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

 GCR_MOUSE               Reviewed;         783 AA.
P06537; E0ZPU5; Q61628; Q61629;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
26-FEB-2020, entry version 214.
RecName: Full=Glucocorticoid receptor;
Short=GR;
AltName: Full=Nuclear receptor subfamily 3 group C member 1;
Name=Nr3c1; Synonyms=Grl, Grl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3780669; DOI=10.1002/j.1460-2075.1986.tb04529.x;
Danielsen M., Northrop J.P., Ringold G.M.;
"The mouse glucocorticoid receptor: mapping of functional domains by
cloning, sequencing and expression of wild-type and mutant receptor
proteins.";
EMBO J. 5:2513-2522(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=20660300; DOI=10.1210/me.2009-0411;
Hinds T.D. Jr., Ramakrishnan S., Cash H.A., Stechschulte L.A., Heinrich G.,
Najjar S.M., Sanchez E.R.;
"Discovery of glucocorticoid receptor-beta in mice with a role in
metabolism.";
Mol. Endocrinol. 24:1715-1727(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-755 (ISOFORMS 1 AND 2).
PubMed=2911477; DOI=10.1093/nar/17.1.445;
Nohno T., Kasai Y., Saito T.;
"Novel cDNA sequence possibly generated by alternative splicing of a mouse
glucocorticoid receptor gene transcript from Shionogi carcinoma 115.";
Nucleic Acids Res. 17:445-445(1989).
[4]
GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
PubMed=2702670;
Vedeckis W.V., Ali M., Allen H.R.;
"Regulation of glucocorticoid receptor protein and mRNA levels.";
Cancer Res. 49:2295-2302(1989).
[5]
PHOSPHORYLATION AT SER-122; SER-150; THR-159; SER-212; SER-220; SER-234 AND
SER-315.
PubMed=2019585;
Bodwell J.E., Orti E., Coull J.M., Pappin D.J.C., Smith L.I., Swift F.;
"Identification of phosphorylated sites in the mouse glucocorticoid
receptor.";
J. Biol. Chem. 266:7549-7555(1991).
[6]
IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
Chinkers M., Pratt W.B.;
"Protein phosphatase 5 is a major component of glucocorticoid
receptor.hsp90 complexes with properties of an FK506-binding
immunophilin.";
J. Biol. Chem. 272:16224-16230(1997).
[7]
INTERACTION WITH STAT5A AND STAT5B.
PubMed=9528750; DOI=10.1128/mcb.18.4.1783;
Cella N., Groner B., Hynes N.E.;
"Characterization of Stat5a and Stat5b homodimers and heterodimers and
their association with the glucocortiocoid receptor in mammary cells.";
Mol. Cell. Biol. 18:1783-1792(1998).
[8]
INTERACTION WITH TRIM28.
PubMed=9742105; DOI=10.1128/mcb.18.10.5880;
Chang C.J., Chen Y.L., Lee S.C.;
"Coactivator TIF1beta interacts with transcription factor C/EBPbeta and
glucocorticoid receptor to induce alpha1-acid glycoprotein gene
expression.";
Mol. Cell. Biol. 18:5880-5887(1998).
[9]
INTERACTION WITH TGFB1I1.
PubMed=10848625; DOI=10.1091/mbc.11.6.2007;
Yang L., Guerrero J., Hong H., DeFranco D.B., Stallcup M.R.;
"Interaction of the tau2 transcriptional activation domain of
glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5,
which localizes to both focal adhesions and the nuclear matrix.";
Mol. Biol. Cell 11:2007-2018(2000).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10678832; DOI=10.1126/science.287.5456.1262;
McNally J.G., Mueller W.G., Walker D., Wolford R., Hager G.L.;
"The glucocorticoid receptor: rapid exchange with regulatory sites in
living cells.";
Science 287:1262-1265(2000).
[11]
SUBCELLULAR LOCATION, HETEROMULTIMERIC COMPLEX FORMATION, INTERACTION WITH
FKBP4, AND MECHANISM OF TRANSLOCATION TO THE NUCLEUS.
PubMed=11278753; DOI=10.1074/jbc.m010809200;
Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.;
"Evidence that the peptidylprolyl isomerase domain of the hsp90-binding
immunophilin FKBP52 is involved in both dynein interaction and
glucocorticoid receptor movement to the nucleus.";
J. Biol. Chem. 276:14884-14889(2001).
[12]
UBIQUITINATION AT LYS-426, MUTAGENESIS OF LYS-426, AND
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).
