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P04150 (GCR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 204. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucocorticoid receptor

Short name=GR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 1
Gene names
Name:NR3C1
Synonyms:GRL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length777 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression. Ref.37 Ref.41

Subunit structure

Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C. 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. Directly interacts with UNC45A. Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers. Interacts with NRIP1, POU2F1, POU2F2 and TRIM28. Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6. Interaction with BAG1 inhibits transactivation. Interacts with HEXIM1, PELP1 and TGFB1I1. Interacts with NCOA1, NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1. Interacts with CLOCK in a ligand-dependent fashion. Ref.17 Ref.18 Ref.19 Ref.22 Ref.29 Ref.31 Ref.32 Ref.33 Ref.37 Ref.42 Ref.43 Ref.61

Subcellular location

Cytoplasm. Mitochondrion. Nucleus. Note: Cytoplasmic in the absence of ligand, nuclear after ligand-binding. Ref.41 Ref.42

Isoform Beta: Nucleus. Note: Localized largely in the nucleus. Ref.41 Ref.42

Tissue specificity

Widely expressed. In the heart, detected in left and right atria, left and right ventricles, aorta, apex, intraventricular septum, and atrioventricular node as well as whole adult and fetal heart. Ref.21

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Ref.15

Post-translational modification

Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. Ref.37 Ref.43

Increased proteasome-mediated degradation in response to glucocorticoids.

Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203-phosphorylated form is mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear. Transcriptional activity correlates with the amount of phosphorylation at Ser-211. May be dephosphorylated by PPP5C, attenuates NR3C1 action. Ref.28

Sumoylated; this reduces transcription transactivation. Ref.27

Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling By similarity.

Polymorphism

Carriers of the 22-Glu-Lys-23 allele are relatively more resistant to the effects of GCs with respect to the sensitivity of the adrenal feedback mechanism than non-carriers, resulting in a better metabolic health profile. Carriers have a better survival than non-carriers, as well as lower serum CRP levels. The 22-Glu-Lys-23 polymorphism is associated with a sex-specific, beneficial body composition at young-adult age, as well as greater muscle strength in males.

Involvement in disease

Glucocorticoid resistance (GCRES) [MIM:138040]: Hypertensive, hyperandrogenic disorder characterized by increased serum cortisol concentrations. Inheritance is autosomal dominant.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.47 Ref.50 Ref.56 Ref.58 Ref.61

Miscellaneous

High constitutive expression of isoform Beta by neutrophils may provide a mechanism by which these cells escape glucocorticoid-induced cell death. Up-regulation by proinflammatory cytokines such as IL8 further enhances their survival in the presence of glucocorticoids during inflammation.

Can up- or down-modulate aggregation and nuclear localization of expanded polyglutamine polypeptides derived from AR and HD through specific regulation of gene expression. Aggregation and nuclear localization of expanded polyglutamine proteins are regulated cellular processes that can be modulated by this receptor, a well-characterized transcriptional regulator.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Pseudohermaphroditism
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionChromatin regulator
Receptor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenal gland development

Inferred from electronic annotation. Source: Ensembl

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

glucocorticoid metabolic process

Inferred from electronic annotation. Source: Ensembl

mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of glucocorticoid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay Ref.37. Source: UniProtKB

signal transduction

Traceable author statement PubMed 7769088. Source: ProtInc

transcription from RNA polymerase II promoter

Traceable author statement PubMed 8621628. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement PubMed 10887960. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Traceable author statement PubMed 10887960. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionglucocorticoid receptor activity

Traceable author statement PubMed 8621628. Source: ProtInc

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 10903900PubMed 7769088. Source: ProtInc

steroid binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 10 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Note: At least 4 isoforms, Alpha (shown here), Alpha-B, Beta and Beta-B, are produced by alternative initiation at Met-1 and Met-27. The existence of isoform Alpha and isoform Alpha-B has been proved by mutagenesis. As the sequence environment of the 2 potential ATG initiator codons is the same for the other alternatively spliced isoforms, alternative initiation of translation could also occur on these transcripts. Additional isoforms seem to exist.
Isoform Alpha (identifier: P04150-1)

Also known as: Alpha-A;

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.
Note: Predominant physiological form. Isoform Alpha-B is produced by alternative initiation at Met-27 of isoform Alpha. Both isoforms exhibit similar subcellular location and nuclear translocation after ligand activation. Isoform Alpha-B appears to be more susceptible to degradation, at least when expressed in mammalian cells, but more effective in transcriptional activation and not in transrepression.
Isoform Beta (identifier: P04150-2)

Also known as: Beta-A;

