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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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi425 – 50076Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri428 – 44821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri464 – 48825NR C4-typePROSITE-ProRule annotationAdd
BLAST

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
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → T: Abolishes expression of A-type isoforms. 1 Publication
Mutagenesisi28 – 281M → T: Abolishes expression of B-type isoforms. 1-B. 1 Publication
Mutagenesisi426 – 4261K → A: Abolishes glucocorticoid-mediated degradation and enhances transcription trans-activation. 1 Publication
Mutagenesisi484 – 4841R → A: Abolishes transactivation activity. 1 Publication
Mutagenesisi484 – 4841R → C: Abolishes transcriptional activity. Does not impair ligand binding. 1 Publication
Mutagenesisi484 – 4841R → K: Does not change transactivation activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3144.
GuidetoPHARMACOLOGYi625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 783783Glucocorticoid receptorPRO_0000019939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei159 – 1591Phosphothreonine1 Publication
Modified residuei212 – 2121Phosphoserine2 Publications
Modified residuei220 – 2201Phosphoserine2 Publications
Modified residuei234 – 2341Phosphoserine2 Publications
Modified residuei275 – 2751PhosphoserineBy similarity
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki301 – 301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki301 – 301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei412 – 4121PhosphoserineCombined sources
Cross-linki426 – 426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei487 – 4871N6-acetyllysineBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei501 – 5011N6-acetyllysineBy similarity
Modified residuei502 – 5021N6-acetyllysineBy similarity
Cross-linki709 – 709Glycyl 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, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06537.
MaxQBiP06537.
PaxDbiP06537.
PeptideAtlasiP06537.
PRIDEiP06537.

PTM databases

iPTMnetiP06537.
PhosphoSiteiP06537.
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).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 dimerization activity Source: MGI

Protein-protein interaction databases

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

Chemistry

BindingDBiP06537.

Structurei

Secondary structure

1
783
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi538 – 5458Combined sources
Helixi562 – 58524Combined sources
Helixi590 – 5923Combined sources
Helixi595 – 62228Combined sources
Beta strandi625 – 6306Combined sources
Beta strandi633 – 6353Combined sources
Helixi637 – 6404Combined sources
Turni643 – 6453Combined sources
Helixi646 – 66217Combined sources
Helixi666 – 67712Combined sources
Beta strandi679 – 6824Combined sources
Helixi689 – 70820Combined sources
Helixi714 – 74734Combined sources
Helixi749 – 7513Combined sources
Helixi757 – 77115Combined sources
Beta strandi775 – 7773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MNEX-ray1.96A527-783[»]
3MNOX-ray1.55A527-783[»]
3MNPX-ray1.50A527-783[»]
ProteinModelPortaliP06537.
SMRiP06537. Positions 425-782.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06537.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 427427ModulatingAdd
BLAST
Regioni492 – 783292Interaction with CLOCKBy similarityAdd
BLAST
Regioni494 – 53441HingeAdd
BLAST
Regioni535 – 783249Steroid-bindingAdd
BLAST
Regioni538 – 703166Interaction with CRY1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 828Poly-Gln
Compositional biasi407 – 42620Glu/Pro/Ser/Thr-rich (PEST region)Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri428 – 44821NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri464 – 48825NR C4-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti437 – 4371V → G in ADM18962 (PubMed:20660300).Curated
Sequence conflicti437 – 4371V → G in CAA31738 (PubMed:2911477).Curated
Sequence conflicti437 – 4371V → G in CAA31739 (PubMed:2911477).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727Missing in isoform 1-B and isoform 2-B. CuratedVSP_018774Add
BLAST
Alternative sequencei458 – 4581G → GR in isoform 2 and isoform 2-B. 1 PublicationVSP_003704
Alternative sequencei735 – 74814VENLL…QTFLD → STKHKSKTTAKKKK in isoform 3. VSP_058320Add
BLAST
Alternative sequencei749 – 78335Missing in isoform 3. VSP_058321Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3MNEX-ray1.96A527-783[»]
3MNOX-ray1.55A527-783[»]
3MNPX-ray1.50A527-783[»]
ProteinModelPortaliP06537.
SMRiP06537. Positions 425-782.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP06537.
ChEMBLiCHEMBL3144.
GuidetoPHARMACOLOGYi625.

PTM databases

iPTMnetiP06537.
PhosphoSiteiP06537.
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: July 6, 2016
This is version 182 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.