Reviewed, UniProtKB/Swiss-Prot P04150 (GCR_HUMAN)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	777 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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) 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. Involved in nuclear translocation By similarity.
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 By similarity. Binds to DNA as a homodimer, and as a heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers. Interacts with NRIP1, POU2F1, POU2F2 and TRIM28. Interacts with NCOA1, NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 By similarity. Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L and p160 coactivators such as NCOA2 and NCOA6. Interaction with BAG1 inhibits transactivation. Interacts with HEXIM1, PELP1 and TGFB1I1.
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic in the absence of ligand, nuclear after ligand-binding. Isoform Beta: Nucleus. Note: Localized largely in the nucleus.
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.17
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-binding domain. Ref.11
Post-translational modification	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. Ref.24 Ref.30 Ref.31 Sumoylated; this reduces transcription transactivation. Ref.23 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	Defects in NR3C1 are a cause of glucocorticoid resistance [MIM:138040]; also known as cortisol resistance. It is a hypertensive, hyperandrogenic disorder characterized by increased serum cortisol concentrations. Inheritance is autosomal dominant. Ref.35 Ref.38 Ref.44 Ref.46 Ref.49
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Disease mutation Pseudohermaphroditism
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
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW response to protein stimulus Inferred from direct assay. Source: MGI transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	mitochondrial matrix Traceable author statement. Source: ProtInc nucleus Inferred from direct assay. Source: HPA
Molecular function	glucocorticoid receptor activity Traceable author statement. Source: ProtInc protein binding Ref.14 Ref.28 Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid binding Inferred from electronic annotation. Source: UniProtKB-KW transcription factor activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Mvp	Q62667	1	EBI-493507,EBI-918333	From a different organism.
SMARCA4	P51532	1	EBI-493507,EBI-302489
SMARCC1	Q92922	1	EBI-493507,EBI-355653

Alternative products

This entry describes 9 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 altrnatively 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: Localized largely in the nucleus. No hormone-binding activity. Widely expressed at low level. Localized largely in the nucleus.

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 777

777

Glucocorticoid receptor

PRO_0000019937

Regions

DNA binding

421 – 486

66

Nuclear receptor

Zinc finger

421 – 441

21

NR C4-type

Zinc finger

457 – 481

25

NR C4-type

Region

1 – 420

420

Modulating

Region

487 – 527

41

Hinge

Region

528 – 777

250

Steroid-binding

Compositional bias

399 – 418

20

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

Amino acid modifications

Modified residue

8

1

Phosphothreonine Ref.30

Modified residue

45

1

Phosphoserine Ref.30

Modified residue

113

1

Phosphoserine By similarity

Modified residue

134

1

Phosphoserine Ref.31

Modified residue

141

1

Phosphoserine By similarity

Modified residue

203

1

Phosphoserine Ref.24

Modified residue

211

1

Phosphoserine Ref.24

Modified residue

226

1

Phosphoserine Ref.31

Modified residue

234

1

Phosphoserine Ref.31

Modified residue

267

1

Phosphoserine Ref.31

Cross-link

277

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

Cross-link

293

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

Cross-link

419

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

Natural variations

Alternative sequence

1 – 26

26

Missing in isoform Alpha-B and isoform Beta-B.

VSP_018773

Alternative sequence

451

1

G → GR in isoform Alpha-2 and isoform Beta-2.

VSP_007363

Alternative sequence

491 – 674

184

Missing in isoform GR-A alpha and isoform GR-A beta.

VSP_013340

Alternative sequence

728 – 777

50

VVENL…LFHQK → NVMWLKPESTSHTLI in isoform Beta, isoform Beta-B, isoform Beta-2 and isoform GR-A beta.

