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P06536 (GCR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length795 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 By similarity. Ref.19

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, CRY1 and CRY2 in a ligand-dependent fashion. Interacts with CIART. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity. Note: Cytoplasmic in the absence of ligand, nuclear after ligand-binding By similarity.

Domain

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

Post-translational modification

Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity By similarity.

Increased proteasome-mediated degradation in response to glucocorticoids.

Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. May be dephosphorylated by PPP5C, attenuates NR3C1 action By similarity. Ref.12

Sumoylated; this reduces transcription transactivation By similarity.

Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling By similarity.

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
Polymorphism
   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_processaging

Inferred from expression pattern PubMed 18758953. Source: RGD

androgen metabolic process

Inferred from expression pattern PubMed 8809674. Source: RGD

brain development

Inferred from expression pattern PubMed 17344647. Source: RGD

cellular response to dexamethasone stimulus

Inferred from mutant phenotype PubMed 12145311. Source: RGD

cellular response to magnesium ion

Inferred from expression pattern PubMed 20350433. Source: RGD

chromatin remodeling

Inferred from mutant phenotype Ref.19. Source: UniProtKB

chromatin-mediated maintenance of transcription

Inferred from mutant phenotype Ref.19. Source: UniProtKB

circadian rhythm

Inferred from expression pattern PubMed 16673181. Source: RGD

lung development

Inferred from expression pattern PubMed 16371448. Source: RGD

muscle atrophy

Inferred from expression pattern PubMed 17622304. Source: RGD

negative regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 22918985. Source: RGD

negative regulation of vascular permeability

Inferred from mutant phenotype PubMed 7648494. Source: RGD

positive regulation of cell growth involved in cardiac muscle cell development

Inferred from mutant phenotype PubMed 22989630. Source: RGD

positive regulation of dendritic spine development

Inferred from mutant phenotype PubMed 22509272. Source: RGD

positive regulation of glucocorticoid receptor signaling pathway

Inferred from direct assay PubMed 22001115. Source: RGD

positive regulation of glutamate secretion

Inferred from mutant phenotype PubMed 19484722. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15310238. Source: RGD

regulation of cell proliferation

Inferred from direct assay PubMed 16115202. Source: RGD

regulation of glucose metabolic process

Inferred from mutant phenotype PubMed 17292727. Source: RGD

response to activity

Inferred from expression pattern PubMed 17557067. Source: RGD

response to arsenic-containing substance

Inferred from direct assay PubMed 15310238. Source: RGD

response to calcium ion

Inferred from expression pattern PubMed 22142627. Source: RGD

response to corticosterone

Inferred from expression pattern PubMed 16673181. Source: RGD

response to dexamethasone

Inferred from expression pattern PubMed 21804312. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 22040414. Source: RGD

response to inactivity

Inferred from expression pattern PubMed 22036623. Source: RGD

response to insulin

Inferred from expression pattern PubMed 16646523. Source: RGD

response to mercury ion

Inferred from expression pattern PubMed 17177174. Source: RGD

response to radiation

Inferred from expression pattern PubMed 17535653. Source: RGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16809634. Source: RGD

dendritic spine

Inferred from direct assay PubMed 21179518. Source: RGD

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from direct assay PubMed 19484722. Source: RGD

nucleus

Inferred from direct assay PubMed 23152847. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 21179518. Source: RGD

protein complex

Inferred from direct assay PubMed 12672265. Source: RGD

   Molecular_functionHsp70 protein binding

Inferred from direct assay PubMed 17177174. Source: RGD

Hsp90 protein binding

Inferred from direct assay PubMed 16175607PubMed 17177174. Source: RGD

RNA polymerase II regulatory region DNA binding

Inferred from direct assay PubMed 21664419. Source: RGD

chromatin binding

Inferred from direct assay PubMed 15808513. Source: RGD

double-stranded DNA binding

Inferred from direct assay Ref.10. Source: RGD

glucocorticoid receptor activity

Inferred from electronic annotation. Source: InterPro

heat shock protein binding

Inferred from direct assay PubMed 12145311. Source: RGD

hormone binding

Inferred from physical interaction PubMed 21325249. Source: RGD

protein binding

Inferred from physical interaction Ref.19PubMed 17827210. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 17827210. Source: UniProtKB

protein dimerization activity

Traceable author statement PubMed 15310238. Source: RGD

protein heterodimerization activity

Inferred from direct assay Ref.10. Source: RGD

protein homodimerization activity

Inferred from direct assay Ref.10. Source: RGD

receptor tyrosine kinase binding

Inferred from physical interaction PubMed 18261979. Source: RGD

sequence-specific DNA binding

Inferred from direct assay Ref.10PubMed 9001244. Source: RGD

sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.10. Source: RGD

steroid binding

Inferred from physical interaction PubMed 12145311. Source: RGD

transcription coactivator activity

Inferred from direct assay PubMed 12145311. Source: RGD

transcription factor binding

Inferred from physical interaction PubMed 20155810. Source: RGD

zinc ion binding

Traceable author statement PubMed 15310238. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MvpQ626672EBI-1187143,EBI-918333
NCOA1Q157882EBI-1187143,EBI-455189From a different organism.
SMARCA4P515323EBI-1187143,EBI-302489From a different organism.
SMARCD1Q96GM52EBI-1187143,EBI-358489From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform A (identifier: P06536-1)

