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P06536

- GCR_RAT

UniProt

P06536 - GCR_RAT

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Protein

Glucocorticoid receptor

Gene

Nr3c1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. 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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi440 – 50566Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri440 – 46021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri476 – 50025NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: RGD
  2. double-stranded DNA binding Source: RGD
  3. glucocorticoid receptor activity Source: InterPro
  4. heat shock protein binding Source: RGD
  5. hormone binding Source: RGD
  6. Hsp70 protein binding Source: RGD
  7. Hsp90 protein binding Source: RGD
  8. protein complex binding Source: UniProtKB
  9. protein dimerization activity Source: RGD
  10. protein heterodimerization activity Source: RGD
  11. protein homodimerization activity Source: RGD
  12. receptor tyrosine kinase binding Source: RGD
  13. RNA polymerase II regulatory region DNA binding Source: RGD
  14. sequence-specific DNA binding Source: RGD
  15. sequence-specific DNA binding transcription factor activity Source: RGD
  16. steroid binding Source: RGD
  17. transcription coactivator activity Source: RGD
  18. transcription factor binding Source: RGD
  19. zinc ion binding Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. androgen metabolic process Source: RGD
  3. brain development Source: RGD
  4. cellular response to dexamethasone stimulus Source: RGD
  5. cellular response to magnesium ion Source: RGD
  6. chromatin-mediated maintenance of transcription Source: UniProtKB
  7. chromatin remodeling Source: UniProtKB
  8. circadian rhythm Source: RGD
  9. lung development Source: RGD
  10. muscle atrophy Source: RGD
  11. negative regulation of synaptic plasticity Source: RGD
  12. negative regulation of vascular permeability Source: RGD
  13. positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
  14. positive regulation of dendritic spine development Source: RGD
  15. positive regulation of glucocorticoid receptor signaling pathway Source: RGD
  16. positive regulation of glutamate secretion Source: RGD
  17. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  18. regulation of cell proliferation Source: RGD
  19. regulation of glucose metabolic process Source: RGD
  20. response to activity Source: RGD
  21. response to arsenic-containing substance Source: RGD
  22. response to calcium ion Source: RGD
  23. response to corticosterone Source: RGD
  24. response to dexamethasone Source: RGD
  25. response to electrical stimulus Source: RGD
  26. response to inactivity Source: RGD
  27. response to insulin Source: RGD
  28. response to mercury ion Source: RGD
  29. response to radiation Source: RGD
  30. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Glucocorticoid receptor
Short name:
GR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 1
Gene namesi
Name:Nr3c1
Synonyms:Grl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2741. Nr3c1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. dendritic spine Source: RGD
  3. mitochondrion Source: UniProtKB-KW
  4. neuron projection Source: RGD
  5. nucleus Source: RGD
  6. postsynaptic density Source: RGD
  7. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → T: Abolishes expression of A-type isoforms. 1 Publication
Mutagenesisi28 – 281M → T: Abolishes expression of B-type isoforms. 1 Publication
Mutagenesisi297 – 2971K → R: Enhances transcriptional activity; when associated with R-313. 1 Publication
Mutagenesisi313 – 3131K → R: Enhances transcriptional activity; when associated with R-297. 1 Publication
Mutagenesisi481 – 4811D → R: Disrupts dimerization and decreases transcription transactivation. 1 Publication
Mutagenesisi488 – 4881R → Q: Loss of chromatin specific function and reduces chromatin remodeling. Abolishes interaction with SMARD1. 1 Publication
Mutagenesisi500 – 5001C → Y: Abolishes interaction with POU2F2. 1 Publication
Mutagenesisi501 – 5011L → P: Abrogates DNA-binding and transcription transactivation. Abolishes interaction with POU2F1 and POU2F2. 2 Publications
Mutagenesisi656 – 6561C → S: Strongly increases affinity for dexamethasone. 1 Publication
Mutagenesisi721 – 7211K → R: Abolishes the stimulatory effect of RWDD3 on its transcriptional activity. Diminishes NCOA2 coactivator activity. 1 Publication
Mutagenesisi773 – 7731E → A: Abolishes interaction with NCOA1 and reduces transcription transactivation; when associated with S-656. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Glucocorticoid receptorPRO_0000019941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei171 – 1711Phosphothreonine1 Publication
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei232 – 2321Phosphoserine1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei287 – 2871PhosphoserineBy similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki313 – 313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei327 – 3271PhosphoserineBy similarity
Cross-linki438 – 438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Curated
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei511 – 5111N6-acetyllysineBy similarity
Modified residuei513 – 5131N6-acetyllysineBy similarity
Modified residuei514 – 5141N6-acetyllysineBy similarity
Cross-linki721 – 721Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity.By similarity
Increased proteasome-mediated degradation in response to glucocorticoids.
Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. May be dephosphorylated by PPP5C, attenuates NR3C1 action (By similarity).By similarity
Sumoylations at Lys-297 and Lys-313 negatively regulate its transcriptional activity. Sumoylation at Lys-721 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylations at Lys-297 and Lys-313 are dispensable whereas sumoylation at Lys-721 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWWD3-dependent manner.1 Publication
Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP06536.
PRIDEiP06536.

PTM databases

PhosphoSiteiP06536.

Expressioni

Gene expression databases

GenevestigatoriP06536.

Interactioni

Subunit structurei

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. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi246578. 15 interactions.
DIPiDIP-38940N.
IntActiP06536. 29 interactions.
MINTiMINT-194828.