VSP_003703

Natural variant

23

1

R → K: dbSNP rs6190. Ref.6 Ref.40 Ref.41 Ref.43 Ref.47 Ref.50 Ref.51

VAR_014140

Natural variant

29

1

F → L

VAR_015628

Natural variant

65

1

F → V: dbSNP rs6192. Ref.6 Ref.41

VAR_014622

Natural variant

112

1

L → F

VAR_015629

Natural variant

233

1

D → N

VAR_015630

Natural variant

363

1

N → 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. dbSNP rs6195. Ref.40 Ref.41 Ref.43 Ref.37 Ref.45

VAR_004675

Natural variant

421

1

C → Y in a glucocorticoid resistant leukemia cell line. Ref.36

VAR_015631

Natural variant

477

1

R → H in glucocorticoid resistance. Ref.44

VAR_013472

Natural variant

559

1

I → N in glucocorticoid resistance; interferes with translocation to the nucleus and thereby strongly reduces transcription activation. Is equally impaired in nuclear export. Acts as dominant negative mutant. Ref.46

VAR_015632

Natural variant

571

1

V → A in pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor. Ref.48

VAR_025014

Natural variant

641

1

D → V in glucocorticoid resistance. Ref.35

VAR_004676

Natural variant

679

1

G → S in glucocorticoid resistance; has 50% binding affinity. Ref.44

VAR_013473

Natural variant

729

1

V → I in glucocorticoid resistance. Ref.38

VAR_004677

Natural variant

747

1

I → M in glucocorticoid resistance; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. Ref.49

VAR_015633

Natural variant

753

1

L → F in two glucocorticoid resistant leukemia cell lines lacking the normal allele. Ref.36 Ref.39

VAR_004678

Experimental info

Mutagenesis

1

1

M → T: Abolishes expression of A-type isoforms. Ref.22

Mutagenesis

27

1

M → T: Abolishes expression of B-type isoforms. Ref.22

Mutagenesis

191

1

F → D: Reduces transactivation by the ADA complex. Ref.13

Mutagenesis

193

1

I → D: Reduces transactivation by the ADA complex. Ref.13

Mutagenesis

194

1

L → A: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225. Ref.13

Mutagenesis

197

1

L → E: Reduces transactivation by the ADA complex. Ref.13

Mutagenesis

213

1

W → A: Strongly reduces transactivation by the ADA complex. Ref.13

Mutagenesis

224

1

L → V: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225. Ref.13

Mutagenesis

225

1

L → F: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224. Ref.13

Mutagenesis

235

1

F → L: Strongly reduces transactivation by the ADA complex; when associated with V-236. Ref.13

Mutagenesis

236

1

L → V: Strongly reduces transactivation by the ADA complex; when associated with L-235. Ref.13

Mutagenesis

277

1

K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293. Ref.23

Mutagenesis

293

1

K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277. Ref.23

Mutagenesis

585

1

R → A: Reduces activation mediated by ligand binding domain; when associated with A-590. Ref.33

Mutagenesis

590

1

D → A: Reduces activation mediated by ligand binding domain; when associated with A-585. Ref.33

Mutagenesis

602

1

F → S: Increases solubility. No effect on transactivation by dexamethasone. Ref.33

Mutagenesis

625

1

P → A: Decreases transactivation by dexamethasone by 95%. Ref.33

Mutagenesis

628

1

I → A: Decreases dimerization and transactivation by dexamethasone; when associated with S-602. Ref.33

Mutagenesis

703

1

K → R: Slightly reduces sumoylation. Ref.23

Sequence conflict

399

1

R → G in BAD97314. Ref.4

Sequence conflict

754

1

A → T in BAD97314. Ref.4

Secondary structure

1

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777

Helix Strand Turn

Details...