The sequence of this isoform differs from the canonical sequence as follows:
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI
Note: No hormone-binding activity. Widely expressed at low level.
Isoform Alpha-2 (identifier: P04150-3)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     451-451: G → GR
Note: Due to a partial intron retention. Lower transcriptional activity. Expressed at low level.
Isoform Beta-2 (identifier: P04150-6)

The sequence of this isoform differs from the canonical sequence as follows:
     451-451: G → GR
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI
Note: Due to a partial intron retention.
Isoform GR-A alpha (identifier: P04150-5)

The sequence of this isoform differs from the canonical sequence as follows:
     491-674: Missing.
Note: Lacks exons 5, 6 and 7. Found in glucocorticoid-resistant myeloma patients.
Isoform GR-A beta (identifier: P04150-7)

The sequence of this isoform differs from the canonical sequence as follows:
     491-674: Missing.
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI
Note: Lacks exons 5, 6 and 7.
Isoform GR-P (identifier: P04150-4)

The sequence of this isoform is not available.
Note: Encoded by exons 2-7 plus several basepairs from the subsequent intron region. Lacks the ligand binding domain. Accounts for up to 10-20% of mRNAs.
Isoform Alpha-B (identifier: P04150-8)

Also known as: Beta-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
Note: Produced by alternative initiation at Met-27 of isoform Alpha. Both isoforms exhibit similar subcellular location and nuclear translocation after ligand activation. Isoform Alpha-B appears to be more susceptible to degradation, at least when expressed in mammalian cells, but more effective in transcriptional activation and not in transrepression.
Isoform Beta-B (identifier: P04150-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI
Note: Produced by alternative initiation at Met-27 of isoform Beta.
Isoform 10 (identifier: P04150-10)

Also known as: hGRDelta313-338;

The sequence of this isoform differs from the canonical sequence as follows:
     313-338: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 777777Glucocorticoid receptor
PRO_0000019937

Regions

DNA binding421 – 48666Nuclear receptor
Zinc finger421 – 44121NR C4-type
Zinc finger457 – 48125NR C4-type
Region1 – 420420Modulating
Region485 – 777293Interaction with CLOCK
Region487 – 52741Hinge
Region528 – 777250Steroid-binding
Compositional bias399 – 41820Glu/Pro/Ser/Thr-rich (PEST region)

Amino acid modifications

Modified residue1131Phosphoserine By similarity
Modified residue1341Phosphoserine Ref.36
Modified residue1411Phosphoserine By similarity
Modified residue2031Phosphoserine Ref.28
Modified residue2111Phosphoserine Ref.28
Modified residue2261Phosphoserine By similarity
Modified residue2671Phosphoserine Ref.36
Modified residue4801N6-acetyllysine Ref.37
Modified residue4921N6-acetyllysine Ref.37
Modified residue4941N6-acetyllysine Ref.37
Modified residue4951N6-acetyllysine Ref.37
Cross-link277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Natural variations

Alternative sequence1 – 2626Missing in isoform Alpha-B and isoform Beta-B.
VSP_018773
Alternative sequence313 – 33826Missing in isoform 10.
VSP_043908
Alternative sequence4511G → GR in isoform Alpha-2 and isoform Beta-2.
VSP_007363
Alternative sequence491 – 674184Missing in isoform GR-A alpha and isoform GR-A beta.
VSP_013340
Alternative sequence728 – 77750VVENL…LFHQK → NVMWLKPESTSHTLI in isoform Beta, isoform Beta-B, isoform Beta-2 and isoform GR-A beta.
VSP_003703
Natural variant231R → K. Ref.8 Ref.52 Ref.53 Ref.55 Ref.59 Ref.62 Ref.63
Corresponds to variant rs6190 [ dbSNP | Ensembl ].
VAR_014140
Natural variant291F → L. Ref.55
VAR_015628
Natural variant651F → V. Ref.8 Ref.53
Corresponds to variant rs6192 [ dbSNP | Ensembl ].
VAR_014622
Natural variant1121L → F. Ref.55
VAR_015629
Natural variant2331D → N. Ref.55
VAR_015630
Natural variant3631N → S May increase sensitivity to exogenously administered glucocorticoids; may contribute to central obesity in men and show lack of association with other risk factors for coronary heart disease and diabetes mellitus. Ref.49 Ref.52 Ref.53 Ref.55 Ref.57
Corresponds to variant rs6195 [ dbSNP | Ensembl ].
VAR_004675
Natural variant4211C → Y in a glucocorticoid resistant leukemia cell line. Ref.48
VAR_015631
Natural variant4771R → H in GCRES. Ref.56
VAR_013472
Natural variant5591I → N in GCRES; interferes with translocation to the nucleus and thereby strongly reduces transcription activation. Is equally impaired in nuclear export. Acts as dominant negative mutant. Ref.58
VAR_015632
Natural variant5711V → A in pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor. Ref.60
VAR_025014
Natural variant6411D → V in GCRES. Ref.47
VAR_004676
Natural variant6791G → S in GCRES; has 50% binding affinity. Ref.56
VAR_013473
Natural variant7291V → I in GCRES. Ref.50
VAR_004677
Natural variant7471I → M in GCRES; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. Ref.61
VAR_015633
Natural variant7531L → F in two glucocorticoid resistant leukemia cell lines lacking the normal allele. Ref.48 Ref.51
VAR_004678

