NR3C1
entrez
2908
canonical
uniprot
P04150
canonical
ensembl
ENSG00000113580
resolver
ensp
ENSP00000231509
resolver
ensp
ENSP00000343205
resolver
ensp
ENSP00000377977
resolver
ensp
ENSP00000387672
resolver
ensp
ENSP00000422518
resolver
ensp
ENSP00000427672
resolver
ensp
ENSP00000540553
resolver
ensp
ENSP00000540554
resolver
ensp
ENSP00000540558
resolver
genesymbol
NR3C1
resolver
genesymbol_syn
GRL
resolver
hgnc
HGNC:7978
resolver
uniprot
A0ZXF9
resolver
uniprot
B0LPG8
resolver
uniprot
D3DQF4
resolver
uniprot
E5KQF5
resolver
uniprot
E5KQF6
resolver
uniprot
F1D8N4
resolver
uniprot
F5ATB7
resolver
uniprot
P04151
resolver
uniprot
Q53EP5
resolver
uniprot
Q6N0A4
resolver
uniprot_entry
E5KQF5_HUMAN
resolver
uniprot_entry
E5KQF6_HUMAN
resolver
uniprot_entry
F1D8N4_HUMAN
resolver
uniprot_entry
GCR_HUMAN
resolver
uniprot_sec
A0ZXF9
resolver
uniprot_sec
B0LPG8
resolver
uniprot_sec
D3DQF4
resolver
uniprot_sec
F5ATB7
resolver
uniprot_sec
P04151
resolver
uniprot_sec
Q53EP5
resolver
uniprot_sec
Q6N0A4
resolver
amino_acid_sequence
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
uniprot
proteins
disease_involvement
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 variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). 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 (PubMed:28139699). 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:28139699, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9590696}.; FUNCTION: [Isoform Alpha]: Has transcriptional activation and repression activity (PubMed:11435610, PubMed:15769988, PubMed:15866175, PubMed:17635946, PubMed:19141540, PubMed:19248771, PubMed:20484466, PubMed:21664385, PubMed:23820903). 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:20484466, PubMed:7769088, PubMed:8621628). 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}.
uniprot
proteins
mass_dalton
85659
uniprot
proteins
mutagenesis
MUTAGEN 1; /note="M->T: Abolishes expression of A-type isoforms."; /evidence="ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175"; MUTAGEN 27; /note="M->T: Abolishes expression of B-type isoforms."; /evidence="ECO:0000269|PubMed:11435610, ECO:0000269|PubMed:15866175"; MUTAGEN 86; /note="M->I: Abolishes expression of C-type isoforms; when associated with I-90 and I-98."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 90; /note="M->I: Abolishes expression of C-type isoforms; when associated with I-86 and I-98."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 98; /note="M->I: Abolishes expression of C-type isoforms; when associated with I-86 and I-90."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 101; /note="D->A: Reduces transcription activation activity of isoform Alpha-C3 by half."; /evidence="ECO:0000269|PubMed:23820903"; MUTAGEN 101; /note="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."; /evidence="ECO:0000269|PubMed:23820903"; MUTAGEN 106..107; /note="QQ->LL: Reduces activity of isoform Alpha-C3 by half."; /evidence="ECO:0000269|PubMed:23820903"; MUTAGEN 113..114; /note="SS->AA: Does not affect the activity of isoform Alpha-C3."; /evidence="ECO:0000269|PubMed:23820903"; MUTAGEN 191; /note="F->D: Reduces transactivation by the ADA complex."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 193; /note="I->D: Reduces transactivation by the ADA complex."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 194; /note="L->A: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 197; /note="L->E: Reduces transactivation by the ADA complex."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 211; /note="S->A: Reduces expression of target genes IGFBP1 and IRF8."; /evidence="ECO:0000269|PubMed:18483179"; MUTAGEN 213; /note="W->A: Strongly reduces transactivation by the ADA complex."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 224; /note="L->V: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 225; /note="L->F: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 226; /note="S->A: Abolishes phosphorylation and enhances transcriptional activation."; /evidence="ECO:0000269|PubMed:18483179"; MUTAGEN 235; /note="F->L: Strongly reduces transactivation by the ADA complex; when associated with V-236."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 236; /note="L->V: Strongly reduces transactivation by the ADA complex; when associated with L-235."; /evidence="ECO:0000269|PubMed:9154805"; MUTAGEN 277; /note="K->R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293."; /evidence="ECO:0000269|PubMed:12144530"; MUTAGEN 293; /note="K->R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277."; /evidence="ECO:0000269|PubMed:12144530"; MUTAGEN 316; /note="M->I: Abolishes expression of D-type isoforms; when associated with I-331 and I-336."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 331; /note="M->I: Abolishes expression of D-type isoforms; when associated with I-316 and I-336."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 336; /note="M->I: Abolishes expression of D-type isoforms; when associated with I-316 and I-331."; /evidence="ECO:0000269|PubMed:15866175"; MUTAGEN 404; /note="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."; /evidence="ECO:0000269|PubMed:18838540"; MUTAGEN 404; /note="S->D: Does not affect translocation to the nucleus following ligand stimulation."; /evidence="ECO:0000269|PubMed:18838540"; MUTAGEN 480; /note="K->A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-492; A-494 and A-495."; /evidence="ECO:0000269|PubMed:19141540"; MUTAGEN 492; /note="K->A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-494 and A-495."; /evidence="ECO:0000269|PubMed:19141540"; MUTAGEN 494; /note="K->A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-495. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-492 and A-495."; /evidence="ECO:0000269|PubMed:19141540"; MUTAGEN 495; /note="K->A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-494. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-492 and A-494."; /evidence="ECO:0000269|PubMed:19141540"; MUTAGEN 585; /note="R->A: Reduces activation mediated by ligand binding domain; when associated with A-590."; /evidence="ECO:0000269|PubMed:12151000"; MUTAGEN 590; /note="D->A: Reduces activation mediated by ligand binding domain; when associated with A-585."; /evidence="ECO:0000269|PubMed:12151000"; MUTAGEN 602; /note="F->S: Increases solubility. No effect on transactivation by dexamethasone."; /evidence="ECO:0000269|PubMed:12151000"; MUTAGEN 625; /note="P->A: Decreases transactivation by dexamethasone by 95%."; /evidence="ECO:0000269|PubMed:12151000"; MUTAGEN 628; /note="I->A: Decreases dimerization and transactivation by dexamethasone; when associated with S-602."; /evidence="ECO:0000269|PubMed:12151000"; MUTAGEN 703; /note="K->R: Slightly reduces sumoylation. Inhibits the stimulatory effect of RWDD3 on its transcriptional activity."; /evidence="ECO:0000269|PubMed:12144530, ECO:0000269|PubMed:23508108
uniprot
proteins
post_translational_modification
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: Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound NR3C1 when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846). {ECO:0000269|PubMed:37478846}.; 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}.
