:2519-2525(2000).
[26]
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).
[27]
EFFECT ON EXPANDED POLYGLUTAMINE PROTEIN.
PubMed=10639135; DOI=10.1073/pnas.97.2.657;
Diamond M.I., Robinson M.R., Yamamoto K.R.;
"Regulation of expanded polyglutamine protein aggregation and nuclear
localization by the glucocorticoid receptor.";
Proc. Natl. Acad. Sci. U.S.A. 97:657-661(2000).
[28]
FUNCTION (ISOFORM GR-P).
PubMed=11358809;
de Lange P., Segeren C.M., Koper J.W., Wiemer E., Sonneveld P.,
Brinkmann A.O., White A., Brogan I.J., de Jong F.H., Lamberts S.W.;
"Expression in hematological malignancies of a glucocorticoid receptor
splice variant that augments glucocorticoid receptor-mediated effects
in transfected cells.";
Cancer Res. 61:3937-3941(2001).
[29]
GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
PubMed=11555652; DOI=10.1074/jbc.M106033200;
Wallace A.D., Cidlowski J.A.;
"Proteasome-mediated glucocorticoid receptor degradation restricts
transcriptional signaling by glucocorticoids.";
J. Biol. Chem. 276:42714-42721(2001).
[30]
REDUCTION OF CELL DEATH IN RESPONSE TO CORTICOSTEROIDS.
PubMed=11238589; DOI=10.1084/jem.193.5.585;
Strickland I., Kisich K., Hauk P.J., Vottero A., Chrousos G.P.,
Klemm D.J., Leung D.Y.M.;
"High constitutive glucocorticoid receptor beta in human neutrophils
enables them to reduce their spontaneous rate of cell death in
response to corticosteroids.";
J. Exp. Med. 193:585-593(2001).
[31]
FUNCTION (ISOFORMS ALPHA AND ALPHA-B), ALTERNATIVE INITIATION, AND
MUTAGENESIS OF MET-1 AND MET-27.
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).
[32]
INDUCTION (ISOFORMS ALPHA AND BETA).
PubMed=11381138; DOI=10.1073/pnas.121455098;
Webster J.C., Oakley R.H., Jewell C.M., Cidlowski J.A.;
"Proinflammatory cytokines regulate human glucocorticoid receptor gene
expression and lead to the accumulation of the dominant negative beta
isoform: a mechanism for the generation of glucocorticoid
resistance.";
Proc. Natl. Acad. Sci. U.S.A. 98:6865-6870(2001).
[33]
SUMOYLATION, AND MUTAGENESIS OF LYS-277; LYS-293 AND LYS-703.
PubMed=12144530; DOI=10.1042/BJ20021085;
Tian S., Poukka H., Palvimo J.J., Jaenne O.A.;
"Small ubiquitin-related modifier-1 (SUMO-1) modification of the
glucocorticoid receptor.";
Biochem. J. 367:907-911(2002).
[34]
PHOSPHORYLATION AT SER-203 AND SER-211.
PubMed=12000743; DOI=10.1074/jbc.M110530200;
Wang Z., Frederick J., Garabedian M.J.;
"Deciphering the phosphorylation 'code' of the glucocorticoid receptor
in vivo.";
J. Biol. Chem. 277:26573-26580(2002).
[35]
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).
[36]
REVIEW ON ALTERNATIVE SPLICING, AND ALTERNATIVE INITIATION.
PubMed=15265776; DOI=10.1196/annals.1321.008;
Lu N.Z., Cidlowski J.A.;
"The origin and functions of multiple human glucocorticoid receptor
isoforms.";
Ann. N. Y. Acad. Sci. 1024:102-123(2004).
[37]
INTERACTION WITH TGFB1I1.
PubMed=15211577; DOI=10.1002/jcb.20109;
Guerrero-Santoro J., Yang L., Stallcup M.R., DeFranco D.B.;
"Distinct LIM domains of Hic-5/ARA55 are required for nuclear matrix
targeting and glucocorticoid receptor binding and coactivation.";
J. Cell. Biochem. 92:810-819(2004).
[38]
FUNCTION (ISOFORMS ALPHA; ALPHA-B; ALPHA-C1; ALPHA-C2; ALPHA-C3;
ALPHA-D1; ALPHA-D2 AND ALPHA-D3), SUBCELLULAR LOCATION (ISOFORM
ALPHA-B), ALTERNATIVE INITIATION (ISOFORMS ALPHA; ALPHA-B; ALPHA-C1;
ALPHA-C2; ALPHA-C3; ALPHA-D1; ALPHA-D2 AND ALPHA-D3), AND MUTAGENESIS
OF MET-1; MET-27; MET-86; MET-90; MET-98; MET-316; MET-331 AND
MET-336.
PubMed=15866175; DOI=10.1016/j.molcel.2005.03.025;
Lu N.Z., Cidlowski J.A.;
"Translational regulatory mechanisms generate N-terminal
glucocorticoid receptor isoforms with unique transcriptional target
genes.";
Mol. Cell 18:331-342(2005).
[39]
INTERACTION WITH NR4A3.
PubMed=15591535; DOI=10.1210/me.2004-0333;
Martens C., Bilodeau S., Maira M., Gauthier Y., Drouin J.;
"Protein-protein interactions and transcriptional antagonism between
the subfamily of NGFI-B/Nur77 orphan nuclear receptors and
glucocorticoid receptor.";
Mol. Endocrinol. 19:885-897(2005).
[40]
INTERACTION WITH HEXIM1.
PubMed=15941832; DOI=10.1073/pnas.0409863102;
Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H.,
Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H.;
"HEXIM1 forms a transcriptionally abortive complex with glucocorticoid
receptor without involving 7SK RNA and positive transcription
elongation factor b.";
Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005).
[41]
INTERACTION WITH UNC45A.
PubMed=16478993; DOI=10.1128/MCB.26.5.1722-1730.2006;
Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F.,
Wood W.M., Felts S.J., Horwitz K.B., Toft D.;
"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
chaperoning pathway.";
Mol. Cell. Biol. 26:1722-1730(2006).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[44]
INTERACTION WITH GSK3B, SUBCELLULAR LOCATION (ISOFORM ALPHA),
PHOSPHORYLATION AT SER-404, MUTAGENESIS OF SER-404, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18838540; DOI=10.1128/MCB.00808-08;
Galliher-Beckley A.J., Williams J.G., Collins J.B., Cidlowski J.A.;
"Glycogen synthase kinase 3beta-mediated serine phosphorylation of the
human glucocorticoid receptor redirects gene expression profiles.";
Mol. Cell. Biol. 28:7309-7322(2008).
[45]
PHOSPHORYLATION AT SER-203; SER-211 AND SER-226, AND MUTAGENESIS OF
SER-211 AND SER-226.
PubMed=18483179; DOI=10.1210/me.2007-0219;
Chen W., Dang T., Blind R.D., Wang Z., Cavasotto C.N., Hittelman A.B.,
Rogatsky I., Logan S.K., Garabedian M.J.;
"Glucocorticoid receptor phosphorylation differentially affects target
gene expression.";
Mol. Endocrinol. 22:1754-1766(2008).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-226 AND
SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[47]
FUNCTION (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR LOCATION (ISOFORM
BETA).
PubMed=19248771; DOI=10.1016/j.bbrc.2009.02.110;
Kino T., Manoli I., Kelkar S., Wang Y., Su Y.A., Chrousos G.P.;
"Glucocorticoid receptor (GR) beta has intrinsic, GRalpha-independent
transcriptional activity.";
Biochem. Biophys. Res. Commun. 381:671-675(2009).
[48]
FUNCTION (ISOFORM ALPHA), ACETYLATION AT LYS-480; LYS-492; LYS-494 AND
LYS-495, MUTAGENESIS OF LYS-480; LYS-492; LYS-494 AND LYS-495, AND
INTERACTION WITH CLOCK.
PubMed=19141540; DOI=10.1096/fj.08-117697;
Nader N., Chrousos G.P., Kino T.;
"Circadian rhythm transcription factor CLOCK regulates the
transcriptional activity of the glucocorticoid receptor by acetylating
its hinge region lysine cluster: potential physiological
implications.";
FASEB J. 23:1572-1583(2009).
[49]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[50]
FUNCTION (ISOFORMS ALPHA; BETA; ALPHA-2 AND 10).
PubMed=20484466; DOI=10.1210/en.2009-1254;
Taniguchi Y., Iwasaki Y., Tsugita M., Nishiyama M., Taguchi T.,
Okazaki M., Nakayama S., Kambayashi M., Hashimoto K., Terada Y.;
"Glucocorticoid receptor-beta and receptor-gamma exert dominant
negative effect on gene repression but not on gene induction.";
Endocrinology 151:3204-3213(2010).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[53]
FUNCTION (ISOFORM ALPHA), AND SUBCELLULAR LOCATION (ISOFORM ALPHA).
PubMed=21664385; DOI=10.1016/j.bbamcr.2011.05.014;
Psarra A.M., Sekeris C.E.;
"Glucocorticoids induce mitochondrial gene transcription in HepG2
cells: role of the mitochondrial glucocorticoid receptor.";
Biochim. Biophys. Acta 1813:1814-1821(2011).
[54]
SUBUNIT.
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).
[55]
INTERACTION WITH CRY1 AND CRY2.
PubMed=22170608; DOI=10.1038/nature10700;
Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H.,
Jonker J.W., Downes M., Evans R.M.;
"Cryptochromes mediate rhythmic repression of the glucocorticoid
receptor.";
Nature 480:552-556(2011).
[56]
ACETYLATION, AND INTERACTION WITH CLOCK.
PubMed=21980503; DOI=10.1371/journal.pone.0025612;
Charmandari E., Chrousos G.P., Lambrou G.I., Pavlaki A., Koide H.,
Ng S.S., Kino T.;
"Peripheral CLOCK regulates target-tissue glucocorticoid receptor
transcriptional activity in a circadian fashion in man.";
PLoS ONE 6:E25612-E25612(2011).
[57]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS ALPHA-B AND
BETA-B), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[58]
FUNCTION (ISOFORMS ALPHA; ALPHA-C3 AND ALPHA-D3).
