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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)DescriptionActionsGraphical viewLength
DNA bindingi440 – 505Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri440 – 460NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri476 – 500NR C4-typePROSITE-ProRule annotationAdd BLAST25

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 modification Source: UniProtKB-KW
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi1M → T: Abolishes expression of A-type isoforms. 1 Publication1
Mutagenesisi28M → T: Abolishes expression of B-type isoforms. 1 Publication1
Mutagenesisi297K → R: Enhances transcriptional activity; when associated with R-313. 1 Publication1
Mutagenesisi313K → R: Enhances transcriptional activity; when associated with R-297. 1 Publication1
Mutagenesisi481D → R: Disrupts dimerization and decreases transcription transactivation. 1 Publication1
Mutagenesisi488R → Q: Loss of chromatin specific function and reduces chromatin remodeling. Abolishes interaction with SMARD1. 1 Publication1
Mutagenesisi500C → Y: Abolishes interaction with POU2F2. 1 Publication1
Mutagenesisi501L → P: Abrogates DNA-binding and transcription transactivation. Abolishes interaction with POU2F1 and POU2F2. 2 Publications1
Mutagenesisi656C → S: Strongly increases affinity for dexamethasone. 1 Publication1
Mutagenesisi721K → R: Abolishes the stimulatory effect of RWDD3 on its transcriptional activity. Diminishes NCOA2 coactivator activity. 1 Publication1
Mutagenesisi773E → A: Abolishes interaction with NCOA1 and reduces transcription transactivation; when associated with S-656. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000199411 – 795Glucocorticoid receptorAdd BLAST795

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Omega-N-methylarginineBy similarity1
Modified residuei46PhosphoserineBy similarity1
Modified residuei134PhosphoserineBy similarity1
Modified residuei155PhosphoserineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei171Phosphothreonine1 Publication1
Modified residuei224PhosphoserineCombined sources1 Publication1
Modified residuei232PhosphoserineCombined sources1 Publication1
Modified residuei246Phosphoserine1 Publication1
Modified residuei287PhosphoserineCombined sources1
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei327PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei499N6-acetyllysineBy similarity1
Modified residuei511N6-acetyllysineBy similarity1
Modified residuei513N6-acetyllysineBy similarity1
Modified residuei514N6-acetyllysineBy similarity1
Cross-linki721Glycyl 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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP06536.
PeptideAtlasiP06536.
PRIDEiP06536.

PTM databases

iPTMnetiP06536.
PhosphoSitePlusiP06536.

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). Interacts with FNIP1 and FNIP2 (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 interactors.
DIPiDIP-38940N.
IntActiP06536. 30 interactors.
MINTiMINT-194828.
STRINGi10116.ENSRNOP00000044335.

Chemistry databases

BindingDBiP06536.

Structurei

Secondary structure

1795
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni441 – 443Combined sources3
Beta strandi444 – 446Combined sources3
Beta strandi449 – 451Combined sources3
Beta strandi454 – 456Combined sources3
Helixi458 – 469Combined sources12
Beta strandi477 – 480Combined sources4
Helixi488 – 490Combined sources3
Helixi493 – 503Combined sources11
Helixi509 – 513Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06536.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 439ModulatingAdd BLAST439
Regioni504 – 795Interaction with CLOCKBy similarityAdd BLAST292
Regioni506 – 546HingeAdd BLAST41
Regioni547 – 795Steroid-bindingAdd BLAST249
Regioni550 – 715Interaction with CRY1By similarityAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi75 – 97Poly-GlnAdd BLAST23
Compositional biasi419 – 438Glu/Pro/Ser/Thr-rich (PEST region)Add BLAST20

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)DescriptionActionsGraphical viewLength
Zinc fingeri440 – 460NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri476 – 500NR C4-typePROSITE-ProRule annotationAdd BLAST25

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)DescriptionActionsGraphical viewLength
Sequence conflicti95 – 96Missing in AAL78956 (Ref. 3) Curated2
Sequence conflicti98D → G in AAA41203 (PubMed:3755378).Curated1
Sequence conflicti345S → T in CAA68545 (PubMed:3684608).Curated1
Sequence conflicti600L → P in CAA72938 (Ref. 2) Curated1
Sequence conflicti600L → P in AAL66772 (Ref. 3) Curated1
Sequence conflicti600L → P in AAL78956 (Ref. 3) Curated1
Sequence conflicti602L → F in AAL66772 (Ref. 3) Curated1
Sequence conflicti602L → F in AAL78956 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti77Missing in strain: Brown Norway/Crl. 1
Natural varianti78 – 79Missing in strain: SHR/OlaIpcv. 2
Natural varianti83 – 96Missing in strain: Sprague-Dawley. Add BLAST14
Natural varianti226S → G in strain: SHR/OlaIpcv and Brown Norway/Crl. Combined sources1 Publication1
Natural varianti260N → D in strain: SHR/OlaIpcv and Brown Norway/Crl. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189691 – 27Missing in isoform B. CuratedAdd BLAST27

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP06536.
ChEMBLiCHEMBL3368.

PTM databases

iPTMnetiP06536.
PhosphoSitePlusiP06536.

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: November 30, 2016
This is version 197 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.