Turn

525 – 527

3

Helix

532 – 539

8

Helix

556 – 578

23

Helix

584 – 586

3

Helix

589 – 616

28

Beta strand

619 – 624

6

Beta strand

627 – 629

3

Helix

633 – 635

3

Helix

639 – 655

17

Helix

660 – 671

12

Beta strand

673 – 676

4

Helix

683 – 704

22

Helix

709 – 732

24

Beta strand

735 – 739

5

Helix

740 – 746

7

Helix

749 – 757

9

Beta strand

769 – 771

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha (Alpha-A) [UniParc]. Last modified November 1, 1986. Version 1. Checksum: C5C90C9A5DD16AAB	FASTA	777	85,659
	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
	Isoform Beta (Beta-A). Checksum: E2D1F6EA0EE14704	FASTA	742	81,509
	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 LLDSMHENVM WLKPESTSHT LI
	Isoform Alpha-2 (Gamma). Checksum: 23048D99B60B169C	FASTA	778	85,815
	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 GRQHNYLCAG RNDCIIDKIR RKNCPACRYR 490 500 510 520 530 540 KCLQAGMNLE ARKTKKKIKG IQQATTGVSQ ETSENPGNKT IVPATLPQLT PTLVSLLEVI 550 560 570 580 590 600 EPEVLYAGYD SSVPDSTWRI MTTLNMLGGR QVIAAVKWAK AIPGFRNLHL DDQMTLLQYS 610 620 630 640 650 660 WMFLMAFALG WRSYRQSSAN LLCFAPDLII NEQRMTLPCM YDQCKHMLYV SSELHRLQVS 670 680 690 700 710 720 YEEYLCMKTL LLLSSVPKDG LKSQELFDEI RMTYIKELGK AIVKREGNSS QNWQRFYQLT 730 740 750 760 770 KLLDSMHEVV ENLLNYCFQT FLDKTMSIEF PEMLAEIITN QIPKYSNGNI KKLLFHQK
	Isoform Beta-2. Checksum: 329BE98BCC1DC0E5	FASTA	743	81,666
	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 GRQHNYLCAG RNDCIIDKIR RKNCPACRYR 490 500 510 520 530 540 KCLQAGMNLE ARKTKKKIKG IQQATTGVSQ ETSENPGNKT IVPATLPQLT PTLVSLLEVI 550 560 570 580 590 600 EPEVLYAGYD SSVPDSTWRI MTTLNMLGGR QVIAAVKWAK AIPGFRNLHL DDQMTLLQYS 610 620 630 640 650 660 WMFLMAFALG WRSYRQSSAN LLCFAPDLII NEQRMTLPCM YDQCKHMLYV SSELHRLQVS 670 680 690 700 710 720 YEEYLCMKTL LLLSSVPKDG LKSQELFDEI RMTYIKELGK AIVKREGNSS QNWQRFYQLT 730 740 KLLDSMHENV MWLKPESTSH TLI
	Isoform GR-A alpha. Checksum: 8CB72DE6B0593EFD	FASTA	593	64,752
	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 VPKDGLKSQE LFDEIRMTYI KELGKAIVKR EGNSSQNWQR FYQLTKLLDS 550 560 570 580 590 MHEVVENLLN YCFQTFLDKT MSIEFPEMLA EIITNQIPKY SNGNIKKLLF HQK
	Isoform GR-A beta. Checksum: 7C1C30CD84689FBE	FASTA	558	60,602
	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 VPKDGLKSQE LFDEIRMTYI KELGKAIVKR EGNSSQNWQR FYQLTKLLDS 550 MHENVMWLKP ESTSHTLI