PubMed=23303127; DOI=10.1038/cddis.2012.193;
Wu I., Shin S.C., Cao Y., Bender I.K., Jafari N., Feng G., Lin S.,
Cidlowski J.A., Schleimer R.P., Lu N.Z.;
"Selective glucocorticoid receptor translational isoforms reveal
glucocorticoid-induced apoptotic transcriptomes.";
Cell Death Dis. 4:E453-E453(2013).
[59]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-45 AND SER-267,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[60]
MUTAGENESIS OF LYS-703.
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).
[61]
FUNCTION (ISOFORMS ALPHA; ALPHA-C3 AND ALPHA-D3), AND MUTAGENESIS OF
ASP-101; 106-GLN-GLN-107 AND 113-SER-SER-114.
PubMed=23820903; DOI=10.1210/me.2013-1009;
Bender I.K., Cao Y., Lu N.Z.;
"Determinants of the heightened activity of glucocorticoid receptor
translational isoforms.";
Mol. Endocrinol. 27:1577-1587(2013).
[62]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[63]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-293, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[64]
FUNCTION (ISOFORM BETA), AND SUBCELLULAR LOCATION (ISOFORM BETA).
PubMed=26711253; DOI=10.1128/MCB.00908-15;
He B., Cruz-Topete D., Oakley R.H., Xiao X., Cidlowski J.A.;
"Human Glucocorticoid Receptor beta (hGRbeta) Regulates
Gluconeogenesis and Inflammation in Mouse Liver.";
Mol. Cell. Biol. 36:714-730(2015).
[65]
FUNCTION, AND INTERACTION WITH PNRC2.
PubMed=25775514; DOI=10.1073/pnas.1409612112;
Cho H., Park O.H., Park J., Ryu I., Kim J., Ko J., Kim Y.K.;
"Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent
manner to recruit UPF1 for rapid mRNA degradation.";
Proc. Natl. Acad. Sci. U.S.A. 112:E1540-E1549(2015).
[66]
FUNCTION (ISOFORM ALPHA), SUBCELLULAR LOCATION (ISOFORM ALPHA), TISSUE
SPECIFICITY, DOMAIN, AND PHOSPHORYLATION AT SER-203 AND SER-211.
PubMed=25847991; DOI=10.1073/pnas.1411356112;
Matthews L.C., Berry A.A., Morgan D.J., Poolman T.M., Bauer K.,
Kramer F., Spiller D.G., Richardson R.V., Chapman K.E., Farrow S.N.,
Norman M.R., Williamson A.J., Whetton A.D., Taylor S.S.,
Tuckermann J.P., White M.R., Ray D.W.;
"Glucocorticoid receptor regulates accurate chromosome segregation and
is associated with malignancy.";
Proc. Natl. Acad. Sci. U.S.A. 112:5479-5484(2015).
[67]
INTERACTION WITH FNIP1 AND FNIP2.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[68]
IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; CDC37; PPP5C; TSC1;
TSC2; AKT; CDK4 AND RAF1.
PubMed=29127155; DOI=10.15252/embj.201796700;
Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R.,
Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C.,
Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M.,
Mollapour M.;
"Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates
folding of kinase and non-kinase clients.";
EMBO J. 36:3650-3665(2017).
[69]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258 AND LYS-277, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[70]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 521-777 OF MUTANT SER-602 IN
COMPLEX WITH NCOA2; DEXAMETHASONE AND RU-486, AND MUTAGENESIS OF
ARG-585; ASP-590; PHE-602; PRO-625 AND ILE-628.
PubMed=12151000; DOI=10.1016/S0092-8674(02)00817-6;
Bledsoe R.K., Montana V.G., Stanley T.B., Delves C.J., Apolito C.J.,
McKee D.D., Consler T.G., Parks D.J., Stewart E.L., Willson T.M.,
Lambert M.H., Moore J.T., Pearce K.H., Xu H.E.;
"Crystal structure of the glucocorticoid receptor ligand binding
domain reveals a novel mode of receptor dimerization and coactivator
recognition.";
Cell 110:93-105(2002).
[71]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 500-777 OF MUTANT SER-602 IN
COMPLEX WITH COACTIVATOR PEPTIDE; DEXAMETHASONE AND WITH RU-486.
PubMed=12686538; DOI=10.1074/jbc.M212711200;
Kauppi B., Jakob C., Faernegaardh M., Yang J., Ahola H., Alarcon M.,
Calles K., Engstrom O., Harlan J., Muchmore S., Ramqvist A.-K.,
Thorell S., Oehman L., Greer J., Gustafsson J.-A., Carlstedt-Duke J.,
Carlquist M.;
"The three-dimensional structures of antagonistic and agonistic forms
of the glucocorticoid receptor ligand-binding domain: RU-486 induces a
transconformation that leads to active antagonism.";
J. Biol. Chem. 278:22748-22754(2003).
[72]
CHARACTERIZATION OF VARIANT GCCR VAL-641.
PubMed=1704018; DOI=10.1172/JCI115046;
Hurley D.M., Accili D., Stratakis C.A., Karl M., Vamvakopoulos N.,
Rorer E., Constantine K., Taylor S.I., Chrousos G.P.;
"Point mutation causing a single amino acid substitution in the
hormone binding domain of the glucocorticoid receptor in familial
glucocorticoid resistance.";
J. Clin. Invest. 87:680-686(1991).
[73]
VARIANTS TYR-421 AND PHE-753.
PubMed=8358735;
Powers J.H., Hillmann A.G., Tang D.C., Harmon J.M.;
"Cloning and expression of mutant glucocorticoid receptors from
glucocorticoid-sensitive and -resistant human leukemic cells.";
Cancer Res. 53:4059-4065(1993).
[74]
VARIANT SER-363.
PubMed=8445027; DOI=10.1210/jcem.76.3.8445027;
Karl M., Lamberts S.W.J., Detera-Wadleigh S.D., Encio I.J.,
Stratakis C.A., Hurley D.M., Accili D., Chrousos G.P.;
"Familial glucocorticoid resistance caused by a splice site deletion
in the human glucocorticoid receptor gene.";
J. Clin. Endocrinol. Metab. 76:683-689(1993).
[75]
VARIANT GCCR ILE-729.
PubMed=7683692; DOI=10.1172/JCI116410;
Malchoff D.M., Brufsky A., Reardon G., McDermott P., Javier E.C.,
Bergh C.H., Rowe D., Malchoff C.D.;
"A mutation of the glucocorticoid receptor in primary cortisol
resistance.";
J. Clin. Invest. 91:1918-1925(1993).
[76]
VARIANT PHE-753.
PubMed=8316249; DOI=10.1210/mend.7.5.8316249;
Ashraf J., Thompson E.B.;
"Identification of the activation-labile gene: a single point mutation
in the human glucocorticoid receptor presents as two distinct receptor
phenotypes.";
Mol. Endocrinol. 7:631-642(1993).
[77]
VARIANTS LYS-23 AND SER-363.
PubMed=9150737; DOI=10.1007/s004390050425;
Koper J.W., Stolk R.P., de Lange P., Huizenga N.A.T.M., Molijn G.-J.,
Pols H.A.P., Grobbee D.E., Karl M., de Jong F.H., Brinkmann A.O.,
Lamberts S.W.J.;
"Lack of association between five polymorphisms in the human
glucocorticoid receptor gene and glucocorticoid resistance.";
Hum. Genet. 99:663-668(1997).
[78]
VARIANTS LYS-23; VAL-65 AND SER-363.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[79]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[80]
VARIANTS LYS-23; LEU-29; PHE-112; ASN-233 AND SER-363.
PubMed=10898924;
DOI=10.1002/1096-8628(20000612)96:3<412::AID-AJMG33>3.0.CO;2-C;
Feng J., Zheng J., Bennett W.P., Heston L.L., Jones I.R., Craddock N.,
Sommer S.S.;
"Five missense variants in the amino-terminal domain of the
glucocorticoid receptor: no association with puerperal psychosis or
schizophrenia.";
Am. J. Med. Genet. 96:412-417(2000).
[81]
VARIANTS GCCR HIS-477 AND SER-679.
PubMed=11589680; DOI=10.1046/j.1365-2265.2001.01323.x;
Ruiz M., Lind U., Gaafvels M., Eggertsen G., Carlstedt-Duke J.,
Nilsson L., Holtmann M., Stierna P., Wikstroem A.-C., Werner S.;
"Characterization of two novel mutations in the glucocorticoid
receptor gene in patients with primary cortisol resistance.";
Clin. Endocrinol. (Oxf.) 55:363-371(2001).
[82]
VARIANT SER-363.
PubMed=11344238; DOI=10.1210/jcem.86.5.7465;
Dobson M.G., Redfern C.P.F., Unwin N., Weaver J.U.;
"The N363S polymorphism of the glucocorticoid receptor: potential
contribution to central obesity in men and lack of association with
other risk factors for coronary heart disease and diabetes mellitus.";
J. Clin. Endocrinol. Metab. 86:2270-2274(2001).
[83]
CHARACTERIZATION OF VARIANT GCCR ASN-559.
PubMed=11701741; DOI=10.1210/jcem.86.11.8017;
Kino T., Stauber R.H., Resau J.H., Pavlakis G.N., Chrousos G.P.;
"Pathologic human GR mutant has a transdominant negative effect on the
wild-type GR by inhibiting its translocation into the nucleus:
importance of the ligand-binding domain for intracellular GR
trafficking.";
J. Clin. Endocrinol. Metab. 86:5600-5608(2001).
[84]
VARIANT LYS-23.
PubMed=12351458; DOI=10.2337/diabetes.51.10.3128;
van Rossum E.F.C., Koper J.W., Huizenga N.A.T.M., Uitterlinden A.G.,
Janssen J.A.M.J.L., Brinkmann A.O., Grobbee D.E., de Jong F.H.,
van Duyn C.M., Pols H.A.P., Lamberts S.W.J.;
"A polymorphism in the glucocorticoid receptor gene, which decreases
sensitivity to glucocorticoids in vivo, is associated with low insulin
and cholesterol levels.";
Diabetes 51:3128-3134(2002).
[85]
VARIANT PSEUDOHERMAPHRODITISM ALA-571.