[13]
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).
[14]
HETEROMULTIMERIC COMPLEX FORMATION, AND MECHANISM OF TRANSLOCATION TO THE
NUCLEUS.
PubMed=11751894; DOI=10.1074/jbc.c100531200;
Davies T.H., Ning Y.M., Sanchez E.R.;
"A new first step in activation of steroid receptors: hormone-induced
switching of FKBP51 and FKBP52 immunophilins.";
J. Biol. Chem. 277:4597-4600(2002).
[15]
INVOLVEMENT IN IMMUNE SYSTEM DEVELOPMENT.
PubMed=12949501; DOI=10.1038/nm895;
Brewer J.A., Khor B., Vogt S.K., Muglia L.M., Fujiwara H., Haegele K.E.,
Sleckman B.P., Muglia L.J.;
"T-cell glucocorticoid receptor is required to suppress COX-2-mediated
lethal immune activation.";
Nat. Med. 9:1318-1322(2003).
[16]
POSSIBLE FUNCTION IN THE CONTROL OF BODY GROWTH.
PubMed=15037546; DOI=10.1101/gad.284704;
Tronche F., Opherk C., Moriggl R., Kellendonk C., Reimann A., Schwake L.,
Reichardt H.M., Stangl K., Gau D., Hoeflich A., Beug H., Schmid W.,
Schuetz G.;
"Glucocorticoid receptor function in hepatocytes is essential to promote
postnatal body growth.";
Genes Dev. 18:492-497(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH FKBP5 AND PPP5C, PHOSPHORYLATION
AT SER-212; SER-220 AND SER-234, AND DEPHOSPHORYLATION AT SER-212 AND
SER-234 BY PPP5C.
PubMed=21994940; DOI=10.1074/jbc.m111.311662;
Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A.,
Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.;
"Protein phosphatase 5 mediates lipid metabolism through reciprocal control
of glucocorticoid receptor and peroxisome proliferator-activated receptor-?
(PPAR?).";
J. Biol. Chem. 286:42911-42922(2011).
[19]
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).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-24, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[21]
INTERACTION WITH CIART.
PubMed=24736997; DOI=10.1371/journal.pbio.1001839;
Goriki A., Hatanaka F., Myung J., Kim J.K., Yoritaka T., Tanoue S., Abe T.,
Kiyonari H., Fujimoto K., Kato Y., Todo T., Matsubara A., Forger D.,
Takumi T.;
"A novel protein, CHRONO, functions as a core component of the mammalian
circadian clock.";
PLoS Biol. 12:E1001839-E1001839(2014).
[22]
FUNCTION.
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).
[23]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-484.
PubMed=25676786; DOI=10.1016/j.steroids.2015.01.022;
Banuelos J., Shin S.C., Lu N.Z.;
"A hotspot in the glucocorticoid receptor DNA-binding domain susceptible to
loss of function mutation.";
Steroids 96:115-120(2015).
[24]
INTERACTION WITH CRY1 AND CRY2.
PubMed=28751364; DOI=10.1073/pnas.1704955114;
Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
Zhao X., Downes M., Evans R.M., Lamia K.A.;
"Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
and modulate transcriptional activity.";
Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
[25]
INTERACTION WITH HSP90AA1 AND HSP90AB1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=27686098; DOI=10.1242/jcs.190959;
Okabe T., Chavan R., Fonseca Costa S.S., Brenna A., Ripperger J.A.,
Albrecht U.;
"REV-ERBalpha influences the stability and nuclear localization of the
glucocorticoid receptor.";
J. Cell Sci. 129:4143-4154(2016).
-!- 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:10678832). 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
(PubMed:15037546). {ECO:0000250|UniProtKB:P04150,
ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:15037546}.
-!- FUNCTION: [Isoform 1]: Has transcriptional activation and repression
activity (By similarity). Mediates glucocorticoid-induced apoptosis (By
similarity). 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 (PubMed:21994940).
{ECO:0000250|UniProtKB:P04150, ECO:0000269|PubMed:21994940,
ECO:0000269|PubMed:25847991}.
-!- FUNCTION: [Isoform 3]: Acts as a dominant negative inhibitor of isoform
1 (PubMed:20660300). Has intrinsic transcriptional activity independent
of isoform Alpha when both isoforms are coexpressed (By similarity).
