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Protein

Glucocorticoid receptor

Gene

Nr3c1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. Involved in chromatin remodeling (PubMed:12917342). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). 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 (By similarity).By similarity1 Publication
Isoform A: Has transcriptional activation and repression activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression.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

  • chromatin binding Source: RGD
  • double-stranded DNA binding Source: RGD
  • glucocorticoid-activated RNA polymerase II transcription factor binding transcription factor activity Source: UniProtKB
  • heat shock protein binding Source: RGD
  • hormone binding Source: RGD
  • Hsp70 protein binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • protein complex binding Source: UniProtKB
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor tyrosine kinase binding Source: RGD
  • RNA polymerase II regulatory region DNA binding Source: RGD
  • sequence-specific DNA binding Source: RGD
  • steroid binding Source: RGD
  • steroid hormone binding Source: UniProtKB
  • transcription coactivator activity Source: RGD
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • androgen metabolic process Source: RGD
  • brain development Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to magnesium ion Source: RGD
  • cellular response to steroid hormone stimulus Source: UniProtKB
  • chromatin-mediated maintenance of transcription Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • circadian rhythm Source: RGD
  • lung development Source: RGD
  • muscle atrophy Source: RGD
  • negative regulation of synaptic plasticity Source: RGD
  • negative regulation of vascular permeability Source: RGD
  • positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
  • positive regulation of dendritic spine development Source: RGD
  • positive regulation of glucocorticoid receptor signaling pathway Source: RGD
  • positive regulation of glutamate secretion Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • regulation of cell proliferation Source: RGD
  • regulation of glucose metabolic process Source: RGD
  • response to activity Source: RGD
  • response to arsenic-containing substance Source: RGD
  • response to calcium ion Source: RGD
  • response to corticosterone Source: RGD
  • response to dexamethasone Source: RGD
  • response to electrical stimulus Source: RGD
  • response to inactivity Source: RGD
  • response to insulin Source: RGD
  • response to mercury ion Source: RGD
  • response to radiation Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2741. Nr3c1.

Subcellular locationi

Isoform A :
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Mitochondrion 1 Publication
  • Cytoplasmcytoskeletonspindle By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

  • Note: After ligand activation, translocates from the cytoplasm to the nucleus.By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendritic spine Source: RGD
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB-SubCell
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • postsynaptic density Source: RGD
  • protein complex Source: RGD
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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

Chemistry

ChEMBLiCHEMBL3368.

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 residuei46 – 461PhosphoserineBy similarity
Modified residuei134 – 1341PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei171 – 1711Phosphothreonine1 Publication
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine; in variant Gly-226Combined sources
Modified residuei232 – 2321PhosphoserineCombined sources1 Publication
Modified residuei232 – 2321Phosphoserine; in variant Gly-226Combined sources
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei287 – 2871PhosphoserineCombined sources
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki313 – 313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki313 – 313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei327 – 3271PhosphoserineBy similarity
Modified residuei424 – 4241PhosphoserineBy similarity
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)1 Publication

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.By similarity
Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. The Ser-224, Ser-246 and Ser-424-phosphorylated forms are mainly cytoplasmic, and the Ser-232-phosphorylated form is nuclear. Phosphorylation at Ser-232 increases transcriptional activity. Phosphorylation at Ser-224, Ser-246 and Ser-424 decreases signaling capacity. Phosphorylation at Ser-424 may protect from glucocorticoid-induced apoptosis. Phosphorylation at Ser-224 and Ser-232 is not required in regulation of chromosome segregation. May be dephosphorylated by PPP5C, attenuates NR3C1 action.By similarity
Sumoylation at Lys-297 and Lys-313 negatively regulates its transcriptional activity. Sumoylation at Lys-721 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-297 and Lys-313 is dispensable whereas sumoylation at Lys-721 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner.1 Publication
Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP06536.
PeptideAtlasiP06536.
PRIDEiP06536.

PTM databases

iPTMnetiP06536.
PhosphoSiteiP06536.

Interactioni

Subunit structurei

Interacts with GRIP1 (By similarity). Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C (PubMed:21730050). 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). Directly interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor (By similarity). Binds STAT5A and STAT5B homodimers and heterodimers (By similarity). Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:10364267, PubMed:10480874). Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6 (PubMed:9111344, PubMed:10866662). Interaction with BAG1 inhibits transactivation (By similarity). Interacts with HEXIM1, PELP1 and TGFB1I1 (By similarity). Interacts with NCOA1 (PubMed:12917342). Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (PubMed:12917342, PubMed:12118039). Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (By similarity). Interacts with CIART (By similarity). Interacts with RWDD3 (PubMed:23508108). Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (PubMed:23508108). Interacts with NR4A3 (via nuclear receptor DNA-binding domain), represses transcription activity of NR4A3 on the POMC promoter Nur response element (NurRE) (By similarity). Directly interacts with PNRC2 to attract and form a complex with UPF1 and DCP1A; the interaction leads to rapid mRNA degradation (By similarity). Interacts with GSK3B (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MvpQ626672EBI-1187143,EBI-918333
NCOA1Q157882EBI-1187143,EBI-455189From a different organism.
PAGR1Q9BTK62EBI-1187143,EBI-2372223From a different organism.
SMARCA4P515323EBI-1187143,EBI-302489From a different organism.
SMARCD1Q96GM52EBI-1187143,EBI-358489From a different organism.

GO - Molecular functioni

  • heat shock protein binding Source: RGD
  • Hsp70 protein binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • protein complex binding Source: UniProtKB
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor tyrosine kinase binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi246578. 15 interactions.
DIPiDIP-38940N.
IntActiP06536. 30 interactions.
MINTiMINT-194828.
STRINGi10116.ENSRNOP00000044335.

Chemistry

BindingDBiP06536.

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. The ligand-binding domain is required for correct chromosome segregation during mitosis although ligand binding is not required.By similarity

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

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiP06536.
KOiK05771.
PhylomeDBiP06536.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. Glcrtcd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_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. AlignAdd to basket

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 (Ref. 3) Curated
Sequence conflicti98 – 981D → G in AAA41203 (PubMed:3755378).Curated
Sequence conflicti345 – 3451S → T in CAA68545 (PubMed:3684608).Curated
Sequence conflicti600 – 6001L → P in CAA72938 (Ref. 2) Curated
Sequence conflicti600 – 6001L → P in AAL66772 (Ref. 3) Curated
Sequence conflicti600 – 6001L → P in AAL78956 (Ref. 3) Curated
Sequence conflicti602 – 6021L → F in AAL66772 (Ref. 3) Curated
Sequence conflicti602 – 6021L → F in AAL78956 (Ref. 3) Curated

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. Combined sources1 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.
PIRiA24194. QRRTG.
RefSeqiNP_036708.2. NM_012576.2.
UniGeneiRn.90070.

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...

Protein-protein interaction databases

BioGridi246578. 15 interactions.
DIPiDIP-38940N.
IntActiP06536. 30 interactions.
MINTiMINT-194828.
STRINGi10116.ENSRNOP00000044335.

Chemistry

BindingDBiP06536.
ChEMBLiCHEMBL3368.

PTM databases

iPTMnetiP06536.
PhosphoSiteiP06536.

Proteomic databases

PaxDbiP06536.
PeptideAtlasiP06536.
PRIDEiP06536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2908.
RGDi2741. Nr3c1.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiP06536.
KOiK05771.
PhylomeDBiP06536.

Miscellaneous databases

EvolutionaryTraceiP06536.
PROiP06536.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. Glcrtcd_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_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]
ProtoNetiSearch...

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: July 6, 2016
This is version 194 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.