P06536 (GCR_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucocorticoid receptor
Short name=GR

Alternative name(s):
Nuclear receptor subfamily 3 group C member 1

Gene names

Name:	Nr3c1
Synonyms:	Grl

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	795 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Plays a significant role in transactivation By similarity. Ref.19
Subunit structure	Heteromultimeric cytoplasmic complex with HSP90, HSP70, and FKBP5 or another immunophilin, or the immunophilin homolog PPP5C. Directly interacts with UNC45A. 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. 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, TGFB1I1, 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 By similarity. Interacts with NCOA1, NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1. 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	Increased proteasome-mediated degradation in response to glucocorticoids. Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative initiation Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Chromatin regulator Receptor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging 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-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 apoptotic process Inferred from mutant phenotype PubMed 16175607. Source: RGD negative regulation of synaptic plasticity Inferred from mutant phenotype PubMed 22918985. Source: RGD negative regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype PubMed 16175607. 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 stimulus Inferred from expression pattern PubMed 16673181. 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 stimulus 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 16809634. Source: RGD mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 16175607PubMed 23152847. Source: RGD postsynaptic density Inferred from direct assay PubMed 21179518. Source: RGD protein complex Inferred from direct assay PubMed 12672265. Source: RGD
Molecular_function	Hsp70 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 mutant phenotype PubMed 16175607. Source: RGD hormone binding Inferred from physical interaction PubMed 21325249. Source: RGD protein complex binding Inferred from direct assay PubMed 17827210. Source: UniProtKB protein heterodimerization activity Inferred from direct assay Ref.10. Source: RGD protein homodimerization activity Inferred from direct assay Ref.10. 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 zinc ion binding Traceable author statement PubMed 15310238. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Mvp	Q62667	2	EBI-1187143,EBI-918333
NCOA1	Q15788	2	EBI-1187143,EBI-455189	From a different organism.
SMARCA4	P51532	3	EBI-1187143,EBI-302489	From a different organism.
SMARCD1	Q96GM5	2	EBI-1187143,EBI-358489	From 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 795

795

Glucocorticoid receptor

PRO_0000019941

Regions

DNA binding

440 – 505

66

Nuclear receptor

Zinc finger

440 – 460

21

NR C4-type

Zinc finger

476 – 500

25

NR C4-type

Region

1 – 439

439

Modulating

Region

506 – 546

41

Hinge

Region

547 – 795

249

Steroid-binding

Compositional bias

75 – 97

23

Poly-Gln

Compositional bias

419 – 438

20

Glu/Pro/Ser/Thr-rich (PEST region)

Amino acid modifications

Modified residue

134

1

Phosphoserine By similarity

Modified residue

155

1

Phosphoserine By similarity

Modified residue

162

1

Phosphoserine By similarity

Modified residue

171

1

Phosphothreonine Ref.12

Modified residue

224

1

Phosphoserine Ref.12

Modified residue

232

1

Phosphoserine Ref.12

Modified residue

246

1

Phosphoserine Ref.12

Modified residue

287

1

Phosphoserine By similarity

Modified residue

327

1

Phosphoserine By similarity

Cross-link

297

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

313

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

438

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Natural variations

Alternative sequence

1 – 27

27

Missing in isoform B.

VSP_018969

Natural variant

77

1

Missing in strain: Brown Norway/Crl.

Natural variant

78 – 79

2

Missing in strain: SHR/OlaIpcv.

Natural variant

83 – 96

14

Missing in strain: Sprague-Dawley.

Natural variant

226

1

S → G in strain: SHR/OlaIpcv and Brown Norway/Crl. Ref.3

Natural variant

260

1

N → D in strain: SHR/OlaIpcv and Brown Norway/Crl. Ref.3

Experimental info

Mutagenesis

1

1

M → T: Abolishes expression of A-type isoforms. Ref.5 Ref.8 Ref.17

Mutagenesis

28

1

M → T: Abolishes expression of B-type isoforms. Ref.5 Ref.8 Ref.17

Mutagenesis

481

1

D → R: Disrupts dimerization and decreases transcription transactivation. Ref.5 Ref.8 Ref.10

Mutagenesis

488

1

R → Q: Loss of chromatin specific function and reduces chromatin remodeling. Abolishes interaction with SMARD1. Ref.5 Ref.8 Ref.19

Mutagenesis

500

1

C → Y: Abolishes interaction with POU2F2. Ref.5 Ref.8 Ref.14

Mutagenesis

501

1

L → P: Abrogates DNA-binding and transcription transactivation. Abolishes interaction with POU2F1 and POU2F2. Ref.5 Ref.8 Ref.14 Ref.16

Mutagenesis

656

1

C → S: Strongly increases affinity for dexamethasone. Ref.5 Ref.7 Ref.8

Mutagenesis

773

1

E → A: Abolishes interaction with NCOA1 and reduces transcription transactivation; when associated with S-656. Ref.5 Ref.8 Ref.18

Sequence conflict

95 – 96

2

Missing in AAL78956. Ref.3

Sequence conflict

98

1

D → G in AAA41203. Ref.1

Sequence conflict

345

1

S → T in CAA68545. Ref.4

Sequence conflict

600

1

L → P in CAA72938. Ref.2

Sequence conflict

600

1

L → P in AAL66772. Ref.3

Sequence conflict

600

1

L → P in AAL78956. Ref.3

Sequence conflict

602

1

L → F in AAL66772. Ref.3

Sequence conflict

602

1

L → F in AAL78956. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

795

Helix Strand Turn

Details...

