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P06536

- GCR_RAT

UniProt

P06536 - GCR_RAT

Protein

Glucocorticoid receptor

Gene

Nr3c1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    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 binding Source: UniProtKB
    9. protein complex binding Source: UniProtKB
    10. protein dimerization activity Source: RGD
    11. protein heterodimerization activity Source: RGD
    12. protein homodimerization activity Source: RGD
    13. receptor tyrosine kinase binding Source: RGD
    14. RNA polymerase II regulatory region DNA binding Source: RGD
    15. sequence-specific DNA binding Source: RGD
    16. sequence-specific DNA binding transcription factor activity Source: RGD
    17. steroid binding Source: RGD
    18. transcription coactivator activity Source: RGD
    19. transcription factor binding Source: RGD
    20. 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

    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-SubCell
    4. neuron projection Source: RGD
    5. nucleus Source: RGD
    6. postsynaptic density Source: RGD
    7. protein complex Source: RGD

    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 – 4433
    Beta strandi444 – 4463
    Beta strandi449 – 4513
    Beta strandi454 – 4563
    Helixi458 – 46912
    Beta strandi477 – 4804
    Helixi488 – 4903
    Helixi493 – 50311
    Helixi509 – 5135

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA    50
    AASQADSKQQ RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS 100
    KAVSLSMGLY MGETETKVMG NDLGYPQQGQ LGLSSGETDF RLLEESIANL 150
    NRSTSVPENP KSSTSATGCA TPTEKEFPKT HSDASSEQQN RKSQTGTNGG 200
    SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI DENLLSPLAG 250
    EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK 300
    DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ 350
    MYHYDMNTAS LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA 400
    LNFPGRSVFS NGYSSPGMRP DVSSPPSSSS AATGPPPKLC LVCSDEASGC 450
    HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN DCIIDKIRRK NCPACRYRKC 500
    LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP AALPQLTPTL 550
    VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL 600
    GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ 650
    RMSLPCMYDQ CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS 700
    QELFDEIRMT YIKELGKAIV KREGNSSQNW QRFYQLTKLL DSMHEVVENL 750
    LTYCFQTFLD KTMSIEFPEM LAEIITNQIP KYSNGNIKKL LFHQK 795
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 179 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