Loses this transcription modulator function on its own (By similarity).
Has no hormone-binding activity (PubMed:20660300). May play a role in
controlling glucose metabolism by maintaining insulin sensitivity
(PubMed:20660300). Reduces hepatic gluconeogenesis through down-
regulation of PEPCK in an isoform Alpha-dependent manner (By
similarity). Directly regulates STAT1 expression in isoform Alpha-
independent manner (By similarity). {ECO:0000250|UniProtKB:P04150,
ECO:0000269|PubMed:20660300}.
-!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90AA1,
HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1,
or the immunophilin homolog PPP5C (PubMed:9195923, PubMed:21994940).
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
(PubMed:9195923, PubMed:11278753). 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 (By similarity). Directly
interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and
as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and
STAT5B homodimers and heterodimers (PubMed:9528750). Interacts with
NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:9742105). Interacts with
several coactivator complexes, including the SMARCA4 complex,
CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2
and NCOA6 (By similarity). Interaction with BAG1 inhibits
transactivation (By similarity). Interacts with HEXIM1, PELP1 and
TGFB1I1 (PubMed:10848625). Interacts with NCOA1 (By similarity).
Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By
similarity). Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent
fashion (PubMed:22170608, PubMed:28751364). Interacts with CIART
(PubMed:24736997). Interacts with RWDD3 (By similarity). Interacts with
UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3
(By similarity). Interacts with GRIP1 (By similarity). 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).
Interacts with MCM3AP (By similarity). Interacts (via domain NR LBD)
with HSP90AA1 and HSP90AB1 (PubMed:27686098). In the absence of
hormonal ligand, interacts with TACC1 (By similarity).
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06536,
ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:10848625,
ECO:0000269|PubMed:11278753, ECO:0000269|PubMed:21994940,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:24736997,
ECO:0000269|PubMed:27686098, ECO:0000269|PubMed:28751364,
ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9528750,
ECO:0000269|PubMed:9742105}.
-!- INTERACTION:
P97784:Cry1; NbExp=3; IntAct=EBI-15959147, EBI-1266607;
Q9R194:Cry2; NbExp=3; IntAct=EBI-15959147, EBI-1266619;
O88485:Dync1i1; NbExp=2; IntAct=EBI-492753, EBI-492834;
P30416:Fkbp4; NbExp=3; IntAct=EBI-492753, EBI-492746;
Q64378:Fkbp5; NbExp=2; IntAct=EBI-492753, EBI-492796;
P11499:Hsp90ab1; NbExp=2; IntAct=EBI-492753, EBI-492813;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278753,
ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}. Nucleus
{ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753,
ECO:0000269|PubMed:25676786, ECO:0000269|PubMed:27686098}.
Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding
(PubMed:11278753). The hormone-occupied receptor undergoes rapid
exchange between chromatin and the nucleoplasmic compartment
(PubMed:10678832). In the presence of NR1D1 shows a time-dependent
subcellular localization, localizing to the cytoplasm at ZT8 and to the
nucleus at ZT20 (PubMed:27686098). Lacks this diurnal pattern of
localization in the absence of NR1D1, localizing to both nucleus and
the cytoplasm at ZT8 and ZT20 (PubMed:27686098).
{ECO:0000269|PubMed:10678832, ECO:0000269|PubMed:11278753,
ECO:0000269|PubMed:27686098}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
{ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}.
Mitochondrion {ECO:0000250|UniProtKB:P04150}. 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}.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
{ECO:0000269|PubMed:20660300}. Cytoplasm {ECO:0000269|PubMed:20660300}.
Note=Expressed predominantly in the nucleus with some expression also
detected in the cytoplasm. {ECO:0000269|PubMed:20660300}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=5;
Name=1; Synonyms=1-A, GR form A, Alpha;
IsoId=P06537-1; Sequence=Displayed;
Name=2; Synonyms=2-A, GR form B, Gamma;
IsoId=P06537-2; Sequence=VSP_003704;
Name=1-B;
IsoId=P06537-3; Sequence=VSP_018774;
Name=2-B;
IsoId=P06537-4; Sequence=VSP_018774, VSP_003704;
Name=3; Synonyms=Beta;
IsoId=P06537-5; Sequence=VSP_058320, VSP_058321;
-!- TISSUE SPECIFICITY: Expressed in spleen, kidney and liver. Expressed in
a circadian manner in the liver (PubMed:27686098). Isoform 3: Expressed
at highest level in spleen with lesser amounts in kidney and liver.