	Isoform GR-P (Sequence not available).	FASTA	–	–
	Isoform Alpha-B (Beta-B). Checksum: C6D7A2D88B4025C1	FASTA	751	82,845
	10 20 30 40 50 60 MDFYKTLRGG ATVKVSASSP SLAVASQSDS KQRRLLVDFP KGSVSNAQQP DLSKAVSLSM 70 80 90 100 110 120 GLYMGETETK VMGNDLGFPQ QGQISLSSGE TDLKLLEESI ANLNRSTSVP ENPKSSASTA 130 140 150 160 170 180 VSAAPTEKEF PKTHSDVSSE QQHLKGQTGT NGGNVKLYTT DQSTFDILQD LEFSSGSPGK 190 200 210 220 230 240 ETNESPWRSD LLIDENCLLS PLAGEDDSFL LEGNSNEDCK PLILPDTKPK IKDNGDLVLS 250 260 270 280 290 300 SPSNVTLPQV KTEKEDFIEL CTPGVIKQEK LGTVYCQASF PGANIIGNKM SAISVHGVST 310 320 330 340 350 360 SGGQMYHYDM NTASLSQQQD QKPIFNVIPP IPVGSENWNR CQGSGDDNLT SLGTLNFPGR 370 380 390 400 410 420 TVFSNGYSSP SMRPDVSSPP SSSSTATTGP PPKLCLVCSD EASGCHYGVL TCGSCKVFFK 430 440 450 460 470 480 RAVEGQHNYL CAGRNDCIID KIRRKNCPAC RYRKCLQAGM NLEARKTKKK IKGIQQATTG 490 500 510 520 530 540 VSQETSENPG NKTIVPATLP QLTPTLVSLL EVIEPEVLYA GYDSSVPDST WRIMTTLNML 550 560 570 580 590 600 GGRQVIAAVK WAKAIPGFRN LHLDDQMTLL QYSWMFLMAF ALGWRSYRQS SANLLCFAPD 610 620 630 640 650 660 LIINEQRMTL PCMYDQCKHM LYVSSELHRL QVSYEEYLCM KTLLLLSSVP KDGLKSQELF 670 680 690 700 710 720 DEIRMTYIKE LGKAIVKREG NSSQNWQRFY QLTKLLDSMH EVVENLLNYC FQTFLDKTMS 730 740 750 IEFPEMLAEI ITNQIPKYSN GNIKKLLFHQ K
	Isoform Beta-B. Checksum: BCF1D97EFD06AB74	FASTA	716	78,695
	10 20 30 40 50 60 MDFYKTLRGG ATVKVSASSP SLAVASQSDS KQRRLLVDFP KGSVSNAQQP DLSKAVSLSM 70 80 90 100 110 120 GLYMGETETK VMGNDLGFPQ QGQISLSSGE TDLKLLEESI ANLNRSTSVP ENPKSSASTA 130 140 150 160 170 180 VSAAPTEKEF PKTHSDVSSE QQHLKGQTGT NGGNVKLYTT DQSTFDILQD LEFSSGSPGK 190 200 210 220 230 240 ETNESPWRSD LLIDENCLLS PLAGEDDSFL LEGNSNEDCK PLILPDTKPK IKDNGDLVLS 250 260 270 280 290 300 SPSNVTLPQV KTEKEDFIEL CTPGVIKQEK LGTVYCQASF PGANIIGNKM SAISVHGVST 310 320 330 340 350 360 SGGQMYHYDM NTASLSQQQD QKPIFNVIPP IPVGSENWNR CQGSGDDNLT SLGTLNFPGR 370 380 390 400 410 420 TVFSNGYSSP SMRPDVSSPP SSSSTATTGP PPKLCLVCSD EASGCHYGVL TCGSCKVFFK 430 440 450 460 470 480 RAVEGQHNYL CAGRNDCIID KIRRKNCPAC RYRKCLQAGM NLEARKTKKK IKGIQQATTG 490 500 510 520 530 540 VSQETSENPG NKTIVPATLP QLTPTLVSLL EVIEPEVLYA GYDSSVPDST WRIMTTLNML 550 560 570 580 590 600 GGRQVIAAVK WAKAIPGFRN LHLDDQMTLL QYSWMFLMAF ALGWRSYRQS SANLLCFAPD 610 620 630 640 650 660 LIINEQRMTL PCMYDQCKHM LYVSSELHRL QVSYEEYLCM KTLLLLSSVP KDGLKSQELF 670 680 690 700 710 DEIRMTYIKE LGKAIVKREG NSSQNWQRFY QLTKLLDSMH ENVMWLKPES TSHTLI