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.
Isoform B (identifier: P06536-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Glucocorticoid receptor
PRO_0000019941

Regions

DNA binding440 – 50566Nuclear receptor
Zinc finger440 – 46021NR C4-type
Zinc finger476 – 50025NR C4-type
Region1 – 439439Modulating
Region504 – 795292Interaction with CLOCK By similarity
Region506 – 54641Hinge
Region547 – 795249Steroid-binding
Region550 – 715166Interaction with CRY1 By similarity
Compositional bias75 – 9723Poly-Gln
Compositional bias419 – 43820Glu/Pro/Ser/Thr-rich (PEST region)

Amino acid modifications

Modified residue1341Phosphoserine By similarity
Modified residue1551Phosphoserine By similarity
Modified residue1621Phosphoserine By similarity
Modified residue1711Phosphothreonine Ref.12
Modified residue2241Phosphoserine Ref.12
Modified residue2321Phosphoserine Ref.12
Modified residue2461Phosphoserine Ref.12
Modified residue2871Phosphoserine By similarity
Modified residue3271Phosphoserine By similarity
Modified residue4991N6-acetyllysine By similarity
Modified residue5111N6-acetyllysine By similarity
Modified residue5131N6-acetyllysine By similarity
Modified residue5141N6-acetyllysine By similarity
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Natural variations

Alternative sequence1 – 2727Missing in isoform B.
VSP_018969
Natural variant771Missing in strain: Brown Norway/Crl.
Natural variant78 – 792Missing in strain: SHR/OlaIpcv.
Natural variant83 – 9614Missing in strain: Sprague-Dawley.
Natural variant2261S → G in strain: SHR/OlaIpcv and Brown Norway/Crl. Ref.3
Natural variant2601N → D in strain: SHR/OlaIpcv and Brown Norway/Crl. Ref.3

Experimental info

Mutagenesis11M → T: Abolishes expression of A-type isoforms. Ref.5 Ref.8 Ref.17
Mutagenesis281M → T: Abolishes expression of B-type isoforms. Ref.5 Ref.8 Ref.17
Mutagenesis4811D → R: Disrupts dimerization and decreases transcription transactivation. Ref.5 Ref.8 Ref.10
Mutagenesis4881R → Q: Loss of chromatin specific function and reduces chromatin remodeling. Abolishes interaction with SMARD1. Ref.5 Ref.8 Ref.19
Mutagenesis5001C → Y: Abolishes interaction with POU2F2. Ref.5 Ref.8 Ref.14
Mutagenesis5011L → P: Abrogates DNA-binding and transcription transactivation. Abolishes interaction with POU2F1 and POU2F2. Ref.5 Ref.8 Ref.14 Ref.16
Mutagenesis6561C → S: Strongly increases affinity for dexamethasone. Ref.5 Ref.7 Ref.8
Mutagenesis7731E → A: Abolishes interaction with NCOA1 and reduces transcription transactivation; when associated with S-656. Ref.5 Ref.8 Ref.18
Sequence conflict95 – 962Missing in AAL78956. Ref.3
Sequence conflict981D → G in AAA41203. Ref.1
Sequence conflict3451S → T in CAA68545. Ref.4
Sequence conflict6001L → P in CAA72938. Ref.2
Sequence conflict6001L → P in AAL66772. Ref.3
Sequence conflict6001L → P in AAL78956. Ref.3
Sequence conflict6021L → F in AAL66772. Ref.3
Sequence conflict6021L → F in AAL78956. Ref.3

Secondary structure

.................. 795
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1995. Version 2.
Checksum: 9C9DE0B1D6724845

FASTA79587,556
        10         20         30         40         50         60 
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ 

        70         80         90        100        110        120 
RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS KAVSLSMGLY MGETETKVMG 

       130        140        150        160        170        180 
NDLGYPQQGQ LGLSSGETDF RLLEESIANL NRSTSVPENP KSSTSATGCA TPTEKEFPKT 

       190        200        210        220        230        240 
HSDASSEQQN RKSQTGTNGG SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI 

       250        260        270        280        290        300 
DENLLSPLAG EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK 

       310        320        330        340        350        360 
DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS 