PubMed=11932321; DOI=10.1210/jcem.87.4.8379;
Mendonca B.B., Leite M.V., de Castro M., Kino T., Elias L.L.K.,
Bachega T.A.S., Arnhold I.J.P., Chrousos G.P., Latronico A.C.;
"Female pseudohermaphroditism caused by a novel homozygous missense
mutation of the GR gene.";
J. Clin. Endocrinol. Metab. 87:1805-1809(2002).
[86]
VARIANT GCCR MET-747, AND ALTERED INTERACTION WITH THE COACTIVATOR
NCOA2.
PubMed=12050230; DOI=10.1210/jcem.87.6.8520;
Vottero A., Kino T., Combe H., Lecomte P., Chrousos G.P.;
"A novel, C-terminal dominant negative mutation of the GR causes
familial glucocorticoid resistance through abnormal interactions with
p160 steroid receptor coactivators.";
J. Clin. Endocrinol. Metab. 87:2658-2667(2002).
[87]
VARIANT LYS-23.
PubMed=15276593; DOI=10.1016/j.amjmed.2004.01.027;
van Rossum E.F.C., Feelders R.A., van den Beld A.W.,
Uitterlinden A.G., Janssen J.A.M.J.L., Ester W., Brinkmann A.O.,
Grobbee D.E., de Jong F.H., Pols H.A.P., Koper J.W., Lamberts S.W.J.;
"Association of the ER22/23EK polymorphism in the glucocorticoid
receptor gene with survival and C-reactive protein levels in elderly
men.";
Am. J. Med. 117:158-162(2004).
[88]
VARIANT LYS-23.
PubMed=15292341; DOI=10.1210/jc.2003-031422;
van Rossum E.F.C., Voorhoeve P.G., te Velde S.J., Koper J.W.,
Delemarre-van de Waal H.A., Kemper H.C.G., Lamberts S.W.J.;
"The ER22/23EK polymorphism in the glucocorticoid receptor gene is
associated with a beneficial body composition and muscle strength in
young adults.";
J. Clin. Endocrinol. Metab. 89:4004-4009(2004).
[89]
VARIANT GCCR PRO-773, CHARACTERIZATION OF VARIANT GCCR PRO-773,
INVOLVEMENT IN GCCR, FUNCTION (ISOFORM ALPHA), INTERACTION WITH GRIP1,
AND SUBCELLULAR LOCATION (ISOFORM ALPHA).
PubMed=15769988; DOI=10.1210/jc.2004-1920;
Charmandari E., Raji A., Kino T., Ichijo T., Tiulpakov A., Zachman K.,
Chrousos G.P.;
"A novel point mutation in the ligand-binding domain (LBD) of the
human glucocorticoid receptor (hGR) causing generalized glucocorticoid
resistance: the importance of the C terminus of hGR LBD in conferring
transactivational activity.";
J. Clin. Endocrinol. Metab. 90:3696-3705(2005).
[90]
VARIANTS LYS-23 AND SER-363, AND CHARACTERIZATION OF VARIANTS LYS-23
AND SER-363.
PubMed=16030164; DOI=10.1210/jc.2005-0646;
Russcher H., Smit P., van den Akker E.L., van Rossum E.F.,
Brinkmann A.O., de Jong F.H., Lamberts S.W., Koper J.W.;
"Two polymorphisms in the glucocorticoid receptor gene directly affect
glucocorticoid-regulated gene expression.";
J. Clin. Endocrinol. Metab. 90:5804-5810(2005).
[91]
VARIANT GCCR LEU-737, CHARACTERIZATION OF VARIANT GCCR LEU-737,
FUNCTION (ISOFORM ALPHA), INTERACTION WITH GRIP1, AND SUBCELLULAR
LOCATION (ISOFORM ALPHA).
PubMed=17635946; DOI=10.1210/jc.2006-2830;
Charmandari E., Kino T., Ichijo T., Jubiz W., Mejia L., Zachman K.,
Chrousos G.P.;
"A novel point mutation in helix 11 of the ligand-binding domain of
the human glucocorticoid receptor gene causing generalized
glucocorticoid resistance.";
J. Clin. Endocrinol. Metab. 92:3986-3990(2007).
[92]
VARIANT GCCR GLN-714, AND CHARACTERIZATION OF VARIANT GCCR GLN-714.
PubMed=20335448; DOI=10.1210/jc.2009-2463;
Nader N., Bachrach B.E., Hurt D.E., Gajula S., Pittman A., Lescher R.,
Kino T.;
"A novel point mutation in helix 10 of the human glucocorticoid
receptor causes generalized glucocorticoid resistance by disrupting
the structure of the ligand-binding domain.";
J. Clin. Endocrinol. Metab. 95:2281-2285(2010).
[93]
VARIANT GCCR ILE-556.
PubMed=21362280;
Zhu H.J., Dai Y.F., Wang O., Li M., Lu L., Zhao W.G., Xing X.P.,
Pan H., Li N.S., Gong F.Y.;
"Generalized glucocorticoid resistance accompanied with an
adrenocortical adenoma and caused by a novel point mutation of human
glucocorticoid receptor gene.";
Chin. Med. J. 124:551-555(2011).
[94]
CHARACTERIZATION OF VARIANT GCCR ALA-423.
PubMed=23426617; DOI=10.1210/jc.2012-3549;
Roberts M.L., Kino T., Nicolaides N.C., Hurt D.E., Katsantoni E.,
Sertedaki A., Komianou F., Kassiou K., Chrousos G.P., Charmandari E.;
"A novel point mutation in the DNA-binding domain (DBD) of the human
glucocorticoid receptor causes primary generalized glucocorticoid
resistance by disrupting the hydrophobic structure of its DBD.";
J. Clin. Endocrinol. Metab. 98:E790-E795(2013).
[95]
VARIANT GCCR GLY-575, AND CHARACTERIZATION OF VARIANT GCCR GLY-575.
PubMed=24483153; DOI=10.1210/jc.2013-3005;
Nicolaides N.C., Roberts M.L., Kino T., Braatvedt G., Hurt D.E.,
Katsantoni E., Sertedaki A., Chrousos G.P., Charmandari E.;
"A novel point mutation of the human glucocorticoid receptor gene
causes primary generalized glucocorticoid resistance through impaired
interaction with the LXXLL motif of the p160 coactivators:
dissociation of the transactivating and transreppressive activities.";
J. Clin. Endocrinol. Metab. 99:E902-E907(2014).
[96]
VARIANT GCCR ARG-726, AND CHARACTERIZATION OF VARIANT GCCR ARG-726.
PubMed=26031419; DOI=10.1111/eci.12470;
Nicolaides N.C., Geer E.B., Vlachakis D., Roberts M.L., Psarra A.M.,
Moutsatsou P., Sertedaki A., Kossida S., Charmandari E.;
"A novel mutation of the hGR gene causing Chrousos syndrome.";
Eur. J. Clin. Invest. 45:782-791(2015).
[97]
CHARACTERIZATION OF VARIANT GCCR ILE-556.
PubMed=26541474; DOI=10.1111/eci.12563;
Nicolaides N.C., Skyrla E., Vlachakis D., Psarra A.M., Moutsatsou P.,
Sertedaki A., Kossida S., Charmandari E.;
"Functional characterization of the hGRalphaT556I causing Chrousos
syndrome.";
Eur. J. Clin. Invest. 46:42-49(2016).
[98]
VARIANTS GCCR SER-477; CYS-478 AND PRO-672, CHARACTERIZATION OF
VARIANTS GCCR SER-477; CYS-478 AND CYS-478, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=27120390; DOI=10.1002/humu.23008;
Vitellius G., Fagart J., Delemer B., Amazit L., Ramos N.,
Bouligand J., Le Billan F., Castinetti F., Guiochon-Mantel A.,
Trabado S., Lombes M.;
"Three novel heterozygous point mutations of NR3C1 causing
glucocorticoid resistance.";
Hum. Mutat. 37:794-803(2016).
-!- FUNCTION: Receptor for glucocorticoids (GC) (PubMed:27120390). 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:9590696). 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 (PubMed:25775514). 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:P06537,
ECO:0000269|PubMed:25775514, ECO:0000269|PubMed:27120390,
ECO:0000269|PubMed:9590696}.
-!- FUNCTION: Isoform Alpha: Has transcriptional activation and
repression activity (PubMed:15866175, PubMed:19248771,
PubMed:20484466, PubMed:23820903, PubMed:11435610,
PubMed:15769988, PubMed:17635946, PubMed:19141540,
PubMed:21664385). Mediates glucocorticoid-induced apoptosis
(PubMed:23303127). Promotes accurate chromosome segregation during
mitosis (PubMed:25847991). May act as a tumor suppressor
(PubMed:25847991). May play a negative role in adipogenesis
through the regulation of lipolytic and antilipogenic gene
expression (By similarity). {ECO:0000250|UniProtKB:P06537,
ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15769988,
ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:17635946,
ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19248771,
ECO:0000269|PubMed:20484466, ECO:0000269|PubMed:21664385,
ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903,
ECO:0000269|PubMed:25847991}.
-!- FUNCTION: Isoform Beta: Acts as a dominant negative inhibitor of
isoform Alpha (PubMed:7769088, PubMed:8621628, PubMed:20484466).
Has intrinsic transcriptional activity independent of isoform
Alpha when both isoforms are coexpressed (PubMed:19248771,
PubMed:26711253). Loses this transcription modulator function on
its own (PubMed:20484466). Has no hormone-binding activity
(PubMed:8621628). May play a role in controlling glucose
metabolism by maintaining insulin sensitivity (By similarity).
Reduces hepatic gluconeogenesis through down-regulation of PEPCK
in an isoform Alpha-dependent manner (PubMed:26711253). Directly
regulates STAT1 expression in isoform Alpha-independent manner
(PubMed:26711253). {ECO:0000250|UniProtKB:P06537,
ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:20484466,
ECO:0000269|PubMed:26711253, ECO:0000269|PubMed:7769088,
ECO:0000269|PubMed:8621628}.
-!- FUNCTION: Isoform Alpha-2: Has lower transcriptional activation
activity than isoform Alpha. Exerts a dominant negative effect on
isoform Alpha trans-repression mechanism (PubMed:20484466).
-!- FUNCTION: Isoform GR-P: Increases activity of isoform Alpha.
{ECO:0000269|PubMed:11358809}.
-!- FUNCTION: Isoform Alpha-B: More effective than isoform Alpha in
transcriptional activation, but not repression activity.
{ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175}.