uniprot
proteins
protein_family
NR3 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10477749
uniprot
proteins
pubmed
10566686
uniprot
proteins
pubmed
10639135
uniprot
proteins
pubmed
10866662
uniprot
proteins
pubmed
10898924
uniprot
proteins
pubmed
10902803
uniprot
proteins
pubmed
11238589
uniprot
proteins
pubmed
11344238
uniprot
proteins
pubmed
11358809
uniprot
proteins
pubmed
11381138
uniprot
proteins
pubmed
11435610
uniprot
proteins
pubmed
11555652
uniprot
proteins
pubmed
11589680
uniprot
proteins
pubmed
11701741
uniprot
proteins
pubmed
11932321
uniprot
proteins
pubmed
12000743
uniprot
proteins
pubmed
12050230
uniprot
proteins
pubmed
12144530
uniprot
proteins
pubmed
12151000
uniprot
proteins
pubmed
12351458
uniprot
proteins
pubmed
12415108
uniprot
proteins
pubmed
12686538
uniprot
proteins
pubmed
15211577
uniprot
proteins
pubmed
15265776
uniprot
proteins
pubmed
15276593
uniprot
proteins
pubmed
15292341
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15591535
uniprot
proteins
pubmed
15769988
uniprot
proteins
pubmed
15866175
uniprot
proteins
pubmed
15941832
uniprot
proteins
pubmed
16030164
uniprot
proteins
pubmed
16478993
uniprot
proteins
pubmed
16914116
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
1704018
uniprot
proteins
pubmed
1707881
uniprot
proteins
pubmed
17404046
uniprot
proteins
pubmed
17635946
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18483179
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18838540
uniprot
proteins
pubmed
19141540
uniprot
proteins
pubmed
19248771
uniprot
proteins
pubmed
1958537
uniprot
proteins
pubmed
19666546
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
2026589
uniprot
proteins
pubmed
20335448
uniprot
proteins
pubmed
20484466
uniprot
proteins
pubmed
20843780
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21362280
uniprot
proteins
pubmed
21664385
uniprot
proteins
pubmed
21701417
uniprot
proteins
pubmed
21730050
uniprot
proteins
pubmed
21980503
uniprot
proteins
pubmed
22170608
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23303127
uniprot
proteins
pubmed
23426617
uniprot
proteins
pubmed
23508108
uniprot
proteins
pubmed
23820903
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24483153
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25775514
uniprot
proteins
pubmed
25847991
uniprot
proteins
pubmed
26031419
uniprot
proteins
pubmed
26541474
uniprot
proteins
pubmed
26711253
uniprot
proteins
pubmed
27120390
uniprot
proteins
pubmed
27353360
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28139699
uniprot
proteins
pubmed
2867473
uniprot
proteins
pubmed
29127155
uniprot
proteins
pubmed
30698747
uniprot
proteins
pubmed
37478846
uniprot
proteins
pubmed
3841189
uniprot
proteins
pubmed
7683692
uniprot
proteins
pubmed
7769088
uniprot
proteins
pubmed
8316249
uniprot
proteins
pubmed
8358712
uniprot
proteins
pubmed
8358735
uniprot
proteins
pubmed
8445027
uniprot
proteins
pubmed
8621628
uniprot
proteins
pubmed
9150737
uniprot
proteins
pubmed
9154805
uniprot
proteins
pubmed
9353307
uniprot
proteins
pubmed
9590696
uniprot
proteins
sequence_length
777
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:30698747, ECO:0000269|PubMed:8621628}. Nucleus {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:30698747, 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}. Chromosome {ECO:0000250|UniProtKB:P06537}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P06537}. Note=After ligand activation, translocates from the cytoplasm to the nucleus (PubMed:30698747). The hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment (By similarity). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). Upon dexamethasone binding associates with the glucocorticoid response elements of target genes (By similarity). {ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:30698747}.; 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}.
uniprot
proteins