       370        380        390        400        410        420 
LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA LNFPGRSVFS NGYSSPGMRP 

       430        440        450        460        470        480 
DVSSPPSSSS AATGPPPKLC LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN 

       490        500        510        520        530        540 
DCIIDKIRRK NCPACRYRKC LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP 

       550        560        570        580        590        600 
AALPQLTPTL VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL 

       610        620        630        640        650        660 
GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ RMSLPCMYDQ 

       670        680        690        700        710        720 
CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS QELFDEIRMT YIKELGKAIV 

       730        740        750        760        770        780 
KREGNSSQNW QRFYQLTKLL DSMHEVVENL LTYCFQTFLD KTMSIEFPEM LAEIITNQIP 

       790 
KYSNGNIKKL LFHQK 

« Hide

Isoform B [UniParc].

Checksum: D6E586FE0E91597F
Show »

FASTA76884,834

References

« Hide 'large scale' references
[1]"Genetic complementation of a glucocorticoid receptor deficiency by expression of cloned receptor cDNA."
Miesfeld R., Rusconi S., Godowski P.J., Maler B.A., Okret S., Wikstroem A.-C., Gustafsson J.-A., Yamamoto K.R.
Cell 46:389-399(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[2]"CAG repeat variation in the gene for rat glucocorticoid receptor: a study of allele frequencies in inbred and wild rat populations and of the steroid-binding properties of their polypeptides in vitro."
Heeley R.P., Gill E., van Zutphen B.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genetic isolation of a QTL on chromosome 18 associated with salt sensitivity in spontaneously hypertensive rats."
Pravenec M., Zidek V., Kostka V., Mlejnek P., Musilova A., Kren V., Jansa P., Forejt J., Lezin E.S., Kurtz T.W.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-226 AND ASP-260.
Strain: Brown Norway/Crl and SHR/OlaIpcv.
[4]"Cloning and sequence analysis of the rat ventral prostate glucocorticoid receptor cDNA."
Chang C., Kokontis J., Chang C.T., Liao S.
Nucleic Acids Res. 15:9603-9603(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-515.
Strain: Sprague-Dawley.
Tissue: Prostate.
[5]"Metal binding 'finger' structures in the glucocorticoid receptor defined by site-directed mutagenesis."
Severne Y., Wieland S., Schaffner W., Rusconi S.
EMBO J. 7:2503-2508(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ZINC-FINGER.
[6]"Regulation of glucocorticoid receptor expression: evidence for transcriptional and posttranslational mechanisms."
Dong Y., Poellinger L., Gustafsson J.-A., Okret S.
Mol. Endocrinol. 2:1256-1264(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
[7]"Creation of 'super' glucocorticoid receptors by point mutations in the steroid binding domain."
Chakraborti P.K., Garabedian M.J., Yamamoto K.R., Simons S.S. Jr.
J. Biol. Chem. 266:22075-22078(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-656.
[8]"Zinc finger mutations that alter domain interactions in the glucocorticoid receptor."
Zandi E., Galli I., Doebbeling U., Rusconi S.
J. Mol. Biol. 230:124-136(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ZINC-FINGER.
[9]"Active, interactive, and inactive steroid receptor mutants."
Lanz R.B., Hug M., Gola M., Tallone T., Wieland S., Rusconi S.
Steroids 59:148-152(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON MUTAGENESIS.
[10]"Steroid receptor heterodimerization demonstrated in vitro and in vivo."
Liu W., Wang J., Sauter N.K., Pearce D.
Proc. Natl. Acad. Sci. U.S.A. 92:12480-12484(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, MUTAGENESIS OF ASP-481.
[11]"GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors."
Hong H., Kohli K., Garabedian M.J., Stallcup M.R.
Mol. Cell. Biol. 17:2735-2744(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA2.
[12]"Phosphorylation and inhibition of rat glucocorticoid receptor transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-specific differences between human and rat glucocorticoid receptor signaling as revealed through GSK-3 phosphorylation."
Rogatsky I., Waase C.L.M., Garabedian M.J.
J. Biol. Chem. 273:14315-14321(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-171; SER-224; SER-232 AND SER-246.
[13]"Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids."
Subramaniam N., Treuter E., Okret S.
J. Biol. Chem. 274:18121-18127(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[14]"Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter."
Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L., Hache R.J.G.