-!- FUNCTION: Isoform 10: Has transcriptional activation activity.
{ECO:0000269|PubMed:20484466}.
-!- FUNCTION: Isoform Alpha-C1: Has transcriptional activation
activity. {ECO:0000269|PubMed:15866175}.
-!- FUNCTION: Isoform Alpha-C2: Has transcriptional activation
activity. {ECO:0000269|PubMed:15866175}.
-!- FUNCTION: Isoform Alpha-C3: Has highest transcriptional activation
activity of all isoforms created by alternative initiation
(PubMed:15866175, PubMed:23820903). Has transcriptional repression
activity (PubMed:23303127). Mediates glucocorticoid-induced
apoptosis (PubMed:23303127, PubMed:23820903).
{ECO:0000269|PubMed:15866175, ECO:0000269|PubMed:23303127,
ECO:0000269|PubMed:23820903}.
-!- FUNCTION: Isoform Alpha-D1: Has transcriptional activation
activity. {ECO:0000269|PubMed:15866175}.
-!- FUNCTION: Isoform Alpha-D2: Has transcriptional activation
activity. {ECO:0000269|PubMed:15866175}.
-!- FUNCTION: Isoform Alpha-D3: Has lowest transcriptional activation
activity of all isoforms created by alternative initiation
(PubMed:15866175, PubMed:23820903). Has transcriptional repression
activity (PubMed:23303127). {ECO:0000269|PubMed:15866175,
ECO:0000269|PubMed:23303127, ECO:0000269|PubMed:23820903}.
-!- SUBUNIT: 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). Probably forms a complex composed of chaperones HSP90
and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein
TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-
chaperones STIP1/HOP and PTGES3/p23 (PubMed:29127155). Directly
interacts with UNC45A (PubMed:16478993). Binds to DNA as a
homodimer, and as heterodimer with NR3C2 or the retinoid X
receptor. Binds STAT5A and STAT5B homodimers and heterodimers (By
similarity). Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (By
similarity). Interacts with several coactivator complexes,
including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex)
and p160 coactivators such as NCOA2 and NCOA6 (PubMed:10866662,
PubMed:12151000, PubMed:12686538, PubMed:9154805, PubMed:9590696).
Interaction with BAG1 inhibits transactivation (PubMed:10477749).
Interacts with HEXIM1, PELP1 and TGFB1I1 (PubMed:12415108,
PubMed:15211577, PubMed:15941832). Interacts with NCOA1
(PubMed:9590696). Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1,
and SMARCE1 (By similarity). Interacts with CLOCK, CRY1 and CRY2
in a ligand-dependent fashion (PubMed:19141540, PubMed:21980503,
PubMed:22170608). Interacts with CIART (By similarity). Interacts
with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and this
interaction is enhanced in the presence of RWDD3 (By similarity).
Interacts with GRIP1 (PubMed:15769988, PubMed:17635946). Interacts
with NR4A3 (via nuclear receptor DNA-binding domain), represses
transcription activity of NR4A3 on the POMC promoter Nur response
element (NurRE) (PubMed:15591535). Directly interacts with PNRC2
to attract and form a complex with UPF1 and DCP1A; the interaction
leads to rapid mRNA degradation (PubMed:25775514). Interacts with
GSK3B (PubMed:18838540). Interacts with FNIP1 and FNIP2
(PubMed:27353360). Interacts (via C-terminus) with HNRNPU (via C-
terminus) (PubMed:9353307). {ECO:0000250|UniProtKB:P06536,
ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:10477749,
ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:12151000,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12686538,
ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15591535,
ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:15941832,
ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:17635946,
ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:19141540,
ECO:0000269|PubMed:21730050, ECO:0000269|PubMed:21980503,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:25775514,
ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155,
ECO:0000269|PubMed:9154805, ECO:0000269|PubMed:9353307,
ECO:0000269|PubMed:9590696}.
-!- INTERACTION:
P31749:AKT1; NbExp=5; IntAct=EBI-493507, EBI-296087;
P59598:Asxl1 (xeno); NbExp=2; IntAct=EBI-493507, EBI-5743705;
Q03135:CAV1; NbExp=2; IntAct=EBI-493507, EBI-603614;
P01730:CD4; NbExp=2; IntAct=EBI-493507, EBI-353826;
P00533:EGFR; NbExp=2; IntAct=EBI-493507, EBI-297353;
P41235:HNF4A; NbExp=2; IntAct=EBI-493507, EBI-1049011;
P07900:HSP90AA1; NbExp=7; IntAct=EBI-493507, EBI-296047;
Q6ZU52:KIAA0408; NbExp=2; IntAct=EBI-493507, EBI-739493;
P06239:LCK; NbExp=3; IntAct=EBI-493507, EBI-1348;
Q62667:Mvp (xeno); NbExp=2; IntAct=EBI-493507, EBI-918333;
P82094:TMF1; NbExp=3; IntAct=EBI-493507, EBI-949763;
-!- SUBCELLULAR LOCATION: Isoform Alpha: Cytoplasm
{ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946,
ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390,
ECO:0000269|PubMed:8621628}. Nucleus {ECO:0000269|PubMed:15769988,
ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:18838540,
ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:8621628}.
Mitochondrion {ECO:0000269|PubMed:21664385}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:25847991}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:25847991}. Note=After ligand activation,
translocates from the cytoplasm to the nucleus.
{ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390,
ECO:0000269|PubMed:8621628}.
-!- SUBCELLULAR LOCATION: Isoform Beta: Nucleus
{ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:26711253,
ECO:0000269|PubMed:8621628}. Cytoplasm
{ECO:0000269|PubMed:19248771, ECO:0000269|PubMed:26711253}.
Note=Expressed predominantly in the nucleus with some expression
also detected in the cytoplasm. {ECO:0000269|PubMed:19248771,
ECO:0000269|PubMed:26711253}.
-!- SUBCELLULAR LOCATION: Isoform Alpha-B: Nucleus
{ECO:0000269|PubMed:15866175}. Cytoplasm
{ECO:0000269|PubMed:15866175}. Note=After ligand activation,
translocates from the cytoplasm to the nucleus.
{ECO:0000269|PubMed:15866175}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=16;
Name=Alpha; Synonyms=Alpha-A, GR-alphaA;
IsoId=P04150-1; Sequence=Displayed;
Note=Predominant physiological form.
{ECO:0000269|PubMed:15866175};
Name=Beta; Synonyms=Beta-A;
IsoId=P04150-2; Sequence=VSP_003703;
Name=Alpha-2; Synonyms=Gamma;
IsoId=P04150-3; Sequence=VSP_007363;
Note=Due to a partial intron retention.;
Name=Beta-2;
IsoId=P04150-6; Sequence=VSP_007363, VSP_003703;
Note=Due to a partial intron retention.;
Name=GR-A alpha;
IsoId=P04150-5; Sequence=VSP_013340;
Note=Lacks exons 5, 6 and 7. Found in glucocorticoid-resistant
myeloma patients. {ECO:0000269|PubMed:8358712};
Name=GR-A beta;
IsoId=P04150-7; Sequence=VSP_013340, VSP_003703;
Note=Lacks exons 5, 6 and 7. {ECO:0000269|PubMed:8358712};
Name=GR-P;
IsoId=P04150-4; Sequence=Not described;
Note=Encoded by exons 2-7 plus several basepairs from the
subsequent intron region. Lacks the ligand binding domain.
Accounts for up to 10-20% of mRNAs.
{ECO:0000269|PubMed:8358712};
Name=Alpha-B; Synonyms=GR-alphaB;
IsoId=P04150-8; Sequence=VSP_018773;
Note=Produced by alternative initiation at Met-27 of isoform
Alpha. Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
Name=Beta-B;
IsoId=P04150-9; Sequence=VSP_018773, VSP_003703;
Note=Produced by alternative initiation at Met-27 of isoform
Beta. Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378, ECO:0000269|PubMed:15866175};
Name=10; Synonyms=hGRDelta313-338;
IsoId=P04150-10; Sequence=VSP_043908;
Name=Alpha-C1; Synonyms=GR-alphaC1;
IsoId=P04150-11; Sequence=VSP_058317;
Note=Produced by alternative initiation at Met-86 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
Name=Alpha-C2; Synonyms=GR-alphaC2;
IsoId=P04150-12; Sequence=VSP_058316;
Note=Produced by alternative initiation at Met-90 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
Name=Alpha-C3; Synonyms=GR-alphaC3;
IsoId=P04150-13; Sequence=VSP_058315;
Note=Produced by alternative initiation at Met-98 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
Name=Alpha-D1; Synonyms=GR-alphaD1;
IsoId=P04150-14; Sequence=VSP_058314;
Note=Produced by alternative initiation at Met-316 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
Name=Alpha-D2; Synonyms=GR-alphaD2;
IsoId=P04150-15; Sequence=VSP_058313;
Note=Produced by alternative initiation at Met-331 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
Name=Alpha-D3; Synonyms=GR-alphaD3;
IsoId=P04150-16; Sequence=VSP_058312;
Note=Produced by alternative initiation at Met-336 of isoform
Alpha. {ECO:0000269|PubMed:15866175};
-!- TISSUE SPECIFICITY: Widely expressed including bone, stomach,
lung, liver, colon, breast, ovary, pancreas and kidney
(PubMed:25847991). In the heart, detected in left and right atria,
left and right ventricles, aorta, apex, intraventricular septum,
and atrioventricular node as well as whole adult and fetal heart
(PubMed:10902803). Isoform Beta: Widely expressed including brain,
bone marrow, thymus, spleen, liver, kidney, pancreas, lung, fat,
skeletal muscle, heart, placenta and blood leukocytes
(PubMed:7769088, PubMed:8621628). Isoform Alpha-2: Expressed at
low level. {ECO:0000269|PubMed:10902803,
ECO:0000269|PubMed:25847991, ECO:0000269|PubMed:7769088,
ECO:0000269|PubMed:8621628}.
-!- INDUCTION: Isoform Alpha: Up-regulated by TNF (at protein level).
Isoform Beta: Up-regulated by TNF and becomes the predominant
isoform which may lead to glucocorticoid resistance (at protein
level). {ECO:0000269|PubMed:11381138}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain
(PubMed:3841189). The ligand-binding domain is required for
correct chromosome segregation during mitosis although ligand
binding is not required (PubMed:25847991).
