Nr3c1

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:10678832). 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 (PubMed:15037546).By similarity2 Publications

Isoform 1: Has transcriptional activation and repression activity (By similarity). Mediates glucocorticoid-induced apoptosis (By similarity). Promotes accurate chromosome segregation during mitosis (PubMed:25847991). May act as a tumor suppressor (PubMed:25847991). May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (PubMed:21994940).By similarity2 Publications

Isoform 3: Acts as a dominant negative inhibitor of isoform 1 (PubMed:20660300). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (By similarity). Loses this transcription modulator function on its own (By similarity). Has no hormone-binding activity (PubMed:20660300). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (PubMed:20660300). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (By similarity). Directly regulates STAT1 expression in isoform Alpha-independent manner (By similarity).By similarity1 Publication

Miscellaneous

T-cell is a critical cellular target of GR, as immune activation in mice lacking GR resulted in significant mortality. This lethal activation is rescued by PTGS2 inhibition but not steroid administration or cytokine neutralization.

Regions

Feature key	Position(s)	DescriptionActions	Length
DNA bindingⁱ	425 – 500	Nuclear receptorPROSITE-ProRule annotationAdd BLAST	76
Zinc fingerⁱ	428 – 448	NR C4-typePROSITE-ProRule annotationAdd BLAST	21
Zinc fingerⁱ	464 – 488	NR C4-typePROSITE-ProRule annotationAdd BLAST	25

GO - Molecular functionⁱ

chromatin binding Source: MGI
core promoter binding Source: MGI
DNA binding
Source: MGI
Inferred from direct assayⁱ
- 15870285
DNA-binding transcription factor activity Source: MGI
double-stranded DNA binding Source: MGI
glucocorticoid receptor activity
Source: MGI
Inferred from direct assayⁱ
heat shock protein binding Source: MGI
hormone binding Source: MGI
Hsp70 protein binding Source: MGI
Hsp90 protein binding Source: MGI
nuclear receptor activity Source: UniProtKB
protein-containing complex binding Source: MGI
protein dimerization activity
Source: MGI
Inferred from direct assayⁱ
- 7883868
protein heterodimerization activity Source: MGI
protein homodimerization activity Source: MGI
protein kinase binding
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 20371704
receptor tyrosine kinase binding Source: MGI
RNA polymerase II proximal promoter sequence-specific DNA binding Source: MGI
RNA polymerase II regulatory region DNA binding Source: MGI
RNA polymerase II transcription factor activity, glucocorticoid-activated sequence-specific DNA binding Source: UniProtKB
sequence-specific DNA binding
Source: MGI
Inferred from direct assayⁱ
- 7883868
steroid binding Source: UniProtKB
steroid hormone binding Source: UniProtKB
SUMO binding Source: MGI
transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: MGI
transcription coactivator activity Source: MGI
transcription factor binding Source: MGI
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

adrenal gland development
Source: MGI
Inferred from mutant phenotypeⁱ
- 7628695
cellular response to dexamethasone stimulus Source: MGI
cellular response to glucocorticoid stimulus Source: MGI
cellular response to steroid hormone stimulus Source: MGI
cellular response to transforming growth factor beta stimulus Source: MGI
chromatin-mediated maintenance of transcription Source: MGI
chromatin remodeling Source: MGI
glucocorticoid metabolic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 10509797
glucocorticoid receptor signaling pathway
Source: MGI
Inferred from direct assayⁱ
- 15199138
mammary gland duct morphogenesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 12198239
maternal behavior
Source: MGI
Inferred from genetic interactionⁱ
- 23071095
negative regulation of glucocorticoid mediated signaling pathway
Source: MGI
Inferred from direct assayⁱ
- 20660300
negative regulation of synaptic plasticity Source: MGI
negative regulation of transcription by RNA polymerase II Source: MGI
negative regulation of vascular permeability Source: MGI
positive regulation of cell growth involved in cardiac muscle cell development Source: MGI
positive regulation of dendritic spine development Source: MGI
positive regulation of glucocorticoid receptor signaling pathway Source: MGI
positive regulation of glutamate secretion Source: MGI
positive regulation of neuron apoptotic process
Source: MGI
Inferred from genetic interactionⁱ
- 10744634
positive regulation of transcription by RNA polymerase II Source: UniProtKB
regulation of cell proliferation Source: MGI
regulation of glucocorticoid biosynthetic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 7628695
regulation of gluconeogenesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 7628695
regulation of glucose metabolic process Source: MGI
regulation of transcription, DNA-templated
Source: MGI
Inferred from direct assayⁱ
- 10224232
response to arsenic-containing substance Source: MGI
transcription, DNA-templated
Source: CAFA
Inferred from direct assayⁱ
- 17081986