J. Biol. Chem. 274:26713-26719(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POU2F1 AND POU2F2, MUTAGENESIS OF CYS-500 AND LEU-501.
[15]"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.
[16]"Heterodimerization of mineralocorticoid and glucocorticoid receptors at a novel negative response element of the 5-HT1A receptor gene."
Ou X.-M., Storring J.M., Kushwaha N., Albert P.R.
J. Biol. Chem. 276:14299-14307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, HETERODIMERIZATION WITH NR3C2, MUTAGENESIS OF LEU-501.
[17]"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-28.
[18]"A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1."
Kucera T., Waltner-Law M., Scott D.K., Prasad R., Granner D.K.
J. Biol. Chem. 277:26098-26102(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA1, MUTAGENESIS OF GLU-773.
[19]"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NCOA1; NCOA3; SMARCA4; SMARCC1; SMARCD1 AND SMARCE1, MUTAGENESIS OF ARG-488.
[20]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA."
Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., Sigler P.B.
Nature 352:497-505(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 434-525.
[22]"Solution structure of the glucocorticoid receptor DNA-binding domain."
Haerd T., Kellenbach E., Boelens R., Maler B.A., Dahlman K., Freedman L.P., Carlstedt-Duke J., Yamamoto K.R., Gustafsson J.-A., Kaptein R.
Science 249:157-160(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 440-510.
[23]"1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element."
Remerowski M.L., Kellenbach E., Boelens R., van der Marel A., van Boom J.H., Maler B.A., Yamamoto K.R., Kaptein R.
Biochemistry 30:11620-11624(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 440-525.
[24]"Identification of the metal coordinating residues in the DNA binding domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR spectroscopy."
Kellenbach E., Maler B.A., Yamamoto K.R., Boelens R., Kaptein R.
FEBS Lett. 291:367-370(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 440-525.
[25]"Refined solution structure of the glucocorticoid receptor DNA-binding domain."
Baumann H., Paulsen K., Kovacs H., Berglund H., Wright A.P.H., Gustafsson J.-A., Haerd T.
Biochemistry 32:13463-13471(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 439-510.
[26]"Heterogeneity in the polyglutamine tract of the glucocorticoid receptor from different rat strains."
Gearing K.L., Gustafsson J.-A., Okret S.
Nucleic Acids Res. 21:2014-2014(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF POLY-GLN REGION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14053 mRNA. Translation: AAA41203.1.
Y12264 mRNA. Translation: CAA72938.1.
AY066016 mRNA. Translation: AAL66772.2.
AF455050 mRNA. Translation: AAL78956.1.
Y00489 mRNA. Translation: CAA68545.1.
X69666 Genomic DNA. No translation available.
X69667 Genomic DNA. No translation available.
X69668 Genomic DNA. No translation available.
X69669 Genomic DNA. No translation available.
X69670 Genomic DNA. No translation available.
PIRQRRTG. A24194.
RefSeqNP_036708.2. NM_012576.2.
UniGeneRn.90070.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GDCNMR-A439-510[»]
1GLUX-ray2.90A/B440-514[»]
1LATX-ray1.90A/B440-515[»]
1R4OX-ray2.50A/B440-525[»]
1R4RX-ray3.00A/B440-525[»]
1RGDNMR-A440-510[»]
2GDANMR-A439-510[»]
3FYLX-ray1.63A/B440-525[»]
3G6PX-ray1.99A/B440-525[»]
3G6QX-ray2.26A/B440-525[»]
3G6RX-ray2.30A/B440-525[»]
3G6TX-ray1.90A/B440-525[»]
3G6UX-ray1.90A/B440-525[»]
3G8UX-ray1.90A/B440-525[»]
3G8XX-ray2.05A/B440-525[»]
3G97X-ray2.08A/B440-525[»]
3G99X-ray1.81A/B440-525[»]
3G9IX-ray1.85A/B440-525[»]
3G9JX-ray2.32A/B440-525[»]
3G9MX-ray1.61A/B440-525[»]
3G9OX-ray1.65A/B440-525[»]
3G9PX-ray1.65A/B440-525[»]
ProteinModelPortalP06536.
SMRP06536. Positions 439-510, 541-795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246578. 15 interactions.
DIPDIP-38940N.
IntActP06536. 29 interactions.
MINTMINT-194828.

Chemistry

BindingDBP06536.
ChEMBLCHEMBL3368.
GuidetoPHARMACOLOGY625.

PTM databases

PhosphoSiteP06536.

Proteomic databases

PaxDbP06536.
PRIDEP06536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24413.
KEGGrno:24413.
UCSCRGD:2741. rat. [P06536-1]

Organism-specific databases

CTD2908.
RGD2741. Nr3c1.

Phylogenomic databases

eggNOGNOG270250.
HOGENOMHOG000037950.
HOVERGENHBG007583.
InParanoidP06536.
KOK05771.
PhylomeDBP06536.

Gene expression databases

GenevestigatorP06536.

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. 2 hits.
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

EvolutionaryTraceP06536.
NextBio603243.
PROP06536.

Entry information

Entry nameGCR_RAT
AccessionPrimary (citable) accession number: P06536
Secondary accession number(s): O08624, Q8R463, Q8R5J0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references