{ECO:0000269|PubMed:25847991, ECO:0000269|PubMed:3841189}.
-!- PTM: Acetylation by CLOCK reduces its binding to glucocorticoid
response elements and its transcriptional activity.
{ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:21980503}.
-!- PTM: Increased proteasome-mediated degradation in response to
glucocorticoids (PubMed:11555652). Isoform Alpha-B appears to be
more susceptible to proteolytic degradation than isoform Alpha
(PubMed:11435610). {ECO:0000269|PubMed:11435610,
ECO:0000269|PubMed:11555652}.
-!- PTM: Phosphorylated in the absence of hormone; becomes
hyperphosphorylated in the presence of glucocorticoid. The Ser-
203, Ser-226 and Ser-404-phosphorylated forms are mainly
cytoplasmic, and the Ser-211-phosphorylated form is nuclear
(PubMed:12000743, PubMed:18838540). Phosphorylation at Ser-211
increases transcriptional activity (PubMed:12000743,
PubMed:18483179). Phosphorylation at Ser-203, Ser-226 and Ser-404
decreases signaling capacity (PubMed:12000743, PubMed:18483179,
PubMed:18838540). Phosphorylation at Ser-404 may protect from
glucocorticoid-induced apoptosis (PubMed:18838540).
Phosphorylation at Ser-203 and Ser-211 is not required in
regulation of chromosome segregation (PubMed:25847991). May be
dephosphorylated by PPP5C, attenuates NR3C1 action (By
similarity). {ECO:0000250|UniProtKB:P06537,
ECO:0000269|PubMed:12000743, ECO:0000269|PubMed:18483179,
ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:25847991}.
-!- PTM: Sumoylation at Lys-277 and Lys-293 negatively regulates its
transcriptional activity (PubMed:12144530). Sumoylation at Lys-703
positively regulates its transcriptional activity in the presence
of RWDD3 (By similarity). Sumoylation at Lys-277 and Lys-293 is
dispensable whereas sumoylation at Lys-703 is critical for the
stimulatory effect of RWDD3 on its transcriptional activity (By
similarity). Heat shock increases sumoylation in a RWDD3-dependent
manner (By similarity). {ECO:0000250|UniProtKB:P06536,
ECO:0000269|PubMed:12144530}.
-!- PTM: Ubiquitinated; restricts glucocorticoid-mediated
transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.
-!- POLYMORPHISM: Carriers of the 22-Glu-Lys-23 allele are relatively
more resistant to the effects of GCs with respect to the
sensitivity of the adrenal feedback mechanism than non-carriers,
resulting in a better metabolic health profile. Carriers have a
better survival than non-carriers, as well as lower serum CRP
levels. The 22-Glu-Lys-23 polymorphism is associated with a sex-
specific, beneficial body composition at young-adult age, as well
as greater muscle strength in males.
-!- DISEASE: Glucocorticoid resistance, generalized (GCCR)
[MIM:615962]: An autosomal dominant disease characterized by
increased plasma cortisol concentration and high urinary free
cortisol, resistance to adrenal suppression by dexamethasone, and
the absence of Cushing syndrome typical signs. Clinical features
include hypoglycemia, hypertension, metabolic alkalosis, chronic
fatigue and profound anxiety. {ECO:0000269|PubMed:11589680,
ECO:0000269|PubMed:11701741, ECO:0000269|PubMed:12050230,
ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:1704018,
ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:20335448,
ECO:0000269|PubMed:21362280, ECO:0000269|PubMed:23426617,
ECO:0000269|PubMed:24483153, ECO:0000269|PubMed:26031419,
ECO:0000269|PubMed:26541474, ECO:0000269|PubMed:27120390,
ECO:0000269|PubMed:7683692}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Isoform Beta: High constitutive expression by
neutrophils may provide a mechanism by which these cells escape
glucocorticoid-induced cell death and up-regulation by
proinflammatory cytokines such as IL8 further enhances their
survival in the presence of glucocorticoids during inflammation.
{ECO:0000269|PubMed:11238589}.
-!- MISCELLANEOUS: Can up- or down-modulate aggregation and nuclear
localization of expanded polyglutamine polypeptides derived from
AR and HD through specific regulation of gene expression.
Aggregation and nuclear localization of expanded polyglutamine
proteins are regulated cellular processes that can be modulated by
this receptor, a well-characterized transcriptional regulator.
{ECO:0000269|PubMed:10639135}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nr3c1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Glucocorticoid receptor entry;
URL="https://en.wikipedia.org/wiki/Glucocorticoid_receptor";
-----------------------------------------------------------------------
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EMBL; X03225; CAA26976.1; -; mRNA.
EMBL; X03348; CAA27054.1; -; mRNA.
EMBL; AH005496; AAB64353.1; -; Genomic_DNA.
EMBL; AH005496; AAB64354.1; -; Genomic_DNA.
EMBL; HQ205546; ADP91135.1; -; Genomic_DNA.
EMBL; HQ205547; ADP91138.1; -; Genomic_DNA.
EMBL; HQ205548; ADP91141.1; -; Genomic_DNA.
EMBL; HQ205549; ADP91144.1; -; Genomic_DNA.
EMBL; HQ205550; ADP91147.1; -; Genomic_DNA.
EMBL; HQ205551; ADP91150.1; -; Genomic_DNA.
EMBL; HQ205552; ADP91153.1; -; Genomic_DNA.
EMBL; HQ205553; ADP91156.1; -; Genomic_DNA.
EMBL; HQ205554; ADP91159.1; -; Genomic_DNA.
EMBL; HQ205555; ADP91162.1; -; Genomic_DNA.
EMBL; HQ205556; ADP91165.1; -; Genomic_DNA.
EMBL; HQ205557; ADP91168.1; -; Genomic_DNA.
EMBL; HQ205558; ADP91171.1; -; Genomic_DNA.
EMBL; HQ205559; ADP91174.1; -; Genomic_DNA.
EMBL; HQ205560; ADP91177.1; -; Genomic_DNA.
EMBL; HQ205561; ADP91180.1; -; Genomic_DNA.
EMBL; HQ205562; ADP91183.1; -; Genomic_DNA.
EMBL; HQ205563; ADP91186.1; -; Genomic_DNA.
EMBL; HQ205564; ADP91189.1; -; Genomic_DNA.
EMBL; HQ205565; ADP91192.1; -; Genomic_DNA.
EMBL; HQ205566; ADP91195.1; -; Genomic_DNA.
EMBL; HQ205567; ADP91198.1; -; Genomic_DNA.
EMBL; HQ205568; ADP91201.1; -; Genomic_DNA.
EMBL; HQ205569; ADP91204.1; -; Genomic_DNA.
EMBL; HQ205570; ADP91207.1; -; Genomic_DNA.
EMBL; HQ205571; ADP91210.1; -; Genomic_DNA.
EMBL; HQ205572; ADP91213.1; -; Genomic_DNA.
EMBL; HQ205573; ADP91216.1; -; Genomic_DNA.
EMBL; HQ205574; ADP91219.1; -; Genomic_DNA.
EMBL; HQ205575; ADP91222.1; -; Genomic_DNA.
EMBL; HQ205576; ADP91225.1; -; Genomic_DNA.
EMBL; HQ205577; ADP91228.1; -; Genomic_DNA.
EMBL; HQ205578; ADP91231.1; -; Genomic_DNA.
EMBL; HQ205579; ADP91234.1; -; Genomic_DNA.
EMBL; HQ205580; ADP91237.1; -; Genomic_DNA.
EMBL; HQ205581; ADP91240.1; -; Genomic_DNA.
EMBL; HQ205582; ADP91243.1; -; Genomic_DNA.
EMBL; HQ205583; ADP91246.1; -; Genomic_DNA.
EMBL; HQ205584; ADP91249.1; -; Genomic_DNA.
EMBL; HQ205585; ADP91252.1; -; Genomic_DNA.
EMBL; AM183262; CAJ65924.1; -; mRNA.
EMBL; HQ450643; AED99114.1; -; mRNA.
EMBL; U01351; AAA16603.1; -; mRNA.
EMBL; AK223594; BAD97314.1; -; mRNA.
EMBL; BX640610; CAE45716.1; -; mRNA.
EMBL; AY436590; AAQ97180.1; -; Genomic_DNA.
EMBL; EU332858; ABY87547.1; -; Genomic_DNA.
EMBL; AC005601; AAC34207.1; -; Genomic_DNA.
EMBL; AC004782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61872.1; -; Genomic_DNA.
EMBL; CH471062; EAW61873.1; -; Genomic_DNA.
EMBL; BC015610; AAH15610.1; -; mRNA.
EMBL; M69104; AAA88049.1; -; Genomic_DNA.
EMBL; AH002750; AAA53151.1; -; Genomic_DNA.
EMBL; S68378; AAB20466.1; -; Genomic_DNA.
CCDS; CCDS34258.1; -. [P04150-3]
CCDS; CCDS4278.1; -. [P04150-1]
CCDS; CCDS47298.1; -. [P04150-2]
PIR; A93370; QRHUGA.
PIR; B93370; QRHUGB.
RefSeq; NP_000167.1; NM_000176.2. [P04150-1]
RefSeq; NP_001018084.1; NM_001018074.1. [P04150-1]
RefSeq; NP_001018085.1; NM_001018075.1. [P04150-1]
RefSeq; NP_001018086.1; NM_001018076.1. [P04150-1]
RefSeq; NP_001018087.1; NM_001018077.1. [P04150-1]
RefSeq; NP_001018661.1; NM_001020825.1. [P04150-2]
RefSeq; NP_001019265.1; NM_001024094.1. [P04150-3]
RefSeq; NP_001191187.1; NM_001204258.1. [P04150-8]
RefSeq; NP_001191188.1; NM_001204259.1. [P04150-11]
RefSeq; NP_001191189.1; NM_001204260.1. [P04150-12]
RefSeq; NP_001191190.1; NM_001204261.1. [P04150-13]
RefSeq; NP_001191191.1; NM_001204262.1. [P04150-14]
RefSeq; NP_001191192.1; NM_001204263.1. [P04150-15]
RefSeq; NP_001191193.1; NM_001204264.1. [P04150-16]
RefSeq; XP_005268476.1; XM_005268419.3. [P04150-3]
RefSeq; XP_005268477.1; XM_005268420.4. [P04150-3]
RefSeq; XP_005268479.1; XM_005268422.3. [P04150-3]
RefSeq; XP_005268480.1; XM_005268423.3. [P04150-3]
RefSeq; XP_016864886.1; XM_017009397.1. [P04150-1]
RefSeq; XP_016864887.1; XM_017009398.1. [P04150-1]
UniGene; Hs.122926; -.