Experimental info

Mutagenesis11M → T: Abolishes expression of A-type isoforms. Ref.26
Mutagenesis271M → T: Abolishes expression of B-type isoforms. Ref.26
Mutagenesis1911F → D: Reduces transactivation by the ADA complex. Ref.17
Mutagenesis1931I → D: Reduces transactivation by the ADA complex. Ref.17
Mutagenesis1941L → A: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225. Ref.17
Mutagenesis1971L → E: Reduces transactivation by the ADA complex. Ref.17
Mutagenesis2131W → A: Strongly reduces transactivation by the ADA complex. Ref.17
Mutagenesis2241L → V: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225. Ref.17
Mutagenesis2251L → F: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224. Ref.17
Mutagenesis2351F → L: Strongly reduces transactivation by the ADA complex; when associated with V-236. Ref.17
Mutagenesis2361L → V: Strongly reduces transactivation by the ADA complex; when associated with L-235. Ref.17
Mutagenesis2771K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293. Ref.27
Mutagenesis2931K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277. Ref.27
Mutagenesis4801K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-492; A-494 and A-495. Ref.37
Mutagenesis4921K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-494 and A-495. Ref.37
Mutagenesis4941K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-495. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-492 and A-495. Ref.37
Mutagenesis4951K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-494. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-492 and A-494. Ref.37
Mutagenesis5851R → A: Reduces activation mediated by ligand binding domain; when associated with A-590. Ref.45
Mutagenesis5901D → A: Reduces activation mediated by ligand binding domain; when associated with A-585. Ref.45
Mutagenesis6021F → S: Increases solubility. No effect on transactivation by dexamethasone. Ref.45
Mutagenesis6251P → A: Decreases transactivation by dexamethasone by 95%. Ref.45
Mutagenesis6281I → A: Decreases dimerization and transactivation by dexamethasone; when associated with S-602. Ref.45
Mutagenesis7031K → R: Slightly reduces sumoylation. Ref.27
Sequence conflict3991R → G in BAD97314. Ref.6
Sequence conflict7541A → T in BAD97314. Ref.6

Secondary structure

.................................................... 777
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha (Alpha-A) [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: C5C90C9A5DD16AAB

FASTA77785,659
        10         20         30         40         50         60 
MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV ASQSDSKQRR 

        70         80         90        100        110        120 
LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI SLSSGETDLK 

       130        140        150        160        170        180 
LLEESIANLN RSTSVPENPK SSASTAVSAA PTEKEFPKTH SDVSSEQQHL KGQTGTNGGN 

       190        200        210        220        230        240 
VKLYTTDQST FDILQDLEFS SGSPGKETNE SPWRSDLLID ENCLLSPLAG EDDSFLLEGN 

       250        260        270        280        290        300 
SNEDCKPLIL PDTKPKIKDN GDLVLSSPSN VTLPQVKTEK EDFIELCTPG VIKQEKLGTV 

       310        320        330        340        350        360 
YCQASFPGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI FNVIPPIPVG 

       370        380        390        400        410        420 
SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP DVSSPPSSSS TATTGPPPKL 

       430        440        450        460        470        480 
CLVCSDEASG CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRYRK 

       490        500        510        520        530        540 
CLQAGMNLEA RKTKKKIKGI QQATTGVSQE TSENPGNKTI VPATLPQLTP TLVSLLEVIE 

       550        560        570        580        590        600 
PEVLYAGYDS SVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW 

       610        620        630        640        650        660 
MFLMAFALGW RSYRQSSANL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS SELHRLQVSY 

       670        680        690        700        710        720 
EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA IVKREGNSSQ NWQRFYQLTK 

       730        740        750        760        770 
LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP EMLAEIITNQ IPKYSNGNIK KLLFHQK 

« Hide

Isoform Beta (Beta-A) [UniParc].