Turn

441 – 443

3

Beta strand

444 – 446

3

Beta strand

449 – 451

3

Beta strand

454 – 456

3

Helix

458 – 469

12

Beta strand

477 – 480

4

Helix

488 – 490

3

Helix

493 – 503

11

Helix

509 – 513

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 9C9DE0B1D6724845	FASTA	795	87,556
	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
	Isoform B [UniParc]. Checksum: D6E586FE0E91597F	FASTA	768	84,834
	10 20 30 40 50 60 MDFYKSLRGG ATVKVSASSP SVAAASQADS KQQRILLDFS KGSTSNVQQR QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQP DLSKAVSLSM GLYMGETETK VMGNDLGYPQ QGQLGLSSGE TDFRLLEESI 130 140 150 160 170 180 ANLNRSTSVP ENPKSSTSAT GCATPTEKEF PKTHSDASSE QQNRKSQTGT NGGSVKLYPT 190 200 210 220 230 240 DQSTFDLLKD LEFSAGSPSK DTNESPWRSD LLIDENLLSP LAGEDDPFLL EGNTNEDCKP 250 260 270 280 290 300 LILPDTKPKI KDTGDTILSS PSSVALPQVK TEKDDFIELC TPGVIKQEKL GPVYCQASFS 310 320 330 340 350 360 GTNIIGNKMS AISVHGVSTS GGQMYHYDMN TASLSQQQDQ KPVFNVIPPI PVGSENWNRC 370 380 390 400 410 420 QGSGEDSLTS LGALNFPGRS VFSNGYSSPG MRPDVSSPPS SSSAATGPPP KLCLVCSDEA 430 440 450 460 470 480 SGCHYGVLTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI RRKNCPACRY RKCLQAGMNL 490 500 510 520 530 540 EARKTKKKIK GIQQATAGVS QDTSENPNKT IVPAALPQLT PTLVSLLEVI EPEVLYAGYD 550 560 570 580 590 600 SSVPDSAWRI MTTLNMLGGR QVIAAVKWAK AILGLRNLHL DDQMTLLQYS WMFLMAFALG 610 620 630 640 650 660 WRSYRQSSGN LLCFAPDLII NEQRMSLPCM YDQCKHMLFV SSELQRLQVS YEEYLCMKTL 670 680 690 700 710 720 LLLSSVPKEG LKSQELFDEI RMTYIKELGK AIVKREGNSS QNWQRFYQLT KLLDSMHEVV 730 740 750 760 ENLLTYCFQT FLDKTMSIEF PEMLAEIITN QIPKYSNGNI KKLLFHQK

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]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.

IPI

IPI00326099.
IPI00563755.

PIR

QRRTG. A24194.

RefSeq

NP_036708.2. NM_012576.2.

UniGene

Rn.90070.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GDC	NMR	-	A	439-510	[»]
1GLU	X-ray	2.90	A/B	440-514	[»]
1LAT	X-ray	1.90	A/B	440-515	[»]
1R4O	X-ray	2.50	A/B	440-525	[»]
1R4R	X-ray	3.00	A/B	440-525	[»]
1RGD	NMR	-	A	440-510	[»]
2GDA	NMR	-	A	439-510	[»]
3FYL	X-ray	1.63	A/B	440-525	[»]
3G6P	X-ray	1.99	A/B	440-525	[»]
3G6Q	X-ray	2.26	A/B	440-525	[»]
3G6R	X-ray	2.30	A/B	440-525	[»]
3G6T	X-ray	1.90	A/B	440-525	[»]
3G6U	X-ray	1.90	A/B	440-525	[»]
3G8U	X-ray	1.90	A/B	440-525	[»]
3G8X	X-ray	2.05	A/B	440-525	[»]
3G97	X-ray	2.08	A/B	440-525	[»]
3G99	X-ray	1.81	A/B	440-525	[»]
3G9I	X-ray	1.85	A/B	440-525	[»]
3G9J	X-ray	2.32	A/B	440-525	[»]
3G9M	X-ray	1.61	A/B	440-525	[»]
3G9O	X-ray	1.65	A/B	440-525	[»]
3G9P	X-ray	1.65	A/B	440-525	[»]

ProteinModelPortal

P06536.

SMR

P06536. Positions 439-510, 541-795.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38940N.

IntAct

P06536. 29 interactions.

PTM databases

PhosphoSite

P06536.

Proteomic databases

PaxDb

P06536.

PRIDE

P06536.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24413.

KEGG

rno:24413.

UCSC

RGD:2741. rat.

Organism-specific databases

CTD

2908.

RGD

2741. Nr3c1.

Phylogenomic databases

eggNOG

NOG270250.

HOGENOM

HOG000037950.

HOVERGEN

HBG007583.

InParanoid

P06536.

KO

K05771.

OrthoDB

EOG402WRW.

Gene expression databases

ArrayExpress

P06536.

Genevestigator

P06536.

GermOnline

ENSRNOG00000014096. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.
3.30.50.10. 1 hit.

InterPro

IPR001409. 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]

Pfam

PF02155. GCR. 2 hits.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06536.

ChEMBL

CHEMBL3368.

EvolutionaryTrace

P06536.

NextBio

603243.

Entry information

Entry name

GCR_RAT

Accession

Primary (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:	May 1, 2013
This is version 165 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program