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Protein

Glucocorticoid receptor

Gene

Nr3c1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications
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).By similarity2 Publications
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).By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi425 – 500Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
Zinc fingeri428 – 448NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri464 – 488NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

  • adrenal gland development Source: MGI
  • cellular response to steroid hormone stimulus Source: MGI
  • chromatin modification Source: UniProtKB-KW
  • glucocorticoid metabolic process Source: MGI
  • glucocorticoid receptor signaling pathway Source: MGI
  • mammary gland duct morphogenesis Source: MGI
  • maternal behavior Source: MGI
  • negative regulation of glucocorticoid mediated signaling pathway Source: MGI
  • positive regulation of neuron apoptotic process Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of glucocorticoid biosynthetic process Source: MGI
  • regulation of gluconeogenesis Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucocorticoid receptor
Short name:
GR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 1
Gene namesi
Name:Nr3c1
Synonyms:Grl, Grl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95824. Nr3c1.

Subcellular locationi

Isoform 1 :
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Mitochondrion By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

  • Note: After ligand activation, translocates from the cytoplasm to the nucleus.By similarity
Isoform 3 :

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • intracellular Source: MGI
  • membrane Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • protein complex Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → T: Abolishes expression of A-type isoforms. 1 Publication1
Mutagenesisi28M → T: Abolishes expression of B-type isoforms. 1-B. 1 Publication1
Mutagenesisi426K → A: Abolishes glucocorticoid-mediated degradation and enhances transcription trans-activation. 1 Publication1
Mutagenesisi484R → A: Abolishes transactivation activity. 1 Publication1
Mutagenesisi484R → C: Abolishes transcriptional activity. Does not impair ligand binding. 1 Publication1
Mutagenesisi484R → K: Does not change transactivation activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3144.
GuidetoPHARMACOLOGYi625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000199391 – 783Glucocorticoid receptorAdd BLAST783

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Omega-N-methylarginineCombined sources1
Modified residuei46PhosphoserineBy similarity1
Modified residuei122Phosphoserine1 Publication1
Modified residuei143PhosphoserineBy similarity1
Modified residuei150Phosphoserine1 Publication1
Modified residuei159Phosphothreonine1 Publication1
Modified residuei212Phosphoserine2 Publications1
Modified residuei220Phosphoserine2 Publications1
Modified residuei234Phosphoserine2 Publications1
Modified residuei275PhosphoserineBy similarity1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei315Phosphoserine1 Publication1
Modified residuei412PhosphoserineCombined sources1
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei487N6-acetyllysineBy similarity1
Modified residuei499N6-acetyllysineBy similarity1
Modified residuei501N6-acetyllysineBy similarity1
Modified residuei502N6-acetyllysineBy similarity1
Cross-linki709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity.By similarity
Increased proteasome-mediated degradation in response to glucocorticoids.1 Publication
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).By similarity2 Publications
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.By similarity
Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06537.
MaxQBiP06537.
PaxDbiP06537.
PeptideAtlasiP06537.
PRIDEiP06537.

PTM databases

iPTMnetiP06537.
PhosphoSitePlusiP06537.
SwissPalmiP06537.

Expressioni

Tissue specificityi

Expressed in spleen, kidney and liver. Isoform 3: Expressed at highest level in spleen with lesser amounts in kidney and liver.1 Publication

Inductioni

Isoform 1: Down-regulated by glucocorticoids. Isoform 3: Up-regulated by glucocorticoids and insulin.1 Publication

Gene expression databases

CleanExiMM_NR3C1.

Interactioni

Subunit structurei

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). 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). 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).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dync1i1O884852EBI-492753,EBI-492834
Fkbp4P304163EBI-492753,EBI-492746
Fkbp5Q643782EBI-492753,EBI-492796
Hsp90ab1P114992EBI-492753,EBI-492813

GO - Molecular functioni

  • protein complex binding Source: MGI
  • protein dimerization activity Source: MGI

Protein-protein interaction databases

DIPiDIP-11N.
IntActiP06537. 4 interactors.
MINTiMINT-152096.
STRINGi10090.ENSMUSP00000025300.

Chemistry databases

BindingDBiP06537.

Structurei

Secondary structure

1783
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi538 – 545Combined sources8
Helixi562 – 585Combined sources24
Helixi590 – 592Combined sources3
Helixi595 – 622Combined sources28
Beta strandi625 – 630Combined sources6
Beta strandi633 – 635Combined sources3
Helixi637 – 640Combined sources4
Turni643 – 645Combined sources3
Helixi646 – 662Combined sources17
Helixi666 – 677Combined sources12
Beta strandi679 – 682Combined sources4
Helixi689 – 708Combined sources20
Helixi714 – 747Combined sources34
Helixi749 – 751Combined sources3
Helixi757 – 771Combined sources15
Beta strandi775 – 777Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MNEX-ray1.96A527-783[»]
3MNOX-ray1.55A527-783[»]
3MNPX-ray1.50A527-783[»]
ProteinModelPortaliP06537.
SMRiP06537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06537.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 427ModulatingAdd BLAST427
Regioni492 – 783Interaction with CLOCKBy similarityAdd BLAST292
Regioni494 – 534HingeAdd BLAST41
Regioni535 – 783Steroid-bindingAdd BLAST249
Regioni538 – 703Interaction with CRY1By similarityAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi75 – 82Poly-Gln8
Compositional biasi407 – 426Glu/Pro/Ser/Thr-rich (PEST region)Add BLAST20