PDB; 1M2Z; X-ray; 2.50 A; A/D=521-777.
PDB; 1NHZ; X-ray; 2.30 A; A=500-777.
PDB; 1P93; X-ray; 2.70 A; A/B/C/D=500-777.
PDB; 3BQD; X-ray; 2.50 A; A=525-777.
PDB; 3CLD; X-ray; 2.84 A; A/B=521-777.
PDB; 3E7C; X-ray; 2.15 A; A/B=521-777.
PDB; 3H52; X-ray; 2.80 A; A/B/C/D=528-777.
PDB; 3K22; X-ray; 2.10 A; A/B=521-777.
PDB; 3K23; X-ray; 3.00 A; A/B/C=521-777.
PDB; 4CSJ; X-ray; 2.30 A; A=500-777.
PDB; 4HN5; X-ray; 1.90 A; A/B=417-506.
PDB; 4HN6; X-ray; 2.55 A; A/B=417-506.
PDB; 4LSJ; X-ray; 2.35 A; A=522-777.
PDB; 4MDD; X-ray; 2.40 A; A/B=522-777.
PDB; 4P6W; X-ray; 1.95 A; A=526-777.
PDB; 4P6X; X-ray; 2.50 A; A/C/E/G/I/K=523-777.
PDB; 4UDC; X-ray; 2.50 A; A=500-777.
PDB; 4UDD; X-ray; 1.80 A; A=500-777.
PDB; 5CBX; X-ray; 2.00 A; A/B/E/F=415-495.
PDB; 5CBY; X-ray; 2.00 A; A/B=415-495.
PDB; 5CBZ; X-ray; 2.20 A; A/B/E/F=419-495.
PDB; 5CC1; X-ray; 2.30 A; A/B/W/X=417-506.
PDB; 5E69; X-ray; 1.85 A; A/B=417-506.
PDB; 5E6A; X-ray; 2.20 A; A/B=417-506.
PDB; 5E6B; X-ray; 2.25 A; A/B=417-506.
PDB; 5E6C; X-ray; 2.20 A; A/B=417-506.
PDB; 5E6D; X-ray; 2.40 A; A/B=417-506.
PDB; 5EMC; X-ray; 2.30 A; A/B=411-500.
PDB; 5EMP; X-ray; 2.30 A; A/B=411-500.
PDB; 5EMQ; X-ray; 2.30 A; A/B=411-500.
PDB; 5G3J; X-ray; 2.40 A; A=500-777.
PDB; 5G5W; X-ray; 2.20 A; A=500-777.
PDB; 5NFP; X-ray; 2.10 A; A=500-777.
PDB; 5NFT; X-ray; 2.30 A; A=500-777.
PDB; 5UC3; X-ray; 2.01 A; A/B=522-777.
PDB; 5VA0; X-ray; 2.29 A; A/B=419-490.
PDB; 5VA7; X-ray; 2.15 A; A/B=419-488.
PDB; 6EL6; X-ray; 2.40 A; A=500-777.
PDB; 6EL7; X-ray; 2.18 A; A=500-777.
PDB; 6EL9; X-ray; 2.19 A; A=500-777.
PDBsum; 1M2Z; -.
PDBsum; 1NHZ; -.
PDBsum; 1P93; -.
PDBsum; 3BQD; -.
PDBsum; 3CLD; -.
PDBsum; 3E7C; -.
PDBsum; 3H52; -.
PDBsum; 3K22; -.
PDBsum; 3K23; -.
PDBsum; 4CSJ; -.
PDBsum; 4HN5; -.
PDBsum; 4HN6; -.
PDBsum; 4LSJ; -.
PDBsum; 4MDD; -.
PDBsum; 4P6W; -.
PDBsum; 4P6X; -.
PDBsum; 4UDC; -.
PDBsum; 4UDD; -.
PDBsum; 5CBX; -.
PDBsum; 5CBY; -.
PDBsum; 5CBZ; -.
PDBsum; 5CC1; -.
PDBsum; 5E69; -.
PDBsum; 5E6A; -.
PDBsum; 5E6B; -.
PDBsum; 5E6C; -.
PDBsum; 5E6D; -.
PDBsum; 5EMC; -.
PDBsum; 5EMP; -.
PDBsum; 5EMQ; -.
PDBsum; 5G3J; -.
PDBsum; 5G5W; -.
PDBsum; 5NFP; -.
PDBsum; 5NFT; -.
PDBsum; 5UC3; -.
PDBsum; 5VA0; -.
PDBsum; 5VA7; -.
PDBsum; 6EL6; -.
PDBsum; 6EL7; -.
PDBsum; 6EL9; -.
DisProt; DP00030; -.
ProteinModelPortal; P04150; -.
SMR; P04150; -.
BioGrid; 109165; 225.
CORUM; P04150; -.
DIP; DIP-576N; -.
ELM; P04150; -.
IntAct; P04150; 76.
MINT; P04150; -.
STRING; 9606.ENSP00000231509; -.
BindingDB; P04150; -.
ChEMBL; CHEMBL2034; -.
DrugBank; DB00240; Alclometasone.
DrugBank; DB00288; Amcinonide.
DrugBank; DB00394; Beclomethasone dipropionate.
DrugBank; DB00443; Betamethasone.
DrugBank; DB01222; Budesonide.
DrugBank; DB01410; Ciclesonide.
DrugBank; DB01013; Clobetasol propionate.
DrugBank; DB13158; Clobetasone.
DrugBank; DB00838; Clocortolone.
DrugBank; DB01380; Cortisone acetate.
DrugBank; DB01260; Desonide.
DrugBank; DB00547; Desoximetasone.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00223; Diflorasone.
DrugBank; DB06781; Difluprednate.
DrugBank; DB00687; Fludrocortisone.
DrugBank; DB00663; Flumethasone.
DrugBank; DB00180; Flunisolide.
DrugBank; DB00591; Fluocinolone Acetonide.
DrugBank; DB01047; Fluocinonide.
DrugBank; DB00324; Fluorometholone.
DrugBank; DB01185; Fluoxymesterone.
DrugBank; DB00846; Flurandrenolide.
DrugBank; DB08906; Fluticasone furoate.
DrugBank; DB00588; Fluticasone Propionate.
DrugBank; DB00769; Hydrocortamate.
DrugBank; DB00741; Hydrocortisone.
DrugBank; DB00873; Loteprednol.
DrugBank; DB00253; Medrysone.
DrugBank; DB00351; Megestrol acetate.
DrugBank; DB00959; Methylprednisolone.
DrugBank; DB00834; Mifepristone.
DrugBank; DB00764; Mometasone.
DrugBank; DB05423; ORG-34517.
DrugBank; DB01384; Paramethasone.
DrugBank; DB01130; Prednicarbate.
DrugBank; DB00860; Prednisolone.
DrugBank; DB00635; Prednisone.
DrugBank; DB00896; Rimexolone.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00620; Triamcinolone.
DrugBank; DB08867; Ulipristal.
DrugBank; DB00596; Ulobetasol.
GuidetoPHARMACOLOGY; 625; -.
iPTMnet; P04150; -.
PhosphoSitePlus; P04150; -.
BioMuta; NR3C1; -.
DMDM; 121069; -.
EPD; P04150; -.
PaxDb; P04150; -.
PeptideAtlas; P04150; -.
PRIDE; P04150; -.
ProteomicsDB; 51657; -.
ProteomicsDB; 51658; -. [P04150-10]
ProteomicsDB; 51659; -. [P04150-2]
ProteomicsDB; 51660; -. [P04150-3]
ProteomicsDB; 51661; -. [P04150-5]
ProteomicsDB; 51662; -. [P04150-6]
ProteomicsDB; 51663; -. [P04150-7]
ProteomicsDB; 51664; -. [P04150-8]
ProteomicsDB; 51665; -. [P04150-9]
DNASU; 2908; -.
Ensembl; ENST00000231509; ENSP00000231509; ENSG00000113580. [P04150-3]
Ensembl; ENST00000343796; ENSP00000343205; ENSG00000113580. [P04150-1]
Ensembl; ENST00000394464; ENSP00000377977; ENSG00000113580. [P04150-1]
Ensembl; ENST00000394466; ENSP00000377979; ENSG00000113580. [P04150-3]
Ensembl; ENST00000415690; ENSP00000387672; ENSG00000113580. [P04150-2]
Ensembl; ENST00000424646; ENSP00000405282; ENSG00000113580. [P04150-10]
Ensembl; ENST00000503201; ENSP00000427672; ENSG00000113580. [P04150-1]
Ensembl; ENST00000504572; ENSP00000422518; ENSG00000113580. [P04150-3]
GeneID; 2908; -.
KEGG; hsa:2908; -.
UCSC; uc003lmy.4; human. [P04150-1]
CTD; 2908; -.
DisGeNET; 2908; -.
EuPathDB; HostDB:ENSG00000113580.14; -.
GeneCards; NR3C1; -.
HGNC; HGNC:7978; NR3C1.
HPA; CAB010435; -.
HPA; HPA004248; -.
MalaCards; NR3C1; -.
MIM; 138040; gene.
MIM; 615962; phenotype.
neXtProt; NX_P04150; -.
OpenTargets; ENSG00000113580; -.
Orphanet; 786; Glucocorticoid resistance.
PharmGKB; PA181; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOGENOM; HOG000037950; -.
HOVERGEN; HBG007583; -.
InParanoid; P04150; -.
KO; K05771; -.
OMA; QSTFDIL; -.
PhylomeDB; P04150; -.
TreeFam; TF106510; -.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-8849473; PTK6 Expression.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
SignaLink; P04150; -.
SIGNOR; P04150; -.
ChiTaRS; NR3C1; human.
EvolutionaryTrace; P04150; -.
GeneWiki; Glucocorticoid_receptor; -.
GenomeRNAi; 2908; -.