Checksum: E2D1F6EA0EE14704
Show »

FASTA74281,509
Isoform Alpha-2 (Gamma) [UniParc].

Checksum: 23048D99B60B169C
Show »

FASTA77885,815
Isoform Beta-2 [UniParc].

Checksum: 329BE98BCC1DC0E5
Show »

FASTA74381,666
Isoform GR-A alpha [UniParc].

Checksum: 8CB72DE6B0593EFD
Show »

FASTA59364,752
Isoform GR-A beta [UniParc].

Checksum: 7C1C30CD84689FBE
Show »

FASTA55860,602
Isoform GR-P (Sequence not available).
Isoform Alpha-B (Beta-B) [UniParc].

Checksum: C6D7A2D88B4025C1
Show »

FASTA75182,845
Isoform Beta-B [UniParc].

Checksum: BCF1D97EFD06AB74
Show »

FASTA71678,695
Isoform 10 (hGRDelta313-338) [UniParc].

Checksum: 39C4B6A962632545
Show »

FASTA75182,904

References

« Hide 'large scale' references
[1]"Primary structure and expression of a functional human glucocorticoid receptor cDNA."
Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R., Thompson E.B., Rosenfeld M.G., Evans R.M.
Nature 318:635-641(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
Tissue: Fibroblast.
[2]"The genomic structure of the human glucocorticoid receptor."
Encio I.J., Detera-Wadleigh S.D.
J. Biol. Chem. 266:7182-7188(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA AND BETA).
[3]"Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"A new transcript splice variant of the human glucocorticoid receptor: identification and tissue distribution of hGR Delta 313-338, an alternative exon 2 transactivation domain isoform."
Turner J.D., Schote A.B., Keipes M., Muller C.P.
Ann. N. Y. Acad. Sci. 1095:334-341(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
[5]"Alternative splicing within the DNA binding domain creates a novel isoform of the human glucocorticoid receptor."
Munroe D.G., Pang J., Taylor G.R., Lau C., Plante R.K., Zhou L.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
Tissue: Osteosarcoma.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Tissue: Kidney.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Tissue: Uterine endothelium.
[8]NIEHS SNPs program
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-23 AND VAL-65.
[9]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Tissue: Placenta.
[13]"Purification of a human glucocorticoid receptor gene promoter-binding protein. Production of polyclonal antibodies against the purified factor."
Leclerc S., Xie B.X., Roy R., Govindan M.V.
J. Biol. Chem. 266:8711-8719(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
[14]"Human glucocorticoid receptor gene promotor-homologous down regulation."
Govindan M.V., Pothier F., Leclerc S., Palaniswami R., Xie B.
J. Steroid Biochem. Mol. Biol. 40:317-323(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
[15]"Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product."
Weinberger C., Hollenberg S.M., Rosenfeld M.G., Evans R.M.
Nature 318:670-672(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[16]"Alternatively spliced glucocorticoid receptor messenger RNAs in glucocorticoid-resistant human multiple myeloma cells."
Moalli P.A., Pillay S., Krett N.L., Rosen S.T.
Cancer Res. 53:3877-3879(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS GP-P; GP-A ALPHA AND GP-A BETA).
[17]"Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor."
Henriksson A., Almloef T., Ford J., McEwan I.J., Gustafsson J.-A., Wright A.P.H.
Mol. Cell. Biol. 17:3065-3073(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TADA2L AND THE ADA COMPLEX, MUTAGENESIS OF PHE-191; ILE-193; LEU-194; LEU-197; TRP-213; LEU-224; LEU-225; PHE-235 AND LEU-236.
[18]"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
Fryer C.J., Archer T.K.
Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE SMARCA4 COMPLEX; NCOA1; NCOA2 AND THE CREBBP/EP300 COMPLEX.
[19]"A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity."
Schneikert J., Huebner S., Martin E., Cato A.B.C.
J. Cell Biol. 146:929-940(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG1.
[20]"Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing."
Rivers C., Levy A., Hancock J., Lightman S., Norman M.
J. Clin. Endocrinol. Metab. 84:4283-4286(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS ALPHA-2 AND BETA-2).
[21]"Steroidogenic enzyme gene expression in the human heart."
Kayes-Wandover K.M., White P.C.
J. Clin. Endocrinol. Metab. 85:2519-2525(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[22]"A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
Mahajan M.A., Samuels H.H.
Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA6.
[23]"Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor."
Diamond M.I., Robinson M.R., Yamamoto K.R.
Proc. Natl. Acad. Sci. U.S.A. 97:657-661(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT ON EXPANDED POLYGLUTAMINE PROTEIN.
[24]"Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids."
Wallace A.D., Cidlowski J.A.