Domaini

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.By similarity

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri428 – 448NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri464 – 488NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiP06537.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. Glcrtcd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02155. GCR. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P06537-1) [UniParc]FASTAAdd to basket
Also known as: 1-A, GR form A, Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA
60 70 80 90 100
AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQPQPDLSKA VSLSMGLYMG
110 120 130 140 150
ETETKVMGND LGYPQQGQLG LSSGETDFRL LEESIANLNR STSRPENPKS
160 170 180 190 200
STPAAGCATP TEKEFPQTHS DPSSEQQNRK SQPGTNGGSV KLYTTDQSTF
210 220 230 240 250
DILQDLEFSA GSPGKETNES PWRSDLLIDE NLLSPLAGED DPFLLEGDVN
260 270 280 290 300
EDCKPLILPD TKPKIQDTGD TILSSPSSVA LPQVKTEKDD FIELCTPGVI
310 320 330 340 350
KQEKLGPVYC QASFSGTNII GNKMSAISVH GVSTSGGQMY HYDMNTASLS
360 370 380 390 400
QQQDQKPVFN VIPPIPVGSE NWNRCQGSGE DNLTSLGAMN FAGRSVFSNG
410 420 430 440 450
YSSPGMRPDV SSPPSSSSTA TGPPPKLCLV CSDEASVCHY GVLTCGSCKV
460 470 480 490 500
FFKRAVEGQH NYLCAGRNDC IIDKIRRKNC PACRYRKCLQ AGMNLEARKT
510 520 530 540 550
KKKIKGIQQA TAGVSQDTSE NANKTIVPAA LPQLTPTLVS LLEVIEPEVL
560 570 580 590 600
YAGYDSSVPD SAWRIMTTLN MLGGRQVIAA VKWAKAIPGF RNLHLDDQMT
610 620 630 640 650
LLQYSWMFLM AFALGWRSYR QASGNLLCFA PDLIINEQRM TLPCMYDQCK
660 670 680 690 700
HMLFISTELQ RLQVSYEEYL CMKTLLLLSS VPKEGLKSQE LFDEIRMTYI
710 720 730 740 750
KELGKAIVKR EGNSSQNWQR FYQLTKLLDS MHDVVENLLS YCFQTFLDKS
760 770 780
MSIEFPEMLA EIITNQIPKY SNGNIKKLLF HQK
Length:783
Mass (Da):86,053
Last modified:January 1, 1988 - v1
Checksum:i455E5C1C3C955F2A
GO
Isoform 2 (identifier: P06537-2) [UniParc]FASTAAdd to basket
Also known as: 2-A, GR form B, Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     458-458: G → GR

Note: Produced by alternative splicing.
Show »
Length:784
Mass (Da):86,209
Checksum:iB52F39BDEDF94ADC
GO
Isoform 1-B (identifier: P06537-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Note: Produced by alternative initiation at Met-28 of isoform 1.
Show »
Length:756
Mass (Da):83,273
Checksum:iAE29F70FF47F964D
GO
Isoform 2-B (identifier: P06537-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     458-458: G → GR

Note: Produced by alternative initiation at Met-28 of isoform 2.
Show »
Length:757
Mass (Da):83,429
Checksum:iEBD44E16FE31A015
GO
Isoform 3 (identifier: P06537-5) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     735-748: VENLLSYCFQTFLD → STKHKSKTTAKKKK
     749-783: Missing.

Show »
Length:748
Mass (Da):81,888
Checksum:i81F4E19AFED446EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti437V → G in ADM18962 (PubMed:20660300).Curated1
Sequence conflicti437V → G in CAA31738 (PubMed:2911477).Curated1
Sequence conflicti437V → G in CAA31739 (PubMed:2911477).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187741 – 27Missing in isoform 1-B and isoform 2-B. CuratedAdd BLAST27
Alternative sequenceiVSP_003704458G → GR in isoform 2 and isoform 2-B. 1 Publication1
Alternative sequenceiVSP_058320735 – 748VENLL…QTFLD → STKHKSKTTAKKKK in isoform 3. Add BLAST14
Alternative sequenceiVSP_058321749 – 783Missing in isoform 3. Add BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04435 mRNA. Translation: CAA28031.1.
HM236293 mRNA. Translation: ADM18962.1.
X13358 mRNA. Translation: CAA31738.1.
X13359 mRNA. Translation: CAA31739.1.
PIRiA25691.
UniGeneiMm.129481.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04435 mRNA. Translation: CAA28031.1.
HM236293 mRNA. Translation: ADM18962.1.
X13358 mRNA. Translation: CAA31738.1.
X13359 mRNA. Translation: CAA31739.1.
PIRiA25691.
UniGeneiMm.129481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MNEX-ray1.96A527-783[»]
3MNOX-ray1.55A527-783[»]
3MNPX-ray1.50A527-783[»]
ProteinModelPortaliP06537.
SMRiP06537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11N.
IntActiP06537. 4 interactors.
MINTiMINT-152096.
STRINGi10090.ENSMUSP00000025300.

Chemistry databases

BindingDBiP06537.
ChEMBLiCHEMBL3144.
GuidetoPHARMACOLOGYi625.

PTM databases

iPTMnetiP06537.
PhosphoSitePlusiP06537.
SwissPalmiP06537.

Proteomic databases

EPDiP06537.
MaxQBiP06537.
PaxDbiP06537.
PeptideAtlasiP06537.
PRIDEiP06537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:95824. Nr3c1.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiP06537.

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.

Miscellaneous databases

ChiTaRSiNr3c1. mouse.
EvolutionaryTraceiP06537.
PROiP06537.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NR3C1.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. Glcrtcd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02155. GCR. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCR_MOUSE
AccessioniPrimary (citable) accession number: P06537
Secondary accession number(s): E0ZPU5, Q61628, Q61629
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.