PRO; PR:P04150; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113580; Expressed in 249 organ(s), highest expression level in endothelial cell.
CleanEx; HS_NR3C1; -.
ExpressionAtlas; P04150; baseline and differential.
Genevisible; P04150; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; TAS:ProtInc.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0001047; F:core promoter binding; IDA:CAFA.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0004883; F:glucocorticoid receptor activity; TAS:ProtInc.
GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0038050; F:RNA polymerase II transcription factor activity, glucocorticoid-activated sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; IDA:UniProtKB.
GO; GO:0032183; F:SUMO binding; IPI:CAFA.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IMP:CAFA.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:CAFA.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IDA:CAFA.
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; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF02155; GCR; 1.
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; 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; Alternative initiation;
Alternative splicing; Apoptosis; Cell cycle; Cell division;
Chromatin regulator; Chromosome partition; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; DNA-binding;
Isopeptide bond; Lipid-binding; Metal-binding; Methylation;
Mitochondrion; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
Pseudohermaphroditism; Receptor; Reference proteome; RNA-binding;
Steroid-binding; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 777 Glucocorticoid receptor.
/FTId=PRO_0000019937.
DOMAIN 524 758 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 418 493 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 421 441 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 457 476 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 420 Modulating.
REGION 98 115 Required for high transcriptional
activity of isoform Alpha-C3.
{ECO:0000269|PubMed:23820903}.
REGION 485 777 Interaction with CLOCK.
REGION 487 523 Hinge.
REGION 532 697 Interaction with CRY1.
{ECO:0000269|PubMed:22170608}.
COMPBIAS 399 418 Glu/Pro/Ser/Thr-rich (PEST region).
MOD_RES 8 8 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12000743,
ECO:0000269|PubMed:18483179,
ECO:0000269|PubMed:25847991}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000269|PubMed:12000743,
ECO:0000269|PubMed:18483179,
ECO:0000269|PubMed:25847991}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:18483179}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 404 404 Phosphoserine; by GSK3-beta.
{ECO:0000269|PubMed:18838540}.
MOD_RES 480 480 N6-acetyllysine.
{ECO:0000269|PubMed:19141540}.
MOD_RES 492 492 N6-acetyllysine.
{ECO:0000269|PubMed:19141540}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000269|PubMed:19141540}.
MOD_RES 495 495 N6-acetyllysine.
{ECO:0000269|PubMed:19141540}.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:12144530}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:12144530}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P06537}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12144530}.
VAR_SEQ 1 335 Missing (in isoform Alpha-D3).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058312.
VAR_SEQ 1 330 Missing (in isoform Alpha-D2).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058313.
VAR_SEQ 1 315 Missing (in isoform Alpha-D1).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058314.
VAR_SEQ 1 97 Missing (in isoform Alpha-C3).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058315.
VAR_SEQ 1 89 Missing (in isoform Alpha-C2).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058316.
VAR_SEQ 1 85 Missing (in isoform Alpha-C1).
{ECO:0000269|PubMed:15866175}.
/FTId=VSP_058317.
VAR_SEQ 1 26 Missing (in isoform Alpha-B and isoform
Beta-B). {ECO:0000305}.
/FTId=VSP_018773.
VAR_SEQ 313 338 Missing (in isoform 10).
{ECO:0000303|PubMed:17404046}.
/FTId=VSP_043908.
VAR_SEQ 451 451 G -> GR (in isoform Alpha-2 and isoform
Beta-2). {ECO:0000303|Ref.6}.
/FTId=VSP_007363.
VAR_SEQ 491 674 Missing (in isoform GR-A alpha and
isoform GR-A beta). {ECO:0000305}.
/FTId=VSP_013340.
VAR_SEQ 728 777 VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGN
IKKLLFHQK -> NVMWLKPESTSHTLI (in isoform
Beta, isoform Beta-B, isoform Beta-2 and
isoform GR-A beta).
{ECO:0000303|PubMed:2867473}.
/FTId=VSP_003703.
VARIANT 23 23 R -> K (polymorphism; reduces
transactivation activity; does not affect
transrepression activity; dbSNP:rs6190).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10898924,
ECO:0000269|PubMed:12351458,
ECO:0000269|PubMed:15276593,
ECO:0000269|PubMed:15292341,
ECO:0000269|PubMed:16030164,
ECO:0000269|PubMed:9150737,
ECO:0000269|Ref.9}.
/FTId=VAR_014140.
VARIANT 29 29 F -> L (in dbSNP:rs148102613).
{ECO:0000269|PubMed:10898924}.
/FTId=VAR_015628.
VARIANT 65 65 F -> V (in dbSNP:rs6192).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.9}.
/FTId=VAR_014622.
VARIANT 72 72 N -> D (polymorphism; associated in cis
with A-321 and S-766 in one individual;
doubles transactivation potential).
{ECO:0000269|PubMed:21701417}.
/FTId=VAR_075797.
VARIANT 112 112 L -> F (in dbSNP:rs542110718).
{ECO:0000269|PubMed:10898924}.
/FTId=VAR_015629.
VARIANT 233 233 D -> N. {ECO:0000269|PubMed:10898924}.
/FTId=VAR_015630.
VARIANT 321 321 V -> A (polymorphism; associated in cis
with D-72 and S-766 in one individual;
doubles transactivation potential).
{ECO:0000269|PubMed:21701417}.
/FTId=VAR_075798.
VARIANT 363 363 N -> S (enhances transactivation
activity; does not affect transrepression
activity; may increase sensitivity to
exogenously administered glucocorticoids;
may contribute to central obesity in men
and show lack of association with other
risk factors for coronary heart disease
and diabetes mellitus; dbSNP:rs56149945).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10898924,
ECO:0000269|PubMed:11344238,
ECO:0000269|PubMed:16030164,
ECO:0000269|PubMed:8445027,
ECO:0000269|PubMed:9150737}.
/FTId=VAR_004675.
VARIANT 421 421 C -> Y. {ECO:0000269|PubMed:8358735}.
/FTId=VAR_015631.
VARIANT 423 423 V -> A (in GCCR; unknown pathological
significance; reduces transactivation
activity; delays nuclear translocation;
does not exert a dominant negative
effect; impairs DNA binding).
{ECO:0000269|PubMed:23426617}.
/FTId=VAR_075799.
VARIANT 477 477 R -> H (in GCCR; dbSNP:rs104893913).
{ECO:0000269|PubMed:11589680}.
/FTId=VAR_013472.
VARIANT 477 477 R -> S (in GCCR; loss of DNA-binding and
of transactivation activity; incomplete
dexamethasone-induced translocation to
the nucleus; no effect on dexamethasone-
binding affinity compared with wild-
type). {ECO:0000269|PubMed:27120390}.
/FTId=VAR_077143.
VARIANT 478 478 Y -> C (in GCCR; decreased DNA-binding
and transactivation activity; incomplete
dexamethasone-induced translocation to
the nucleus; no effect on dexamethasone-
binding affinity compared with wild-
type). {ECO:0000269|PubMed:27120390}.
/FTId=VAR_077144.
VARIANT 556 556 T -> I (in GCCR; reduces transactivation
activity; enhances transrepression
activity; reduces affinity for ligand;
delays nuclear translocation; does not
exert a dominant negative effect; does
not impair DNA binding).
{ECO:0000269|PubMed:21362280,
ECO:0000269|PubMed:26541474}.
/FTId=VAR_075800.
VARIANT 559 559 I -> N (in GCCR; interferes with
translocation to the nucleus and thereby
strongly reduces transcription
activation; is equally impaired in
nuclear export; acts as dominant negative
mutant; dbSNP:rs104893909).
{ECO:0000269|PubMed:11701741}.
/FTId=VAR_015632.
VARIANT 571 571 V -> A (in pseudohermaphroditism; female
with hypokalemia due to glucocorticoid
resistance; 6-fold reduction in binding
affinity compared with the wild-type
receptor; dbSNP:rs104893911).
{ECO:0000269|PubMed:11932321}.
/FTId=VAR_025014.
VARIANT 575 575 V -> G (in GCCR; unknown pathological
significance; reduces transactivation
activity; enhances transrepression
activity; reduces affinity for ligand;
delays nuclear translocation; does not
exert a dominant negative effect; does
not impair DNA binding).
{ECO:0000269|PubMed:24483153}.
/FTId=VAR_075801.
VARIANT 641 641 D -> V (in GCCR; dbSNP:rs104893908).
{ECO:0000269|PubMed:1704018}.
/FTId=VAR_004676.
VARIANT 672 672 L -> P (in GCCR; loss of dexamethasone-
binding, dexamethasone-induced
translocation to the nucleus and of
transactivation activity).
{ECO:0000269|PubMed:27120390}.
/FTId=VAR_077145.
VARIANT 679 679 G -> S (in GCCR; has 50% binding
affinity; dbSNP:rs104893914).
{ECO:0000269|PubMed:11589680}.
/FTId=VAR_013473.
VARIANT 714 714 R -> Q (in GCCR; unknown pathological
significance; reduces transactivation;
reduces affinity for ligand; exerts a
dominant negative effect; does not impair
DNA binding).
{ECO:0000269|PubMed:20335448}.
/FTId=VAR_075802.
VARIANT 726 726 H -> R (in GCCR; unknown pathological
significance; reduces transactivation and
transrepression activity; reduces
affinity for ligand; delays nuclear
translocation; does not impair DNA
binding). {ECO:0000269|PubMed:26031419}.
/FTId=VAR_075803.
VARIANT 729 729 V -> I (in GCCR; dbSNP:rs1027058734).
{ECO:0000269|PubMed:7683692}.
/FTId=VAR_004677.
VARIANT 737 737 F -> L (in GCCR; reduces transactivation
of the glucocorticoid-inducible tumor
virus promoter; reduces affinity for
ligand; delays its nuclear translocation;
acts as dominant negative mutant;
dbSNP:rs121909727).
{ECO:0000269|PubMed:17635946}.
/FTId=VAR_071935.
VARIANT 747 747 I -> M (in GCCR; alters interaction with
NCOA2 and strongly reduces transcription
activation; acts as dominant negative
mutant; dbSNP:rs104893910).
{ECO:0000269|PubMed:12050230}.
/FTId=VAR_015633.
VARIANT 753 753 L -> F (in dbSNP:rs121909726).