J. Biol. Chem. 276:42714-42721(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
[25]"High constitutive glucocorticoid receptor beta in human neutrophils enables them to reduce their spontaneous rate of cell death in response to corticosteroids."
Strickland I., Kisich K., Hauk P.J., Vottero A., Chrousos G.P., Klemm D.J., Leung D.Y.M.
J. Exp. Med. 193:585-593(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF CELL DEATH IN RESPONSE TO CORTICOSTEROIDS.
[26]"Molecular identification and characterization of A and B forms of the glucocorticoid receptor."
Yudt M.R., Cidlowski J.A.
Mol. Endocrinol. 15:1093-1103(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION, MUTAGENESIS OF MET-1 AND MET-27.
[27]"Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor."
Tian S., Poukka H., Palvimo J.J., Jaenne O.A.
Biochem. J. 367:907-911(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, MUTAGENESIS OF LYS-277; LYS-293 AND LYS-703.
[28]"Deciphering the phosphorylation 'code' of the glucocorticoid receptor in vivo."
Wang Z., Frederick J., Garabedian M.J.
J. Biol. Chem. 277:26573-26580(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-203 AND SER-211.
[29]"Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[30]"The origin and functions of multiple human glucocorticoid receptor isoforms."
Lu N.Z., Cidlowski J.A.
Ann. N. Y. Acad. Sci. 1024:102-123(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ALTERNATIVE SPLICING, ALTERNATIVE INITIATION.
[31]"Distinct LIM domains of Hic-5/ARA55 are required for nuclear matrix targeting and glucocorticoid receptor binding and coactivation."
Guerrero-Santoro J., Yang L., Stallcup M.R., DeFranco D.B.
J. Cell. Biochem. 92:810-819(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[32]"HEXIM1 forms a transcriptionally abortive complex with glucocorticoid receptor without involving 7SK RNA and positive transcription elongation factor b."
Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H., Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H.
Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEXIM1.
[33]"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.
Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UNC45A.
[34]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications."
Nader N., Chrousos G.P., Kino T.
FASEB J. 23:1572-1583(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-480; LYS-492; LYS-494 AND LYS-495, MUTAGENESIS OF LYS-480; LYS-492; LYS-494 AND LYS-495, INTERACTION WITH CLOCK.
[38]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[39]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[40]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"Glucocorticoids induce mitochondrial gene transcription in HepG2 cells: role of the mitochondrial glucocorticoid receptor."
Psarra A.M., Sekeris C.E.
Biochim. Biophys. Acta 1813:1814-1821(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[42]"The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress."
Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.
J. Biol. Chem. 286:30152-30160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[43]"Peripheral CLOCK regulates target-tissue glucocorticoid receptor transcriptional activity in a circadian fashion in man."
Charmandari E., Chrousos G.P., Lambrou G.I., Pavlaki A., Koide H., Ng S.S., Kino T.
PLoS ONE 6:E25612-E25612(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION, INTERACTION WITH CLOCK.
[44]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[45]"Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition."
Bledsoe R.K., Montana V.G., Stanley T.B., Delves C.J., Apolito C.J., McKee D.D., Consler T.G., Parks D.J., Stewart E.L., Willson T.M., Lambert M.H., Moore J.T., Pearce K.H., Xu H.E.
Cell 110:93-105(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 521-777 OF MUTANT SER-602 IN COMPLEX WITH NCOA2; DEXAMETHASONE AND RU-486, MUTAGENESIS OF ARG-585; ASP-590; PHE-602; PRO-625 AND ILE-628.
[46]"The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism."
Kauppi B., Jakob C., Faernegaardh M., Yang J., Ahola H., Alarcon M., Calles K., Engstrom O., Harlan J., Muchmore S., Ramqvist A.-K., Thorell S., Oehman L., Greer J., Gustafsson J.-A., Carlstedt-Duke J., Carlquist M.
J. Biol. Chem. 278:22748-22754(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 500-777 OF MUTANT SER-602 IN COMPLEX WITH COACTIVATOR PEPTIDE; DEXAMETHASONE AND WITH RU-486.
[47]"Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance."
Hurley D.M., Accili D., Stratakis C.A., Karl M., Vamvakopoulos N., Rorer E., Constantine K., Taylor S.I., Chrousos G.P.
J. Clin. Invest. 87:680-686(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT GCRES VAL-641.
[48]"Cloning and expression of mutant glucocorticoid receptors from glucocorticoid-sensitive and -resistant human leukemic cells."