References

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[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: 2867473] [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: 1707881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA AND BETA).
[3]	"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.
[4]	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.
[5]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). Tissue: Uterine endothelium.
[6]	NIEHS SNPs program Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-23 AND VAL-65.
[7]	"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. , 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: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). Tissue: Placenta.
[9]	"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: 2026589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
[10]	"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: 1958537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
[11]	"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: 3841189] [Abstract] Cited for: DOMAINS.
[12]	"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: 8358712] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS GP-P; GP-A ALPHA AND GP-A BETA).
[13]	"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: 9154805] [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.
[14]	"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex." Fryer C.J., Archer T.K. Nature 393:88-91(1998) [PubMed: 9590696] [Abstract] Cited for: INTERACTION WITH THE SMARCA4 COMPLEX; NCOA1; NCOA2 AND THE CREBBP/EP300 COMPLEX.
[15]	"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: 10477749] [Abstract] Cited for: INTERACTION WITH BAG1.
[16]	"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: 10566686] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS ALPHA-2 AND BETA-2).
[17]	"Steroidogenic enzyme gene expression in the human heart." Kayes-Wandover K.M., White P.C. J. Clin. Endocrinol. Metab. 85:2519-2525(2000) [PubMed: 10902803] [Abstract] Cited for: TISSUE SPECIFICITY.
[18]	"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: 10866662] [Abstract] Cited for: INTERACTION WITH NCOA6.
[19]	"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: 10639135] [Abstract] Cited for: EFFECT ON EXPANDED POLYGLUTAMINE PROTEIN.
[20]	"Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids." Wallace A.D., Cidlowski J.A. J. Biol. Chem. 276:42714-42721(2001) [PubMed: 11555652] [Abstract] Cited for: GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
[21]	"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: 11238589] [Abstract] Cited for: REDUCTION OF CELL DEATH IN RESPONSE TO CORTICOSTEROIDS.
[22]	"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: 11435610] [Abstract] Cited for: ALTERNATIVE INITIATION, MUTAGENESIS OF MET-1 AND MET-27.
[23]	"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: 12144530] [Abstract] Cited for: SUMOYLATION, MUTAGENESIS OF LYS-277; LYS-293 AND LYS-703.
[24]	"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: 12000743] [Abstract] Cited for: PHOSPHORYLATION AT SER-203 AND SER-211.
[25]	"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: 12415108] [Abstract] Cited for: INTERACTION WITH PELP1.
[26]	"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: 15265776] [Abstract] Cited for: REVIEW ON ALTERNATIVE SPLICING, ALTERNATIVE INITIATION, POST-TRANSLATIONAL MODIFICATIONS.
[27]	"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: 15211577] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[28]	"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: 15941832] [Abstract] Cited for: INTERACTION WITH HEXIM1.
[29]	"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: 16478993] [Abstract] Cited for: INTERACTION WITH UNC45A.
[30]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-45, MASS SPECTROMETRY.
[31]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-226; SER-234 AND SER-267, MASS SPECTROMETRY.
[32]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[33]	"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: 12151000] [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.
[34]	"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: 12686538] [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.
[35]	"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: 1704018] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GLUCOCORTICOID RESISTANCE VAL-641.
[36]	"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: 8358735] [Abstract] Cited for: VARIANTS TYR-421 AND PHE-753.
[37]	"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: 8445027] [Abstract] Cited for: VARIANT SER-363.
[38]	"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: 7683692] [Abstract] Cited for: VARIANT GLUCOCORTICOID RESISTANCE ILE-729.
[39]	"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: 8316249] [Abstract] Cited for: VARIANT PHE-753.
[40]	"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: 9150737] [Abstract] Cited for: VARIANTS LYS-23 AND SER-363.
[41]	"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: 10391209] [Abstract] Cited for: VARIANTS LYS-23; VAL-65 AND SER-363.
[42]	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)
[43]	"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: 10898924] [Abstract] Cited for: VARIANTS LYS-23; LEU-29; PHE-112; ASN-233 AND SER-363.
[44]	"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: 11589680] [Abstract] Cited for: VARIANTS GLUCOCORTICOID RESISTANCE HIS-477 AND SER-679.
[45]	"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: 11344238] [Abstract] Cited for: VARIANT SER-363.
[46]	"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: 11701741] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GLUCOCORTICOID RESISTANCE ASN-559.
[47]	"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: 12351458] [Abstract] Cited for: VARIANT LYS-23.
[48]	"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: 11932321] [Abstract] Cited for: VARIANT PSEUDOHERMAPHRODITISM ALA-571.
[49]	"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: 12050230] [Abstract] Cited for: VARIANT GLUCOCORTICOID RESISTANCE MET-747, ALTERED INTERACTION WITH THE COACTIVATOR NCOA2.
[50]	"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: 15276593] [Abstract] Cited for: VARIANT LYS-23.
[51]	"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: 15292341] [Abstract] Cited for: VARIANT LYS-23.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Wikipedia