Structurei

Secondary structure

1
795
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni441 – 4433Combined sources
Beta strandi444 – 4463Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi454 – 4563Combined sources
Helixi458 – 46912Combined sources
Beta strandi477 – 4804Combined sources
Helixi488 – 4903Combined sources
Helixi493 – 50311Combined sources
Helixi509 – 5135Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP06536.
SMRiP06536. Positions 439-510, 541-795.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06536.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 439439ModulatingAdd
BLAST
Regioni504 – 795292Interaction with CLOCKBy similarityAdd
BLAST
Regioni506 – 54641HingeAdd
BLAST
Regioni547 – 795249Steroid-bindingAdd
BLAST
Regioni550 – 715166Interaction with CRY1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 9723Poly-GlnAdd
BLAST
Compositional biasi419 – 43820Glu/Pro/Ser/Thr-rich (PEST region)Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri440 – 46021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri476 – 50025NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG270250.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiP06536.
KOiK05771.
PhylomeDBiP06536.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. 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]
PfamiPF02155. GCR. 2 hits.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform A (identifier: P06536-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA
60 70 80 90 100
AASQADSKQQ RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS
110 120 130 140 150
KAVSLSMGLY MGETETKVMG NDLGYPQQGQ LGLSSGETDF RLLEESIANL
160 170 180 190 200
NRSTSVPENP KSSTSATGCA TPTEKEFPKT HSDASSEQQN RKSQTGTNGG
210 220 230 240 250
SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI DENLLSPLAG
260 270 280 290 300
EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK
310 320 330 340 350
DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ
360 370 380 390 400
MYHYDMNTAS LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA
410 420 430 440 450
LNFPGRSVFS NGYSSPGMRP DVSSPPSSSS AATGPPPKLC LVCSDEASGC
460 470 480 490 500
HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN DCIIDKIRRK NCPACRYRKC
510 520 530 540 550
LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP AALPQLTPTL
560 570 580 590 600
VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL
610 620 630 640 650
GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ
660 670 680 690 700
RMSLPCMYDQ CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS
710 720 730 740 750
QELFDEIRMT YIKELGKAIV KREGNSSQNW QRFYQLTKLL DSMHEVVENL
760 770 780 790
LTYCFQTFLD KTMSIEFPEM LAEIITNQIP KYSNGNIKKL LFHQK
Length:795
Mass (Da):87,556
Last modified:November 1, 1995 - v2
Checksum:i9C9DE0B1D6724845
GO
Isoform B (identifier: P06536-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:768
Mass (Da):84,834
Checksum:iD6E586FE0E91597F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 962Missing in AAL78956. 1 PublicationCurated
Sequence conflicti98 – 981D → G in AAA41203. (PubMed:3755378)Curated
Sequence conflicti345 – 3451S → T in CAA68545. (PubMed:3684608)Curated
Sequence conflicti600 – 6001L → P in CAA72938. 1 PublicationCurated
Sequence conflicti600 – 6001L → P in AAL66772. 1 PublicationCurated
Sequence conflicti600 – 6001L → P in AAL78956. 1 PublicationCurated
Sequence conflicti602 – 6021L → F in AAL66772. 1 PublicationCurated
Sequence conflicti602 – 6021L → F in AAL78956. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771Missing in strain: Brown Norway/Crl.
Natural varianti78 – 792Missing in strain: SHR/OlaIpcv.
Natural varianti83 – 9614Missing in strain: Sprague-Dawley.
Add
BLAST
Natural varianti226 – 2261S → G in strain: SHR/OlaIpcv and Brown Norway/Crl. 1 Publication
Natural varianti260 – 2601N → D in strain: SHR/OlaIpcv and Brown Norway/Crl. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727Missing in isoform B. CuratedVSP_018969Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA24194. QRRTG.
RefSeqiNP_036708.2. NM_012576.2.
UniGeneiRn.90070.

Genome annotation databases

GeneIDi24413.
KEGGirno:24413.
UCSCiRGD:2741. rat. [P06536-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi A24194. QRRTG.
RefSeqi NP_036708.2. NM_012576.2.
UniGenei Rn.90070.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P06536.
SMRi P06536. Positions 439-510, 541-795.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246578. 15 interactions.
DIPi DIP-38940N.
IntActi P06536. 29 interactions.
MINTi MINT-194828.

Chemistry

BindingDBi P06536.
ChEMBLi CHEMBL3368.
GuidetoPHARMACOLOGYi 625.

PTM databases

PhosphoSitei P06536.

Proteomic databases

PaxDbi P06536.
PRIDEi P06536.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24413.
KEGGi rno:24413.
UCSCi RGD:2741. rat. [P06536-1 ]

Organism-specific databases

CTDi 2908.
RGDi 2741. Nr3c1.

Phylogenomic databases

eggNOGi NOG270250.
HOGENOMi HOG000037950.
HOVERGENi HBG007583.
InParanoidi P06536.
KOi K05771.
PhylomeDBi P06536.

Miscellaneous databases

EvolutionaryTracei P06536.
NextBioi 603243.
PROi P06536.

Gene expression databases

Genevestigatori P06536.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi 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 ]
Pfami PF02155. GCR. 2 hits.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: SUMOYLATION AT LYS-297; LYS-313 AND LYS-721, INTERACTION WITH UBE2I/UBC9 AND RWDD3, MUTAGENESIS OF LYS-297; LYS-313 AND LYS-721.
  22. "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.
  23. Cited for: STRUCTURE BY NMR OF 440-510.
  24. "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.
  25. "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.
  26. "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.
  27. "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.

Entry informationi

Entry nameiGCR_RAT
AccessioniPrimary (citable) accession number: P06536
Secondary accession number(s): O08624, Q8R463, Q8R5J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3