Powers J.H., Hillmann A.G., Tang D.C., Harmon J.M.
Cancer Res. 53:4059-4065(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TYR-421 AND PHE-753.
[49]"Familial glucocorticoid resistance caused by a splice site deletion in the human glucocorticoid receptor gene."
Karl M., Lamberts S.W.J., Detera-Wadleigh S.D., Encio I.J., Stratakis C.A., Hurley D.M., Accili D., Chrousos G.P.
J. Clin. Endocrinol. Metab. 76:683-689(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-363.
[50]"A mutation of the glucocorticoid receptor in primary cortisol resistance."
Malchoff D.M., Brufsky A., Reardon G., McDermott P., Javier E.C., Bergh C.H., Rowe D., Malchoff C.D.
J. Clin. Invest. 91:1918-1925(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GCRES ILE-729.
[51]"Identification of the activation-labile gene: a single point mutation in the human glucocorticoid receptor presents as two distinct receptor phenotypes."
Ashraf J., Thompson E.B.
Mol. Endocrinol. 7:631-642(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-753.
[52]"Lack of association between five polymorphisms in the human glucocorticoid receptor gene and glucocorticoid resistance."
Koper J.W., Stolk R.P., de Lange P., Huizenga N.A.T.M., Molijn G.-J., Pols H.A.P., Grobbee D.E., Karl M., de Jong F.H., Brinkmann A.O., Lamberts S.W.J.
Hum. Genet. 99:663-668(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-23 AND SER-363.
[53]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-23; VAL-65 AND SER-363.
[54]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[55]"Five missense variants in the amino-terminal domain of the glucocorticoid receptor: no association with puerperal psychosis or schizophrenia."
Feng J., Zheng J., Bennett W.P., Heston L.L., Jones I.R., Craddock N., Sommer S.S.
Am. J. Med. Genet. 96:412-417(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-23; LEU-29; PHE-112; ASN-233 AND SER-363.
[56]"Characterization of two novel mutations in the glucocorticoid receptor gene in patients with primary cortisol resistance."
Ruiz M., Lind U., Gaafvels M., Eggertsen G., Carlstedt-Duke J., Nilsson L., Holtmann M., Stierna P., Wikstroem A.-C., Werner S.
Clin. Endocrinol. (Oxf.) 55:363-371(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GCRES HIS-477 AND SER-679.
[57]"The N363S polymorphism of the glucocorticoid receptor: potential contribution to central obesity in men and lack of association with other risk factors for coronary heart disease and diabetes mellitus."
Dobson M.G., Redfern C.P.F., Unwin N., Weaver J.U.
J. Clin. Endocrinol. Metab. 86:2270-2274(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-363.
[58]"Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking."
Kino T., Stauber R.H., Resau J.H., Pavlakis G.N., Chrousos G.P.
J. Clin. Endocrinol. Metab. 86:5600-5608(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT GCRES ASN-559.
[59]"A polymorphism in the glucocorticoid receptor gene, which decreases sensitivity to glucocorticoids in vivo, is associated with low insulin and cholesterol levels."
van Rossum E.F.C., Koper J.W., Huizenga N.A.T.M., Uitterlinden A.G., Janssen J.A.M.J.L., Brinkmann A.O., Grobbee D.E., de Jong F.H., van Duyn C.M., Pols H.A.P., Lamberts S.W.J.
Diabetes 51:3128-3134(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-23.
[60]"Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene."
Mendonca B.B., Leite M.V., de Castro M., Kino T., Elias L.L.K., Bachega T.A.S., Arnhold I.J.P., Chrousos G.P., Latronico A.C.
J. Clin. Endocrinol. Metab. 87:1805-1809(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSEUDOHERMAPHRODITISM ALA-571.
[61]"A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators."
Vottero A., Kino T., Combe H., Lecomte P., Chrousos G.P.
J. Clin. Endocrinol. Metab. 87:2658-2667(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GCRES MET-747, ALTERED INTERACTION WITH THE COACTIVATOR NCOA2.
[62]"Association of the ER22/23EK polymorphism in the glucocorticoid receptor gene with survival and C-reactive protein levels in elderly men."
van Rossum E.F.C., Feelders R.A., van den Beld A.W., Uitterlinden A.G., Janssen J.A.M.J.L., Ester W., Brinkmann A.O., Grobbee D.E., de Jong F.H., Pols H.A.P., Koper J.W., Lamberts S.W.J.
Am. J. Med. 117:158-162(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-23.
[63]"The ER22/23EK polymorphism in the glucocorticoid receptor gene is associated with a beneficial body composition and muscle strength in young adults."
van Rossum E.F.C., Voorhoeve P.G., te Velde S.J., Koper J.W., Delemarre-van de Waal H.A., Kemper H.C.G., Lamberts S.W.J.
J. Clin. Endocrinol. Metab. 89:4004-4009(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-23.
+Additional computationally mapped references.