{ECO:0000269|PubMed:20660300, ECO:0000269|PubMed:27686098}.
-!- INDUCTION: Isoform 1: Down-regulated by glucocorticoids. Isoform 3: Up-
regulated by glucocorticoids and insulin.
{ECO:0000269|PubMed:20660300}.
-!- 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|UniProtKB:P04150}.
-!- PTM: Increased proteasome-mediated degradation in response to
glucocorticoids. {ECO:0000269|PubMed:11555652}.
-!- PTM: Phosphorylated in the absence of hormone; becomes
hyperphosphorylated in the presence of glucocorticoids. Phosphorylated
in the absence of hormone; becomes hyperphosphorylated in the presence
of glucocorticoid. The Ser-212, Ser-234 and Ser-412-phosphorylated
forms are mainly cytoplasmic, and the Ser-220-phosphorylated form is
nuclear (By similarity). Phosphorylation at Ser-220 increases
transcriptional activity (By similarity). Phosphorylation at Ser-212,
Ser-234 and Ser-412 decreases signaling capacity (By similarity).
Phosphorylation at Ser-412 may protect from glucocorticoid-induced
apoptosis (By similarity). Phosphorylation at Ser-212 and Ser-220 is
not required in regulation of chromosome segregation (By similarity).
May be dephosphorylated by PPP5C, attenuates NR3C1 action
(PubMed:21994940). {ECO:0000250|UniProtKB:P04150,
ECO:0000269|PubMed:2019585, ECO:0000269|PubMed:21994940}.
-!- PTM: Sumoylation at Lys-285 and Lys-301 negatively regulates its
transcriptional activity. Sumoylation at Lys-709 positively regulates
its transcriptional activity in the presence of RWDD3. Sumoylation at
Lys-285 and Lys-301 is dispensable whereas sumoylation at Lys-709 is
critical for the stimulatory effect of RWDD3 on its transcriptional
activity. Heat shock increases sumoylation in a RWDD3-dependent manner.
{ECO:0000250|UniProtKB:P06536}.
-!- PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional
signaling. {ECO:0000269|PubMed:11555652}.
-!- MISCELLANEOUS: T-cell is a critical cellular target of GR, as immune
activation in mice lacking GR resulted in significant mortality. This
lethal activation is rescued by PTGS2 inhibition but not steroid
administration or cytokine neutralization.
-!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
{ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 1-B]: Produced by alternative initiation at
Met-28 of isoform 1. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 2-B]: Produced by alternative initiation at
Met-28 of isoform 2. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
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EMBL; X04435; CAA28031.1; -; mRNA.
EMBL; HM236293; ADM18962.1; -; mRNA.
EMBL; X13358; CAA31738.1; -; mRNA.
EMBL; X13359; CAA31739.1; -; mRNA.
PIR; A25691; A25691.
PDB; 3MNE; X-ray; 1.96 A; A=527-783.
PDB; 3MNO; X-ray; 1.55 A; A=527-783.
PDB; 3MNP; X-ray; 1.50 A; A=527-783.
PDBsum; 3MNE; -.
PDBsum; 3MNO; -.
PDBsum; 3MNP; -.
SMR; P06537; -.
CORUM; P06537; -.
DIP; DIP-11N; -.
IntAct; P06537; 8.
STRING; 10090.ENSMUSP00000095199; -.
BindingDB; P06537; -.
ChEMBL; CHEMBL3144; -.
DrugCentral; P06537; -.
GuidetoPHARMACOLOGY; 625; -.
iPTMnet; P06537; -.
PhosphoSitePlus; P06537; -.
SwissPalm; P06537; -.
EPD; P06537; -.
jPOST; P06537; -.
MaxQB; P06537; -.
PaxDb; P06537; -.
PeptideAtlas; P06537; -.
PRIDE; P06537; -.
MGI; MGI:95824; Nr3c1.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
InParanoid; P06537; -.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
ChiTaRS; Nr3c1; mouse.
EvolutionaryTrace; P06537; -.
PRO; PR:P06537; -.
Proteomes; UP000000589; Unplaced.
RNAct; P06537; protein.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0004883; F:glucocorticoid receptor activity; IDA:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0042562; F:hormone binding; ISO:MGI.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:MGI.
GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
GO; GO:0032183; F:SUMO binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030325; P:adrenal gland development; IMP:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISO:MGI.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; ISO:MGI.
GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0042711; P:maternal behavior; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1900170; P:negative regulation of glucocorticoid mediated signaling pathway; IDA:MGI.
GO; GO:0031914; P:negative regulation of synaptic plasticity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; ISO:MGI.
GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IGI:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
GO; GO:0031946; P:regulation of glucocorticoid biosynthetic process; IMP:MGI.
GO; GO:0006111; P:regulation of gluconeogenesis; IMP:MGI.
GO; GO:0010906; P:regulation of glucose metabolic process; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0046685; P:response to arsenic-containing substance; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IDA:CAFA.
Gene3D; 1.10.565.10; -; 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; 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;
Chromatin regulator; Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond;
Lipid-binding; Metal-binding; Methylation; Mitochondrion; Nucleus;
Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1..783
/note="Glucocorticoid receptor"
/id="PRO_0000019939"
DOMAIN 530..764
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 425..500
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 428..448
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 464..488
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..427
/note="Modulating"
REGION 492..783
/note="Interaction with CLOCK"
/evidence="ECO:0000250"
REGION 494..529
/note="Hinge"
REGION 538..703
/note="Interaction with CRY1"
/evidence="ECO:0000250"
COMPBIAS 75..82
/note="Poly-Gln"
COMPBIAS 407..426
/note="Glu/Pro/Ser/Thr-rich (PEST region)"
MOD_RES 24
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 46
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 122
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585"
MOD_RES 143
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 150
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585"
MOD_RES 159
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:2019585"
MOD_RES 212
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585,
ECO:0000269|PubMed:21994940"
MOD_RES 220
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585,
ECO:0000269|PubMed:21994940"
MOD_RES 234
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585,
ECO:0000269|PubMed:21994940"
MOD_RES 275
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 315
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:2019585"
MOD_RES 412
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 487
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 499
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 501
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P04150"
MOD_RES 502
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P04150"
CROSSLNK 285
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000250|UniProtKB:P04150"
CROSSLNK 285
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P04150"
CROSSLNK 301
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000250|UniProtKB:P04150"
CROSSLNK 301
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P04150"
CROSSLNK 426
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000305|PubMed:11555652"
CROSSLNK 709
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250|UniProtKB:P04150"
VAR_SEQ 1..27
/note="Missing (in isoform 1-B and isoform 2-B)"
/evidence="ECO:0000305"
/id="VSP_018774"
VAR_SEQ 458
/note="G -> GR (in isoform 2 and isoform 2-B)"
/evidence="ECO:0000303|PubMed:2911477"
/id="VSP_003704"
VAR_SEQ 735..748
/note="VENLLSYCFQTFLD -> STKHKSKTTAKKKK (in isoform 3)"
/id="VSP_058320"
VAR_SEQ 749..783
/note="Missing (in isoform 3)"
/id="VSP_058321"
MUTAGEN 1
/note="M->T: Abolishes expression of A-type isoforms."
/evidence="ECO:0000269|PubMed:11435610"
MUTAGEN 28
/note="M->T: Abolishes expression of B-type isoforms. 1-B."
/evidence="ECO:0000269|PubMed:11435610"
MUTAGEN 426
/note="K->A: Abolishes glucocorticoid-mediated degradation
and enhances transcription trans-activation."
/evidence="ECO:0000269|PubMed:11555652"
MUTAGEN 484
/note="R->A: Abolishes transactivation activity."
/evidence="ECO:0000269|PubMed:25676786"
MUTAGEN 484
/note="R->C: Abolishes transcriptional activity. Does not
impair ligand binding."
/evidence="ECO:0000269|PubMed:25676786"
MUTAGEN 484
/note="R->K: Does not change transactivation activity."