Glucocorticoid receptor entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03225 mRNA. Translation: CAA26976.1.
X03348 mRNA. Translation: CAA27054.1.
U80946 , U78506, U78507, U78508, U78509, U78510, U78511, U78512 Genomic DNA. Translation: AAB64353.1.
U80947 , U78506, U78507, U78508, U78509, U78510, U78511, U78512 Genomic DNA. Translation: AAB64354.1.
U01351 mRNA. Translation: AAA16603.1.
AK223594 mRNA. Translation: BAD97314.1.
BX640610 mRNA. Translation: CAE45716.1.
AY436590 Genomic DNA. Translation: AAQ97180.1.
AC005601 Genomic DNA. Translation: AAC34207.1.
AC004782 Genomic DNA. No translation available.
AC091925 Genomic DNA. No translation available.
BC015610 mRNA. Translation: AAH15610.1.
M69104 Genomic DNA. Translation: AAA88049.1.
M73816 Genomic DNA. Translation: AAA53151.1.
S68378 Genomic DNA. Translation: AAB20466.1.

IPI

IPI00022282.
IPI00219946.
IPI00251749.
IPI00555880.
IPI00604604.
IPI00604725.
IPI00759700.
IPI00759729.

PIR

QRHUGA. A93370.
QRHUGB. B93370.

RefSeq

NP_000167.1.
NP_001018084.1.
NP_001018085.1.
NP_001018086.1.
NP_001018087.1.
NP_001018661.1.
NP_001019265.1.

UniGene

Hs.122926

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M2Z	X-ray	2.50	A/D	521-777	[»]
1NHZ	X-ray	2.30	A	500-777	[»]
1P93	X-ray	2.70	A/B/C/D	500-777	[»]
3BQD	X-ray	2.50	A	525-777	[»]
3CLD	X-ray	2.84	A/B	521-777	[»]
3E7C	X-ray	2.15	A/B	521-777	[»]

SMR

P04150. Positions 417-491.

DisProt

DP00030.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:576N.

IntAct

P04150. 3 interactions.

STRING

P04150.

PTM databases

PhosphoSite

P04150.

Proteomic databases

PRIDE

P04150.

Genome annotation databases

Ensembl

ENST00000231509; ENSP00000231509; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000343796; ENSP00000343205; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000361001; ENSP00000354274; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000394464; ENSP00000377977; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000394466; ENSP00000377979; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000415690; ENSP00000387672; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000416954; ENSP00000404218; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000424646; ENSP00000405282; ENSG00000113580; Homo sapiens. [Genome view]
ENST00000454007; ENSP00000415216; ENSG00000113580; Homo sapiens. [Genome view]

GeneID

2908.

KEGG

hsa:2908.

UCSC

uc003lmy.1. human.
uc003lmz.1. human.
uc003lna.1. human.

Organism-specific databases

CTD

2908.

GeneCards

GC05M142639.

H-InvDB

HIX0005273.

HGNC

HGNC:7978. NR3C1.

HPA

CAB010435.
HPA004248.

MIM

138040. gene+phenotype.

Orphanet

786. Glucocorticoid resistance.

PharmGKB

PA181.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P04150.

OMA

LPDTKPK.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P04150.

Bgee

P04150.

CleanEx

HS_NR3C1.

Genevestigator

P04150.

GermOnline

ENSG00000113580. Homo sapiens.

Family and domain databases

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]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

Pfam

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

PRINTS

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

ProDom

PD000035. Znf_C4steroid. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

PROSITE

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

ProtoNet

Search...

Other Resources

BindingDB

P04150.

DrugBank

DB00288. 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.

NextBio

11517.

SOURCE

Search...

Entry information

Entry name

GCR_HUMAN

Accession

Primary (citable) accession number: P04150
Secondary accession number(s): P04151, Q53EP5, Q6N0A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	November 3, 2009
This is version 155 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.