Web resources

GeneReviews
NIEHS-SNPs
Wikipedia

Glucocorticoid receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03225 mRNA. Translation: CAA26976.1.
X03348 mRNA. Translation: CAA27054.1.
U80946 expand/collapse EMBL AC list , U78506, U78507, U78508, U78509, U78510, U78511, U78512 Genomic DNA. Translation: AAB64353.1.
U80947 expand/collapse EMBL AC list , U78506, U78507, U78508, U78509, U78510, U78511, U78512 Genomic DNA. Translation: AAB64354.1.
HQ205546 Genomic DNA. Translation: ADP91135.1.
HQ205547 Genomic DNA. Translation: ADP91138.1.
HQ205548 Genomic DNA. Translation: ADP91141.1.
HQ205549 Genomic DNA. Translation: ADP91144.1.
HQ205550 Genomic DNA. Translation: ADP91147.1.
HQ205551 Genomic DNA. Translation: ADP91150.1.
HQ205552 Genomic DNA. Translation: ADP91153.1.
HQ205553 Genomic DNA. Translation: ADP91156.1.
HQ205554 Genomic DNA. Translation: ADP91159.1.
HQ205555 Genomic DNA. Translation: ADP91162.1.
HQ205556 Genomic DNA. Translation: ADP91165.1.
HQ205557 Genomic DNA. Translation: ADP91168.1.
HQ205558 Genomic DNA. Translation: ADP91171.1.
HQ205559 Genomic DNA. Translation: ADP91174.1.
HQ205560 Genomic DNA. Translation: ADP91177.1.
HQ205561 Genomic DNA. Translation: ADP91180.1.
HQ205562 Genomic DNA. Translation: ADP91183.1.
HQ205563 Genomic DNA. Translation: ADP91186.1.
HQ205564 Genomic DNA. Translation: ADP91189.1.
HQ205565 Genomic DNA. Translation: ADP91192.1.
HQ205566 Genomic DNA. Translation: ADP91195.1.
HQ205567 Genomic DNA. Translation: ADP91198.1.
HQ205568 Genomic DNA. Translation: ADP91201.1.
HQ205569 Genomic DNA. Translation: ADP91204.1.
HQ205570 Genomic DNA. Translation: ADP91207.1.
HQ205571 Genomic DNA. Translation: ADP91210.1.
HQ205572 Genomic DNA. Translation: ADP91213.1.
HQ205573 Genomic DNA. Translation: ADP91216.1.
HQ205574 Genomic DNA. Translation: ADP91219.1.
HQ205575 Genomic DNA. Translation: ADP91222.1.
HQ205576 Genomic DNA. Translation: ADP91225.1.
HQ205577 Genomic DNA. Translation: ADP91228.1.
HQ205578 Genomic DNA. Translation: ADP91231.1.
HQ205579 Genomic DNA. Translation: ADP91234.1.
HQ205580 Genomic DNA. Translation: ADP91237.1.
HQ205581 Genomic DNA. Translation: ADP91240.1.
HQ205582 Genomic DNA. Translation: ADP91243.1.
HQ205583 Genomic DNA. Translation: ADP91246.1.
HQ205584 Genomic DNA. Translation: ADP91249.1.
HQ205585 Genomic DNA. Translation: ADP91252.1.
AM183262 mRNA. Translation: CAJ65924.1.
U01351 mRNA. Translation: AAA16603.1.
AK223594 mRNA. Translation: BAD97314.1.
BX640610 mRNA. Translation: CAE45716.1.
AY436590 Genomic DNA. Translation: AAQ97180.1.
EU332858 Genomic DNA. Translation: ABY87547.1.
AC005601 Genomic DNA. Translation: AAC34207.1.
AC004782 Genomic DNA. No translation available.
AC091925 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61872.1.
CH471062 Genomic DNA. Translation: EAW61873.1.
BC015610 mRNA. Translation: AAH15610.1.
M69104 Genomic DNA. Translation: AAA88049.1.
AH002750 Genomic DNA. Translation: AAA53151.1.
S68378 Genomic DNA. Translation: AAB20466.1.
PIRQRHUGA. A93370.
QRHUGB. B93370.
RefSeqNP_000167.1. NM_000176.2.
NP_001018084.1. NM_001018074.1.
NP_001018085.1. NM_001018075.1.
NP_001018086.1. NM_001018076.1.
NP_001018087.1. NM_001018077.1.
NP_001018661.1. NM_001020825.1.
NP_001019265.1. NM_001024094.1.
NP_001191187.1. NM_001204258.1.
NP_001191188.1. NM_001204259.1.
NP_001191189.1. NM_001204260.1.
NP_001191190.1. NM_001204261.1.
NP_001191191.1. NM_001204262.1.
NP_001191192.1. NM_001204263.1.
NP_001191193.1. NM_001204264.1.
XP_005268476.1. XM_005268419.2.
XP_005268477.1. XM_005268420.2.
XP_005268478.1. XM_005268421.2.
XP_005268479.1. XM_005268422.2.
XP_005268480.1. XM_005268423.2.
UniGeneHs.122926.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2ZX-ray2.50A/D521-777[»]
1NHZX-ray2.30A500-777[»]
1P93X-ray2.70A/B/C/D500-777[»]
3BQDX-ray2.50A525-777[»]
3CLDX-ray2.84A/B521-777[»]
3E7CX-ray2.15A/B521-777[»]
3H52X-ray2.80A/B/C/D528-777[»]
3K22X-ray2.10A/B521-777[»]
3K23X-ray3.00A/B/C521-777[»]
4HN5X-ray1.90A/B417-506[»]
4HN6X-ray2.55A/B417-506[»]
4LSJX-ray2.35A522-777[»]
DisProtDP00030.
ProteinModelPortalP04150.
SMRP04150. Positions 418-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109165. 146 interactions.
DIPDIP-576N.
IntActP04150. 53 interactions.
MINTMINT-150603.
STRING9606.ENSP00000231509.