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, DNA-binding, Receptor
Biological process	Transcription, Transcription regulation
Ligand	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, Grl1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Unplaced

Organism-specific databases

MGIⁱ	MGI:95824 Nr3c1

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	1	M → T: Abolishes expression of A-type isoforms. 1 Publication	1
Mutagenesisⁱ	28	M → T: Abolishes expression of B-type isoforms. 1-B. 1 Publication	1
Mutagenesisⁱ	426	K → A: Abolishes glucocorticoid-mediated degradation and enhances transcription trans-activation. 1 Publication	1
Mutagenesisⁱ	484	R → A: Abolishes transactivation activity. 1 Publication	1
Mutagenesisⁱ	484	R → C: Abolishes transcriptional activity. Does not impair ligand binding. 1 Publication	1
Mutagenesisⁱ	484	R → K: Does not change transactivation activity. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL3144
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	625

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000019939	1 – 783	Glucocorticoid receptorAdd BLAST		783

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	24	Omega-N-methylarginineCombined sources	1
Modified residueⁱ	46	PhosphoserineBy similarity	1
Modified residueⁱ	122	Phosphoserine1 Publication	1
Modified residueⁱ	143	PhosphoserineBy similarity	1
Modified residueⁱ	150	Phosphoserine1 Publication	1
Modified residueⁱ	159	Phosphothreonine1 Publication	1
Modified residueⁱ	212	Phosphoserine2 Publications	1
Modified residueⁱ	220	Phosphoserine2 Publications	1
Modified residueⁱ	234	Phosphoserine2 Publications	1
Modified residueⁱ	275	PhosphoserineBy similarity	1
Cross-linkⁱ	285	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linkⁱ	285	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linkⁱ	301	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linkⁱ	301	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	315	Phosphoserine1 Publication	1
Modified residueⁱ	412	PhosphoserineCombined sources	1
Cross-linkⁱ	426	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	487	N6-acetyllysineBy similarity	1
Modified residueⁱ	499	N6-acetyllysineBy similarity	1
Modified residueⁱ	501	N6-acetyllysineBy similarity	1
Modified residueⁱ	502	N6-acetyllysineBy similarity	1
Cross-linkⁱ	709	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

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.1 Publication

Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoids. Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-212, Ser-234 and Ser-412-phosphorylated forms are mainly cytoplasmic, and the Ser-220-phosphorylated form is nuclear (By similarity). Phosphorylation at Ser-220 increases transcriptional activity (By similarity). Phosphorylation at Ser-212, Ser-234 and Ser-412 decreases signaling capacity (By similarity). Phosphorylation at Ser-412 may protect from glucocorticoid-induced apoptosis (By similarity). Phosphorylation at Ser-212 and Ser-220 is not required in regulation of chromosome segregation (By similarity). May be dephosphorylated by PPP5C, attenuates NR3C1 action (PubMed:21994940).By similarity2 Publications

Sumoylation at Lys-285 and Lys-301 negatively regulates its transcriptional activity. Sumoylation at Lys-709 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-285 and Lys-301 is dispensable whereas sumoylation at Lys-709 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner.By similarity

Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P06537
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P06537
PaxDbⁱ	P06537
PeptideAtlas More...PeptideAtlasⁱ	P06537
PRIDEⁱ	P06537

PTM databases

iPTMnetⁱ	P06537
PhosphoSitePlusⁱ	P06537
SwissPalmⁱ	P06537

Expressionⁱ

Tissue specificityⁱ

Expressed in spleen, kidney and liver. Isoform 3: Expressed at highest level in spleen with lesser amounts in kidney and liver.1 Publication

Inductionⁱ

Isoform 1: Down-regulated by glucocorticoids. Isoform 3: Up-regulated by glucocorticoids and insulin.1 Publication

Gene expression databases

CleanExⁱ	MM_NR3C1

CleanExⁱ

MM_NR3C1

Interactionⁱ

Subunit structureⁱ

Heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID, STIP1, or the immunophilin homolog PPP5C (PubMed:9195923, PubMed:21994940). 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 (PubMed:9195923, PubMed:11278753). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Directly interacts with UNC45A (By similarity). Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers (PubMed:9528750). Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (PubMed:9742105). Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6 (By similarity). Interaction with BAG1 inhibits transactivation (By similarity). Interacts with HEXIM1, PELP1 and TGFB1I1 (PubMed:10848625). Interacts with NCOA1 (By similarity). Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By similarity). Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (PubMed:22170608). Interacts with CIART (PubMed:24736997). Interacts with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity). Interacts with GRIP1 (By similarity). 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). Interacts (via C-terminus) with HNRNPU (via C-terminus) (By similarity).By similarity9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
Cry1	P97784	3	EBI-15959147,EBI-1266607
Cry2	Q9R194	3	EBI-15959147,EBI-1266619
Dync1i1	O88485	2	EBI-492753,EBI-492834
Fkbp4	P30416	3	EBI-492753,EBI-492746
Fkbp5	Q64378	2	EBI-492753,EBI-492796
Hsp90ab1	P11499	2	EBI-492753,EBI-492813

GO - Molecular functionⁱ

heat shock protein binding Source: MGI
Hsp70 protein binding Source: MGI
Hsp90 protein binding Source: MGI
protein dimerization activity
Source: MGI
Inferred from direct assayⁱ
- 7883868
protein heterodimerization activity Source: MGI
protein homodimerization activity Source: MGI
protein kinase binding
Source: ARUK-UCL
Inferred from physical interactionⁱ
- 20371704
receptor tyrosine kinase binding Source: MGI
SUMO binding Source: MGI
transcription factor binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-11N
IntActⁱ	P06537, 7 interactors
STRINGⁱ	10090.ENSMUSP00000025300

Chemistry databases

BindingDBⁱ

P06537

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	538 – 545	Combined sources	8
Helixⁱ	562 – 585	Combined sources	24
Helixⁱ	590 – 592	Combined sources	3
Helixⁱ	595 – 622	Combined sources	28
Beta strandⁱ	625 – 630	Combined sources	6
Beta strandⁱ	633 – 635	Combined sources	3
Helixⁱ	637 – 640	Combined sources	4
Turnⁱ	643 – 645	Combined sources	3
Helixⁱ	646 – 662	Combined sources	17
Helixⁱ	666 – 677	Combined sources	12
Beta strandⁱ	679 – 682	Combined sources	4
Helixⁱ	689 – 708	Combined sources	20
Helixⁱ	714 – 747	Combined sources	34
Helixⁱ	749 – 751	Combined sources	3
Helixⁱ	757 – 771	Combined sources	15
Beta strandⁱ	775 – 777	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P06537
SMRⁱ	P06537
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P06537

EvolutionaryTraceⁱ

P06537

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	530 – 764	NR LBDPROSITE-ProRule annotationAdd BLAST		235

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 427	ModulatingAdd BLAST	427
Regionⁱ	492 – 783	Interaction with CLOCKBy similarityAdd BLAST	292
Regionⁱ	494 – 529	HingeAdd BLAST	36
Regionⁱ	538 – 703	Interaction with CRY1By similarityAdd BLAST	166

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	75 – 82	Poly-Gln		8
Compositional biasⁱ	407 – 426	Glu/Pro/Ser/Thr-rich (PEST region)Add BLAST		20

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

Belongs to the nuclear hormone receptor family. NR3 subfamily.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	428 – 448	NR C4-typePROSITE-ProRule annotationAdd BLAST		21
Zinc fingerⁱ	464 – 488	NR C4-typePROSITE-ProRule annotationAdd BLAST		25

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
HOGENOMⁱ	HOG000037950
HOVERGENⁱ	HBG007583
InParanoidⁱ	P06537

Family and domain databases

Gene3Dⁱ	3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR001409 Glcrtcd_rcpt IPR035500 NHR_like_dom_sf IPR000536 Nucl_hrmn_rcpt_lig-bd IPR001723 Nuclear_hrmn_rcpt IPR001628 Znf_hrmn_rcpt IPR013088 Znf_NHR/GATA
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02155 GCR, 1 hit PF00104 Hormone_recep, 1 hit PF00105 zf-C4, 1 hit
PRINTSⁱ	PR00528 GLCORTICOIDR PR00398 STRDHORMONER PR00047 STROIDFINGER
SMARTⁱ	View protein in SMART SM00430 HOLI, 1 hit SM00399 ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508 SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843 NR_LBD, 1 hit PS00031 NUCLEAR_REC_DBD_1, 1 hit PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (5+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 5 isoformsⁱ produced by alternative splicing and alternative initiation. Align Add to basket

This entry has 5 described isoforms and 6 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P06537-1) [UniParc]FASTA Add to basket

Also known as: 1-A, GR form A, Alpha

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 GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA 
        60         70         80         90        100
AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQPQPDLSKA VSLSMGLYMG 
       110        120        130        140        150
ETETKVMGND LGYPQQGQLG LSSGETDFRL LEESIANLNR STSRPENPKS 
       160        170        180        190        200
STPAAGCATP TEKEFPQTHS DPSSEQQNRK SQPGTNGGSV KLYTTDQSTF 
       210        220        230        240        250
DILQDLEFSA GSPGKETNES PWRSDLLIDE NLLSPLAGED DPFLLEGDVN 
       260        270        280        290        300
EDCKPLILPD TKPKIQDTGD TILSSPSSVA LPQVKTEKDD FIELCTPGVI 
       310        320        330        340        350
KQEKLGPVYC QASFSGTNII GNKMSAISVH GVSTSGGQMY HYDMNTASLS 
       360        370        380        390        400
QQQDQKPVFN VIPPIPVGSE NWNRCQGSGE DNLTSLGAMN FAGRSVFSNG 
       410        420        430        440        450
YSSPGMRPDV SSPPSSSSTA TGPPPKLCLV CSDEASVCHY GVLTCGSCKV 
       460        470        480        490        500
FFKRAVEGQH NYLCAGRNDC IIDKIRRKNC PACRYRKCLQ AGMNLEARKT 
       510        520        530        540        550
KKKIKGIQQA TAGVSQDTSE NANKTIVPAA LPQLTPTLVS LLEVIEPEVL 
       560        570        580        590        600
YAGYDSSVPD SAWRIMTTLN MLGGRQVIAA VKWAKAIPGF RNLHLDDQMT 
       610        620        630        640        650
LLQYSWMFLM AFALGWRSYR QASGNLLCFA PDLIINEQRM TLPCMYDQCK 
       660        670        680        690        700
HMLFISTELQ RLQVSYEEYL CMKTLLLLSS VPKEGLKSQE LFDEIRMTYI 
       710        720        730        740        750
KELGKAIVKR EGNSSQNWQR FYQLTKLLDS MHDVVENLLS YCFQTFLDKS 
       760        770        780 
MSIEFPEMLA EIITNQIPKY SNGNIKKLLF HQK

Length:783

Mass (Da):86,053

Last modified:January 1, 1988 - v1

Checksum:ⁱ455E5C1C3C955F2A

GO

Isoform 2 (identifier: P06537-2) [UniParc]FASTA Add to basket

Also known as: 2-A, GR form B, Gamma

The sequence of this isoform differs from the canonical sequence as follows:
458-458: G → GR

« Hide

        10         20         30         40         50
MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA 
        60         70         80         90        100
AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQPQPDLSKA VSLSMGLYMG 
       110        120        130        140        150
ETETKVMGND LGYPQQGQLG LSSGETDFRL LEESIANLNR STSRPENPKS 
       160        170        180        190        200
STPAAGCATP TEKEFPQTHS DPSSEQQNRK SQPGTNGGSV KLYTTDQSTF 
       210        220        230        240        250
DILQDLEFSA GSPGKETNES PWRSDLLIDE NLLSPLAGED DPFLLEGDVN 
       260        270        280        290        300
EDCKPLILPD TKPKIQDTGD TILSSPSSVA LPQVKTEKDD FIELCTPGVI 
       310        320        330        340        350
KQEKLGPVYC QASFSGTNII GNKMSAISVH GVSTSGGQMY HYDMNTASLS 
       360        370        380        390        400
QQQDQKPVFN VIPPIPVGSE NWNRCQGSGE DNLTSLGAMN FAGRSVFSNG 
       410        420        430        440        450
YSSPGMRPDV SSPPSSSSTA TGPPPKLCLV CSDEASVCHY GVLTCGSCKV 
       460        470        480        490        500
FFKRAVEGRQ HNYLCAGRND CIIDKIRRKN CPACRYRKCL QAGMNLEARK 
       510        520        530        540        550
TKKKIKGIQQ ATAGVSQDTS ENANKTIVPA ALPQLTPTLV SLLEVIEPEV 
       560        570        580        590        600
LYAGYDSSVP DSAWRIMTTL NMLGGRQVIA AVKWAKAIPG FRNLHLDDQM 
       610        620        630        640        650
TLLQYSWMFL MAFALGWRSY RQASGNLLCF APDLIINEQR MTLPCMYDQC 
       660        670        680        690        700
KHMLFISTEL QRLQVSYEEY LCMKTLLLLS SVPKEGLKSQ ELFDEIRMTY 
       710        720        730        740        750
IKELGKAIVK REGNSSQNWQ RFYQLTKLLD SMHDVVENLL SYCFQTFLDK 
       760        770        780 
SMSIEFPEML AEIITNQIPK YSNGNIKKLL FHQK

Note: Produced by alternative splicing.

Show »

Length:784

Mass (Da):86,209

Checksum:ⁱB52F39BDEDF94ADC

GO

Isoform 1-B (identifier: P06537-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MDLYKTLRGG ATVKVSASSP SVAAASQADS KQQRILLDFS KGSASNAQQQ 
        60         70         80         90        100
QQQQQPQPDL SKAVSLSMGL YMGETETKVM GNDLGYPQQG QLGLSSGETD 
       110        120        130        140        150
FRLLEESIAN LNRSTSRPEN PKSSTPAAGC ATPTEKEFPQ THSDPSSEQQ 
       160        170        180        190        200
NRKSQPGTNG GSVKLYTTDQ STFDILQDLE FSAGSPGKET NESPWRSDLL 
       210        220        230        240        250
IDENLLSPLA GEDDPFLLEG DVNEDCKPLI LPDTKPKIQD TGDTILSSPS 
       260        270        280        290        300
SVALPQVKTE KDDFIELCTP GVIKQEKLGP VYCQASFSGT NIIGNKMSAI 
       310        320        330        340        350
SVHGVSTSGG QMYHYDMNTA SLSQQQDQKP VFNVIPPIPV GSENWNRCQG 
       360        370        380        390        400
SGEDNLTSLG AMNFAGRSVF SNGYSSPGMR PDVSSPPSSS STATGPPPKL 
       410        420        430        440        450
CLVCSDEASV CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR 
       460        470        480        490        500
KNCPACRYRK CLQAGMNLEA RKTKKKIKGI QQATAGVSQD TSENANKTIV 
       510        520        530        540        550
PAALPQLTPT LVSLLEVIEP EVLYAGYDSS VPDSAWRIMT TLNMLGGRQV 
       560        570        580        590        600
IAAVKWAKAI PGFRNLHLDD QMTLLQYSWM FLMAFALGWR SYRQASGNLL 
       610        620        630        640        650
CFAPDLIINE QRMTLPCMYD QCKHMLFIST ELQRLQVSYE EYLCMKTLLL 
       660        670        680        690        700
LSSVPKEGLK SQELFDEIRM TYIKELGKAI VKREGNSSQN WQRFYQLTKL 
       710        720        730        740        750
LDSMHDVVEN LLSYCFQTFL DKSMSIEFPE MLAEIITNQI PKYSNGNIKK 

LLFHQK

Note: Produced by alternative initiation at Met-28 of isoform 1.

Show »

Length:756

Mass (Da):83,273

Checksum:ⁱAE29F70FF47F964D

GO

Isoform 2-B (identifier: P06537-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-27: Missing.
458-458: G → GR

« Hide

        10         20         30         40         50
MDLYKTLRGG ATVKVSASSP SVAAASQADS KQQRILLDFS KGSASNAQQQ 
        60         70         80         90        100
QQQQQPQPDL SKAVSLSMGL YMGETETKVM GNDLGYPQQG QLGLSSGETD 
       110        120        130        140        150
FRLLEESIAN LNRSTSRPEN PKSSTPAAGC ATPTEKEFPQ THSDPSSEQQ 
       160        170        180        190        200
NRKSQPGTNG GSVKLYTTDQ STFDILQDLE FSAGSPGKET NESPWRSDLL 
       210        220        230        240        250
IDENLLSPLA GEDDPFLLEG DVNEDCKPLI LPDTKPKIQD TGDTILSSPS 
       260        270        280        290        300
SVALPQVKTE KDDFIELCTP GVIKQEKLGP VYCQASFSGT NIIGNKMSAI 
       310        320        330        340        350
SVHGVSTSGG QMYHYDMNTA SLSQQQDQKP VFNVIPPIPV GSENWNRCQG 
       360        370        380        390        400
SGEDNLTSLG AMNFAGRSVF SNGYSSPGMR PDVSSPPSSS STATGPPPKL 
       410        420        430        440        450
CLVCSDEASV CHYGVLTCGS CKVFFKRAVE GRQHNYLCAG RNDCIIDKIR 
       460        470        480        490        500
RKNCPACRYR KCLQAGMNLE ARKTKKKIKG IQQATAGVSQ DTSENANKTI 
       510        520        530        540        550
VPAALPQLTP TLVSLLEVIE PEVLYAGYDS SVPDSAWRIM TTLNMLGGRQ 
       560        570        580        590        600
VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW MFLMAFALGW RSYRQASGNL 
       610        620        630        640        650
LCFAPDLIIN EQRMTLPCMY DQCKHMLFIS TELQRLQVSY EEYLCMKTLL 
       660        670        680        690        700
LLSSVPKEGL KSQELFDEIR MTYIKELGKA IVKREGNSSQ NWQRFYQLTK 
       710        720        730        740        750
LLDSMHDVVE NLLSYCFQTF LDKSMSIEFP EMLAEIITNQ IPKYSNGNIK 

KLLFHQK

Note: Produced by alternative initiation at Met-28 of isoform 2.

Show »

Length:757

Mass (Da):83,429

Checksum:ⁱEBD44E16FE31A015

GO

Isoform 3 (identifier: P06537-5) [UniParc]FASTA Add to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
735-748: VENLLSYCFQTFLD → STKHKSKTTAKKKK
749-783: Missing.