/evidence="ECO:0000269|PubMed:25676786"
CONFLICT 437
/note="V -> G (in Ref. 2; ADM18962 and 3; CAA31738/
CAA31739)"
/evidence="ECO:0000305"
HELIX 538..545
/evidence="ECO:0000244|PDB:3MNP"
HELIX 562..585
/evidence="ECO:0000244|PDB:3MNP"
HELIX 590..592
/evidence="ECO:0000244|PDB:3MNP"
HELIX 595..622
/evidence="ECO:0000244|PDB:3MNP"
STRAND 625..630
/evidence="ECO:0000244|PDB:3MNP"
STRAND 633..635
/evidence="ECO:0000244|PDB:3MNP"
HELIX 637..640
/evidence="ECO:0000244|PDB:3MNP"
TURN 643..645
/evidence="ECO:0000244|PDB:3MNP"
HELIX 646..662
/evidence="ECO:0000244|PDB:3MNP"
HELIX 666..677
/evidence="ECO:0000244|PDB:3MNP"
STRAND 679..682
/evidence="ECO:0000244|PDB:3MNP"
HELIX 689..708
/evidence="ECO:0000244|PDB:3MNP"
HELIX 714..747
/evidence="ECO:0000244|PDB:3MNP"
HELIX 749..751
/evidence="ECO:0000244|PDB:3MNP"
HELIX 757..771
/evidence="ECO:0000244|PDB:3MNP"
STRAND 775..777
/evidence="ECO:0000244|PDB:3MNP"
SEQUENCE 783 AA; 86053 MW; 455E5C1C3C955F2A CRC64;
MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA AASQADSKQQ
RILLDFSKGS ASNAQQQQQQ QQPQPDLSKA VSLSMGLYMG ETETKVMGND LGYPQQGQLG
LSSGETDFRL LEESIANLNR STSRPENPKS STPAAGCATP TEKEFPQTHS DPSSEQQNRK
SQPGTNGGSV KLYTTDQSTF DILQDLEFSA GSPGKETNES PWRSDLLIDE NLLSPLAGED
DPFLLEGDVN EDCKPLILPD TKPKIQDTGD TILSSPSSVA LPQVKTEKDD FIELCTPGVI
KQEKLGPVYC QASFSGTNII GNKMSAISVH GVSTSGGQMY HYDMNTASLS QQQDQKPVFN
VIPPIPVGSE NWNRCQGSGE DNLTSLGAMN FAGRSVFSNG YSSPGMRPDV SSPPSSSSTA
TGPPPKLCLV CSDEASVCHY GVLTCGSCKV FFKRAVEGQH NYLCAGRNDC IIDKIRRKNC
PACRYRKCLQ AGMNLEARKT KKKIKGIQQA TAGVSQDTSE NANKTIVPAA LPQLTPTLVS
LLEVIEPEVL YAGYDSSVPD SAWRIMTTLN MLGGRQVIAA VKWAKAIPGF RNLHLDDQMT
LLQYSWMFLM AFALGWRSYR QASGNLLCFA PDLIINEQRM TLPCMYDQCK HMLFISTELQ
RLQVSYEEYL CMKTLLLLSS VPKEGLKSQE LFDEIRMTYI KELGKAIVKR EGNSSQNWQR
FYQLTKLLDS MHDVVENLLS YCFQTFLDKS MSIEFPEMLA EIITNQIPKY SNGNIKKLLF
HQK


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Related Genes :
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr3c1 Grl Grl1] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr3c1 Grl] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[nr3c1 grl] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) (Fragment)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
[RORC NR1F3 RORG RZRG] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma)
[Nr2c2 Mtr2r1 Tak1 Tr4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[NR4A1 GFRP1 HMR NAK1] Nuclear receptor subfamily 4 group A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3)
[AR DHTR NR3C4] Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4)
[Nr1d1 Ear1] Nuclear receptor subfamily 1 group D member 1 (Rev-erbA-alpha) (V-erbA-related protein 1) (EAR-1)
[nhr-6 cnr-8 nr4a5 C48D5.1] Nuclear hormone receptor family member nhr-6 (Nuclear receptor subfamily 4 group A member 5) (Steroid hormone receptor family member cnr8)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Nr4a1 Gfrp Hmr N10 Nur77] Nuclear receptor subfamily 4 group A member 1 (Nuclear hormone receptor NUR/77) (Nuclear protein N10) (Orphan nuclear receptor HMR)
[Nr1h2 Lxrb] Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor subfamily 1 group H member 2) (Orphan nuclear receptor OR-1) (Ubiquitously-expressed nuclear receptor) (UR)
[Thra C-erba-alpha Nr1a1] Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha)
[Nr4a1 Hmr Ngfib] Nuclear receptor subfamily 4 group A member 1 (NUR77) (Nerve growth factor-induced protein I-B) (NGFI-B) (Orphan nuclear receptor HMR)
[NR2C2 TAK1 TR4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)

Bibliography :