Chemistry

BindingDBP04150.
ChEMBLCHEMBL2034.
DrugBankDB00288. Amcinonide.
DB00443. Betamethasone.
DB01222. Budesonide.
DB01234. Dexamethasone.
DB00663. Flumethasone Pivalate.
DB00180. Flunisolide.
DB00588. Fluticasone Propionate.
DB00769. Hydrocortamate.
DB00741. Hydrocortisone.
DB00873. Loteprednol Etabonate.
DB00959. Methylprednisolone.
DB00834. Mifepristone.
DB00764. Mometasone.
DB00635. Prednisone.
GuidetoPHARMACOLOGY625.

PTM databases

PhosphoSiteP04150.

Polymorphism databases

DMDM121069.

Proteomic databases

PaxDbP04150.
PRIDEP04150.

Protocols and materials databases

DNASU2908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231509; ENSP00000231509; ENSG00000113580. [P04150-3]
ENST00000343796; ENSP00000343205; ENSG00000113580. [P04150-1]
ENST00000394464; ENSP00000377977; ENSG00000113580. [P04150-1]
ENST00000394466; ENSP00000377979; ENSG00000113580. [P04150-3]
ENST00000415690; ENSP00000387672; ENSG00000113580. [P04150-2]
ENST00000424646; ENSP00000405282; ENSG00000113580. [P04150-10]
ENST00000503201; ENSP00000427672; ENSG00000113580. [P04150-1]
ENST00000504572; ENSP00000422518; ENSG00000113580. [P04150-3]
GeneID2908.
KEGGhsa:2908.
UCSCuc003lmz.3. human. [P04150-1]

Organism-specific databases

CTD2908.
GeneCardsGC05M142639.
HGNCHGNC:7978. NR3C1.
HPACAB010435.
HPA004248.
MIM138040. gene+phenotype.
neXtProtNX_P04150.
Orphanet786. Glucocorticoid resistance.
PharmGKBPA181.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270250.
HOGENOMHOG000037950.
HOVERGENHBG007583.
KOK05771.
OMAQSTFDIL.
OrthoDBEOG7B31M9.
PhylomeDBP04150.
TreeFamTF106510.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP04150.

Gene expression databases

ArrayExpressP04150.
BgeeP04150.
CleanExHS_NR3C1.
GenevestigatorP04150.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR001409. Glcrtcd_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF02155. GCR. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNR3C1. human.
EvolutionaryTraceP04150.
GeneWikiGlucocorticoid_receptor.
GenomeRNAi2908.
NextBio11517.
PROP04150.
SOURCESearch...

Entry information

Entry nameGCR_HUMAN
AccessionPrimary (citable) accession number: P04150
Secondary accession number(s): A0ZXF9 expand/collapse secondary AC list , B0LPG8, D3DQF4, P04151, Q53EP5, Q6N0A4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: April 16, 2014
This is version 204 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM