Details for: Nr3c1
Associated with
Other Information
Genular Protein ID: 3621395754
Symbol: GCR_RAT
Name: Glucocorticoid receptor
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 3755378
Title: Genetic complementation of a glucocorticoid receptor deficiency by expression of cloned receptor cDNA.
PubMed ID: 3755378
PubMed ID: 3684608
Title: Cloning and sequence analysis of the rat ventral prostate glucocorticoid receptor cDNA.
PubMed ID: 3684608
PubMed ID: 3191912
Title: Metal binding 'finger' structures in the glucocorticoid receptor defined by site-directed mutagenesis.
PubMed ID: 3191912
PubMed ID: 3216865
Title: Regulation of glucocorticoid receptor expression: evidence for transcriptional and posttranslational mechanisms.
PubMed ID: 3216865
PubMed ID: 1939229
Title: Creation of 'super' glucocorticoid receptors by point mutations in the steroid binding domain.
PubMed ID: 1939229
PubMed ID: 8450530
Title: Zinc finger mutations that alter domain interactions in the glucocorticoid receptor.
PubMed ID: 8450530
PubMed ID: 8191545
Title: Active, interactive, and inactive steroid receptor mutants.
PubMed ID: 8191545
PubMed ID: 8618925
Title: Steroid receptor heterodimerization demonstrated in vitro and in vivo.
PubMed ID: 8618925
PubMed ID: 9111344
Title: GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors.
PubMed ID: 9111344
PubMed ID: 9603939
Title: 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.
PubMed ID: 9603939
PubMed ID: 10364267
Title: Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids.
PubMed ID: 10364267
PubMed ID: 10480874
Title: Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter.
PubMed ID: 10480874
PubMed ID: 10866662
Title: A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP.
PubMed ID: 10866662
PubMed ID: 11278286
Title: Heterodimerization of mineralocorticoid and glucocorticoid receptors at a novel negative response element of the 5-HT1A receptor gene.
PubMed ID: 11278286
PubMed ID: 11435610
Title: Molecular identification and characterization of A and B forms of the glucocorticoid receptor.
PubMed ID: 11435610
PubMed ID: 12118039
Title: A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1.
PubMed ID: 12118039
PubMed ID: 12917342
Title: BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.
PubMed ID: 12917342
PubMed ID: 16641100
Title: Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.
PubMed ID: 16641100
PubMed ID: 21730050
Title: The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.
PubMed ID: 21730050
PubMed ID: 22673903
Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
PubMed ID: 22673903
DOI: 10.1038/ncomms1871
PubMed ID: 23508108
Title: RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity.
PubMed ID: 23508108
DOI: 10.1128/mcb.01470-12
PubMed ID: 15220929
PubMed ID: 1865905
Title: Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA.
PubMed ID: 1865905
DOI: 10.1038/352497a0
PubMed ID: 2115209
Title: Solution structure of the glucocorticoid receptor DNA-binding domain.
PubMed ID: 2115209
PubMed ID: 1751485
Title: 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
PubMed ID: 1751485
DOI: 10.1021/bi00114a003
PubMed ID: 1936288
Title: Identification of the metal coordinating residues in the DNA binding domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR spectroscopy.
PubMed ID: 1936288
PubMed ID: 8257681
Title: Refined solution structure of the glucocorticoid receptor DNA-binding domain.
PubMed ID: 8257681
DOI: 10.1021/bi00212a011
PubMed ID: 8493115
Title: Heterogeneity in the polyglutamine tract of the glucocorticoid receptor from different rat strains.
PubMed ID: 8493115
Sequence Information:
- Length: 795
- Mass: 87556
- Checksum: 9C9DE0B1D6724845
- Sequence:
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQQPDLS KAVSLSMGLY MGETETKVMG NDLGYPQQGQ LGLSSGETDF RLLEESIANL NRSTSVPENP KSSTSATGCA TPTEKEFPKT HSDASSEQQN RKSQTGTNGG SVKLYPTDQS TFDLLKDLEF SAGSPSKDTN ESPWRSDLLI DENLLSPLAG EDDPFLLEGN TNEDCKPLIL PDTKPKIKDT GDTILSSPSS VALPQVKTEK DDFIELCTPG VIKQEKLGPV YCQASFSGTN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPV FNVIPPIPVG SENWNRCQGS GEDSLTSLGA LNFPGRSVFS NGYSSPGMRP DVSSPPSSSS AATGPPPKLC LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN DCIIDKIRRK NCPACRYRKC LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP AALPQLTPTL VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIL GLRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ RMSLPCMYDQ CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS QELFDEIRMT YIKELGKAIV KREGNSSQNW QRFYQLTKLL DSMHEVVENL LTYCFQTFLD KTMSIEFPEM LAEIITNQIP KYSNGNIKKL LFHQK
Genular Protein ID: 743144588
Symbol: A6J3I0_RAT
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15632090
Title: Gene and alternative splicing annotation with AIR.