« Hide

        10         20         30         40         50
MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA 
        60         70         80         90        100
AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQPQPDLSKA VSLSMGLYMG 
       110        120        130        140        150
ETETKVMGND LGYPQQGQLG LSSGETDFRL LEESIANLNR STSRPENPKS 
       160        170        180        190        200
STPAAGCATP TEKEFPQTHS DPSSEQQNRK SQPGTNGGSV KLYTTDQSTF 
       210        220        230        240        250
DILQDLEFSA GSPGKETNES PWRSDLLIDE NLLSPLAGED DPFLLEGDVN 
       260        270        280        290        300
EDCKPLILPD TKPKIQDTGD TILSSPSSVA LPQVKTEKDD FIELCTPGVI 
       310        320        330        340        350
KQEKLGPVYC QASFSGTNII GNKMSAISVH GVSTSGGQMY HYDMNTASLS 
       360        370        380        390        400
QQQDQKPVFN VIPPIPVGSE NWNRCQGSGE DNLTSLGAMN FAGRSVFSNG 
       410        420        430        440        450
YSSPGMRPDV SSPPSSSSTA TGPPPKLCLV CSDEASVCHY GVLTCGSCKV 
       460        470        480        490        500
FFKRAVEGQH NYLCAGRNDC IIDKIRRKNC PACRYRKCLQ AGMNLEARKT 
       510        520        530        540        550
KKKIKGIQQA TAGVSQDTSE NANKTIVPAA LPQLTPTLVS LLEVIEPEVL 
       560        570        580        590        600
YAGYDSSVPD SAWRIMTTLN MLGGRQVIAA VKWAKAIPGF RNLHLDDQMT 
       610        620        630        640        650
LLQYSWMFLM AFALGWRSYR QASGNLLCFA PDLIINEQRM TLPCMYDQCK 
       660        670        680        690        700
HMLFISTELQ RLQVSYEEYL CMKTLLLLSS VPKEGLKSQE LFDEIRMTYI 
       710        720        730        740 
KELGKAIVKR EGNSSQNWQR FYQLTKLLDS MHDVSTKHKS KTTAKKKK

Show »

Length:748

Mass (Da):81,888

Checksum:ⁱ81F4E19AFED446EB

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E9PUR6	E9PUR6_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	792	Annotation score:
E9PYV1	E9PYV1_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	793	Annotation score:
E9Q310	E9Q310_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	488	Annotation score:
E9Q8A6	E9Q8A6_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	129	Annotation score:
D3YTK8	D3YTK8_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	49	Annotation score:
D3Z280	D3Z280_MOUSE	Glucocorticoid receptor Glucocorticoid receptor	Nr3c1	24	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	437	V → G in ADM18962 (PubMed:20660300).Curated	1
Sequence conflictⁱ	437	V → G in CAA31738 (PubMed:2911477).Curated	1
Sequence conflictⁱ	437	V → G in CAA31739 (PubMed:2911477).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_018774	1 – 27	Missing in isoform 1-B and isoform 2-B. CuratedAdd BLAST	27
Alternative sequenceⁱVSP_003704	458	G → GR in isoform 2 and isoform 2-B. 1 Publication	1
Alternative sequenceⁱVSP_058320	735 – 748	VENLL…QTFLD → STKHKSKTTAKKKK in isoform 3. Add BLAST	14
Alternative sequenceⁱVSP_058321	749 – 783	Missing in isoform 3. Add BLAST	35

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04435 mRNA Translation: CAA28031.1 HM236293 mRNA Translation: ADM18962.1 X13358 mRNA Translation: CAA31738.1 X13359 mRNA Translation: CAA31739.1
PIRⁱ	A25691
UniGeneⁱ	Mm.129481

Keywords - Coding sequence diversityⁱ

Alternative initiation, Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P06537-2	Isoform 2-B of Glucocorticoid receptor		MOUSE		757	UniRef100_P06537-4
Glucocorticoid receptor (Fragment)		MOUSE		16
P06537-4	Isoform 2 of Glucocorticoid receptor		MOUSE		784	UniRef100_P06537-4
Glucocorticoid receptor (Fragment)		MOUSE		16