{ECO:0000269|PubMed:8316249,
ECO:0000269|PubMed:8358735}.
/FTId=VAR_004678.
VARIANT 766 766 N -> S (polymorphism; associated in cis
with D-72 and A-321 in one individual;
doubles transactivation potential).
{ECO:0000269|PubMed:21701417}.
/FTId=VAR_075804.
VARIANT 773 773 L -> P (in GCCR; reduces transactivation
of the glucocorticoid-inducible tumor
virus promoter; reduces affinity for
ligand; delays its nuclear translocation;
acts as dominant negative mutant;
dbSNP:rs104893912).
{ECO:0000269|PubMed:15769988}.
/FTId=VAR_071936.
MUTAGEN 1 1 M->T: Abolishes expression of A-type
isoforms. {ECO:0000269|PubMed:11435610,
ECO:0000269|PubMed:15866175}.
MUTAGEN 27 27 M->T: Abolishes expression of B-type
isoforms. {ECO:0000269|PubMed:11435610,
ECO:0000269|PubMed:15866175}.
MUTAGEN 86 86 M->I: Abolishes expression of C-type
isoforms; when associated with I-90 and
I-98. {ECO:0000269|PubMed:15866175}.
MUTAGEN 90 90 M->I: Abolishes expression of C-type
isoforms; when associated with I-86 and
I-98. {ECO:0000269|PubMed:15866175}.
MUTAGEN 98 98 M->I: Abolishes expression of C-type
isoforms; when associated with I-86 and
I-90. {ECO:0000269|PubMed:15866175}.
MUTAGEN 101 101 D->A: Reduces transcription activation
activity of isoform Alpha-C3 by half.
{ECO:0000269|PubMed:23820903}.
MUTAGEN 101 101 D->K: Reduces transcription activation
activity of isoform Alpha-C3 by half.
Suppresses apoptosis-inducing activity of
isoform Alpha-C3. Impairs recruitment of
selected coregulators onto DNA binding
sites. {ECO:0000269|PubMed:23820903}.
MUTAGEN 106 107 QQ->LL: Reduces activity of isoform
Alpha-C3 by half.
{ECO:0000269|PubMed:23820903}.
MUTAGEN 113 114 SS->AA: Does not affect the activity of
isoform Alpha-C3.
{ECO:0000269|PubMed:23820903}.
MUTAGEN 191 191 F->D: Reduces transactivation by the ADA
complex. {ECO:0000269|PubMed:9154805}.
MUTAGEN 193 193 I->D: Reduces transactivation by the ADA
complex. {ECO:0000269|PubMed:9154805}.
MUTAGEN 194 194 L->A: Strongly reduces transactivation by
the ADA complex; when associated with V-
224 and F-225.
{ECO:0000269|PubMed:9154805}.
MUTAGEN 197 197 L->E: Reduces transactivation by the ADA
complex. {ECO:0000269|PubMed:9154805}.
MUTAGEN 211 211 S->A: Reduces expression of target genes
IGFBP1 and IRF8.
{ECO:0000269|PubMed:18483179}.
MUTAGEN 213 213 W->A: Strongly reduces transactivation by
the ADA complex.
{ECO:0000269|PubMed:9154805}.
MUTAGEN 224 224 L->V: Strongly reduces transactivation by
the ADA complex; when associated with A-
194 and F-225.
{ECO:0000269|PubMed:9154805}.
MUTAGEN 225 225 L->F: Strongly reduces transactivation by
the ADA complex; when associated with A-
194 and V-224.
{ECO:0000269|PubMed:9154805}.
MUTAGEN 226 226 S->A: Abolishes phosphorylation and
enhances transcriptional activation.
{ECO:0000269|PubMed:18483179}.
MUTAGEN 235 235 F->L: Strongly reduces transactivation by
the ADA complex; when associated with V-
236. {ECO:0000269|PubMed:9154805}.
MUTAGEN 236 236 L->V: Strongly reduces transactivation by
the ADA complex; when associated with L-
235. {ECO:0000269|PubMed:9154805}.
MUTAGEN 277 277 K->R: Strongly reduces sumoylation.
Almost complete loss of sumoylation; when
associated with R-293.
{ECO:0000269|PubMed:12144530}.
MUTAGEN 293 293 K->R: Strongly reduces sumoylation.
Almost complete loss of sumoylation; when
associated with R-277.
{ECO:0000269|PubMed:12144530}.
MUTAGEN 316 316 M->I: Abolishes expression of D-type
isoforms; when associated with I-331 and
I-336. {ECO:0000269|PubMed:15866175}.
MUTAGEN 331 331 M->I: Abolishes expression of D-type
isoforms; when associated with I-316 and
I-336. {ECO:0000269|PubMed:15866175}.
MUTAGEN 336 336 M->I: Abolishes expression of D-type
isoforms; when associated with I-316 and
I-331. {ECO:0000269|PubMed:15866175}.
MUTAGEN 404 404 S->A: Abolishes phosphorylation. Does not
affect translocation to the nucleus
following ligand stimulation. Increases
protein half-life and transcriptional
repressor activity. Alters repertoire of
regulated genes. Increases cell death.
{ECO:0000269|PubMed:18838540}.
MUTAGEN 404 404 S->D: Does not affect translocation to
the nucleus following ligand stimulation.
{ECO:0000269|PubMed:18838540}.
MUTAGEN 480 480 K->A: Decrease in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer. Complete loss in acetylation
and in repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-492;
A-494 and A-495.
{ECO:0000269|PubMed:19141540}.
MUTAGEN 492 492 K->A: Decrease in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer. Complete loss in acetylation
and in repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-480;
A-494 and A-495.
{ECO:0000269|PubMed:19141540}.
MUTAGEN 494 494 K->A: Decrease in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-495.
Complete loss in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-480;
A-492 and A-495.
{ECO:0000269|PubMed:19141540}.
MUTAGEN 495 495 K->A: Decrease in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-494.
Complete loss in acetylation and in
repression of its transcriptional
activity by CLOCK-ARNTL/BMAL1
heterodimer; when associated with A-480;
A-492 and A-494.
{ECO:0000269|PubMed:19141540}.
MUTAGEN 585 585 R->A: Reduces activation mediated by
ligand binding domain; when associated
with A-590.
{ECO:0000269|PubMed:12151000}.
MUTAGEN 590 590 D->A: Reduces activation mediated by
ligand binding domain; when associated
with A-585.
{ECO:0000269|PubMed:12151000}.
MUTAGEN 602 602 F->S: Increases solubility. No effect on
transactivation by dexamethasone.
{ECO:0000269|PubMed:12151000}.
MUTAGEN 625 625 P->A: Decreases transactivation by
dexamethasone by 95%.
{ECO:0000269|PubMed:12151000}.
MUTAGEN 628 628 I->A: Decreases dimerization and
transactivation by dexamethasone; when
associated with S-602.
{ECO:0000269|PubMed:12151000}.
MUTAGEN 703 703 K->R: Slightly reduces sumoylation.
Inhibits the stimulatory effect of RWDD3
on its transcriptional activity.
{ECO:0000269|PubMed:12144530,
ECO:0000269|PubMed:23508108}.
CONFLICT 399 399 R -> G (in Ref. 7; BAD97314).
{ECO:0000305}.
CONFLICT 754 754 A -> T (in Ref. 7; BAD97314).
{ECO:0000305}.
TURN 422 424 {ECO:0000244|PDB:5E69}.
STRAND 430 432 {ECO:0000244|PDB:5E69}.
STRAND 435 437 {ECO:0000244|PDB:5E69}.
HELIX 439 450 {ECO:0000244|PDB:5E69}.
STRAND 458 461 {ECO:0000244|PDB:5E69}.
TURN 467 472 {ECO:0000244|PDB:5E69}.
HELIX 474 484 {ECO:0000244|PDB:5E69}.
TURN 525 527 {ECO:0000244|PDB:1M2Z}.
HELIX 532 538 {ECO:0000244|PDB:4UDD}.
STRAND 550 552 {ECO:0000244|PDB:3K22}.
HELIX 556 579 {ECO:0000244|PDB:4UDD}.
HELIX 584 586 {ECO:0000244|PDB:4UDD}.
HELIX 589 615 {ECO:0000244|PDB:4UDD}.
STRAND 617 619 {ECO:0000244|PDB:4P6W}.
STRAND 621 624 {ECO:0000244|PDB:4UDD}.
STRAND 627 629 {ECO:0000244|PDB:4UDD}.
HELIX 631 634 {ECO:0000244|PDB:4UDD}.
HELIX 639 655 {ECO:0000244|PDB:4UDD}.
HELIX 660 671 {ECO:0000244|PDB:4UDD}.
STRAND 673 675 {ECO:0000244|PDB:4UDD}.
HELIX 683 702 {ECO:0000244|PDB:4UDD}.
STRAND 704 706 {ECO:0000244|PDB:4P6W}.
HELIX 708 741 {ECO:0000244|PDB:4UDD}.
HELIX 743 745 {ECO:0000244|PDB:4UDD}.
HELIX 751 765 {ECO:0000244|PDB:4UDD}.
STRAND 769 771 {ECO:0000244|PDB:5UC3}.
SEQUENCE 777 AA; 85659 MW; C5C90C9A5DD16AAB CRC64;
MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV ASQSDSKQRR
LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI SLSSGETDLK
LLEESIANLN RSTSVPENPK SSASTAVSAA PTEKEFPKTH SDVSSEQQHL KGQTGTNGGN
VKLYTTDQST FDILQDLEFS SGSPGKETNE SPWRSDLLID ENCLLSPLAG EDDSFLLEGN
SNEDCKPLIL PDTKPKIKDN GDLVLSSPSN VTLPQVKTEK EDFIELCTPG VIKQEKLGTV
YCQASFPGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI FNVIPPIPVG
SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP DVSSPPSSSS TATTGPPPKL
CLVCSDEASG CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRYRK
CLQAGMNLEA RKTKKKIKGI QQATTGVSQE TSENPGNKTI VPATLPQLTP TLVSLLEVIE
PEVLYAGYDS SVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW
MFLMAFALGW RSYRQSSANL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS SELHRLQVSY
EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA IVKREGNSSQ NWQRFYQLTK
LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP EMLAEIITNQ IPKYSNGNIK KLLFHQK


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