PubMed ID: 15632090
DOI: 10.1101/gr.2889405
Sequence Information:
- Length: 794
- Mass: 87417
- Checksum: 7E5262DEEDA65AB0
- Sequence:
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQPDLSK AVSLSMGLYM GETETKVMGN DLGYPQQGQL GLSSGETDFR LLEESIANLN RSTSVPENPK SSTSATGCAT PTEKEFPKTH SDASSEQQNR KSQTGTNGGS VKLYPTDQST FDLLKDLEFS AGSPGKDTNE SPWRSDLLID ENLLSPLAGE DDPFLLEGDT NEDCKPLILP DTKPKIKDTG DTILSSPSSV ALPQVKTEKD DFIELCTPGV IKQEKLGPVY CQASFSGTNI IGNKMSAISV HGVSTSGGQM YHYDMNTASL SQQQDQKPVF NVIPPIPVGS ENWNRCQGSG EDSLTSLGAL NFPGRSVFSN GYSSPGMRPD VSSPPSSSSA ATGPPPKLCL VCSDEASGCH YGVLTCGSCK VFFKRAVEGQ HNYLCAGRND CIIDKIRRKN CPACRYRKCL QAGMNLEARK TKKKIKGIQQ ATAGVSQDTS ENPNKTIVPA ALPQLTPTLV SLLEVIEPEV LYAGYDSSVP DSAWRIMTTL NMLGGRQVIA AVKWAKAIPG FRNLHLDDQM TLLQYSWMFL MAFALGWRSY RQSSGNLLCF APDLIINEQR MSLPCMYDQC KHMLFVSSEL QRLQVSYEEY LCMKTLLLLS SVPKEGLKSQ ELFDEIRMTY IKELGKAIVK REGNSSQNWQ RFYQLTKLLD SMHEVVENLL TYCFQTFLDK TMSIEFPEML AEIITNQIPK YSNGNIKKLL FHQK
Genular Protein ID: 4215660563
Symbol: E9PT44_RAT
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15057822
Title: Genome sequence of the Brown Norway rat yields insights into mammalian evolution.
PubMed ID: 15057822
DOI: 10.1038/nature02426
Sequence Information:
- Length: 795
- Mass: 87573
- Checksum: AC958EFA9796A30E
- Sequence:
MDSKESLAPP GRDEVPGSLL GQGRGSVMDF YKSLRGGATV KVSASSPSVA AASQADSKQQ RILLDFSKGS TSNVQQRQQQ QQQQQQQQQQ QQQQQPDLSK AVSLSMGLYM GETETKVMGN DLGYPQQGQL GLSSGETDFR LLEESIANLN RSTSVPENPK SSTSATGCAT PTEKEFPKTH SDASSEQQNR KSQTGTNGGS VKLYPTDQST FDLLKDLEFS AGSPGKDTNE SPWRSDLLID ENLLSPLAGE DDPFLLEGDT NEDCKPLILP DTKPKIKDTG DTILSSPSSV ALPQVKTEKD DFIELCTPGV IKQEKLGPVY CQASFSGTNI IGNKMSAISV HGVSTSGGQM YHYDMNTASL SQQQDQKPVF NVIPPIPVGS ENWNRCQGSG EDSLTSLGAL NFPGRSVFSN GYSSPGMRPD VSSPPSSSSA ATGPPPKLCL VCSDEASGCH YGVLTCGSCK VFFKRAVEGR QHNYLCAGRN DCIIDKIRRK NCPACRYRKC LQAGMNLEAR KTKKKIKGIQ QATAGVSQDT SENPNKTIVP AALPQLTPTL VSLLEVIEPE VLYAGYDSSV PDSAWRIMTT LNMLGGRQVI AAVKWAKAIP GFRNLHLDDQ MTLLQYSWMF LMAFALGWRS YRQSSGNLLC FAPDLIINEQ RMSLPCMYDQ CKHMLFVSSE LQRLQVSYEE YLCMKTLLLL SSVPKEGLKS QELFDEIRMT YIKELGKAIV KREGNSSQNW QRFYQLTKLL DSMHEVVENL LTYCFQTFLD KTMSIEFPEM LAEIITNQIP KYSNGNIKKL LFHQK
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.