Protein	Similar proteins		Species	Score	Length	Source
P06537	Glucocorticoid receptor	)	RAT		795	UniRef90_P06536
Glucocorticoid receptor		MOUSE		793
UPI000A30F4AB		MUSPA		793
UPI000A3154D9		MUSCR		787
UPI000B4E9FC3		MERUN		781
+22

Protein	Similar proteins		Species	Score	Length	Source
P06537	Glucocorticoid receptor	)	HUMAN		777	UniRef50_P04150
Glucocorticoid receptor		PONAB		777
Glucocorticoid receptor		XENLA		776
Glucocorticoid receptor		PIG		782
Glucocorticoid receptor		CAVPO		771
+535

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04435 mRNA Translation: CAA28031.1 HM236293 mRNA Translation: ADM18962.1 X13358 mRNA Translation: CAA31738.1 X13359 mRNA Translation: CAA31739.1
PIRⁱ	A25691
UniGeneⁱ	Mm.129481

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3MNE	X-ray	1.96	A	527-783	[»]
	3MNO	X-ray	1.55	A	527-783	[»]
	3MNP	X-ray	1.50	A	527-783	[»]
ProteinModelPortalⁱ	P06537
SMRⁱ	P06537
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-11N
IntActⁱ	P06537, 7 interactors
STRINGⁱ	10090.ENSMUSP00000025300

Chemistry databases

BindingDBⁱ	P06537
ChEMBLⁱ	CHEMBL3144
GuidetoPHARMACOLOGYⁱ	625

PTM databases

iPTMnetⁱ	P06537
PhosphoSitePlusⁱ	P06537
SwissPalmⁱ	P06537

Proteomic databases

EPDⁱ	P06537
MaxQBⁱ	P06537
PaxDbⁱ	P06537
PeptideAtlasⁱ	P06537
PRIDEⁱ	P06537

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Organism-specific databases

MGIⁱ	MGI:95824 Nr3c1

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
HOGENOMⁱ	HOG000037950
HOVERGENⁱ	HBG007583
InParanoidⁱ	P06537

Miscellaneous databases

ChiTaRSⁱ	Nr3c1 mouse
EvolutionaryTraceⁱ	P06537
Protein Ontology More...PROⁱ	PR:P06537
SOURCEⁱ	Search...

Gene expression databases

CleanExⁱ	MM_NR3C1

CleanExⁱ

MM_NR3C1

Family and domain databases

Gene3Dⁱ	3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR001409 Glcrtcd_rcpt IPR035500 NHR_like_dom_sf IPR000536 Nucl_hrmn_rcpt_lig-bd IPR001723 Nuclear_hrmn_rcpt IPR001628 Znf_hrmn_rcpt IPR013088 Znf_NHR/GATA
Pfamⁱ	View protein in Pfam PF02155 GCR, 1 hit PF00104 Hormone_recep, 1 hit PF00105 zf-C4, 1 hit
PRINTSⁱ	PR00528 GLCORTICOIDR PR00398 STRDHORMONER PR00047 STROIDFINGER
SMARTⁱ	View protein in SMART SM00430 HOLI, 1 hit SM00399 ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508 SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843 NR_LBD, 1 hit PS00031 NUCLEAR_REC_DBD_1, 1 hit PS51030 NUCLEAR_REC_DBD_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GCR_MOUSE
Accessionⁱ	P06537Primary (citable) accession number: P06537 Secondary accession number(s): E0ZPU5, Q61628, Q61629
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 1, 1988
	Last modified:	September 12, 2018
	This is version 202 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

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Annotation systems

Supporting data

UniProtKB - P06537 (GCR_MOUSE)

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Glucocorticoid receptor

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Mitochondrion

Cytoskeleton

Nucleus

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Nucleus

Other locations

Cytoskeleton

Cytosol

Mitochondrion

Nucleus

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Keywords - Cellular componenti

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Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