UniProtKB - P06537 (GCR_MOUSE)
Glucocorticoid receptor
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 PublicationsHas 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 PublicationsActs 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 PublicationMiscellaneous
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 434 – 509 | Nuclear receptorPROSITE-ProRule annotationAdd BLAST | 76 | |
Zinc fingeri | 437 – 457 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 473 – 497 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
GO - Molecular functioni
- chromatin binding Source: MGI
- core promoter sequence-specific DNA binding Source: MGI
- DNA binding Source: MGI
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription factor activity Source: MGI
- DNA-binding transcription repressor activity, RNA polymerase II-specific Source: MGI
- double-stranded DNA binding Source: MGI
- glucocorticoid receptor activity Source: MGI
- heat shock protein binding Source: MGI
- hormone binding Source: MGI
- Hsp70 protein binding Source: MGI
- Hsp90 protein binding Source: MGI
- identical protein binding Source: MGI
- nuclear receptor activity Source: UniProtKB
- protein-containing complex binding Source: MGI
- protein kinase binding Source: ARUK-UCL
- receptor tyrosine kinase binding Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: MGI
- sequence-specific double-stranded DNA binding Source: MGI
- steroid binding Source: UniProtKB
- steroid hormone binding Source: UniProtKB
- transcription coactivator activity Source: MGI
- zinc ion binding Source: InterPro
GO - Biological processi
- adrenal gland development Source: MGI
- 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 remodeling Source: MGI
- epigenetic maintenance of chromatin in transcription-competent conformation Source: MGI
- glucocorticoid metabolic process Source: MGI
- glucocorticoid receptor signaling pathway Source: BHF-UCL
- intracellular steroid hormone receptor signaling pathway Source: GO_Central
- mammary gland duct morphogenesis Source: MGI
- maternal behavior Source: MGI
- negative regulation of apoptotic process Source: MGI
- negative regulation of synaptic plasticity Source: MGI
- negative regulation of transcription, DNA-templated 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 miRNA transcription Source: BHF-UCL
- positive regulation of neuron apoptotic process Source: MGI
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- regulation of cell population proliferation Source: MGI
- regulation of glucocorticoid biosynthetic process Source: MGI
- regulation of gluconeogenesis Source: MGI
- regulation of glucose metabolic process Source: MGI
- regulation of transcription, DNA-templated Source: CAFA
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to arsenic-containing substance Source: MGI
Keywordsi
Molecular function | Chromatin regulator, DNA-binding, Receptor |
Biological process | Transcription, Transcription regulation |
Ligand | Lipid-binding, Metal-binding, Steroid-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand R-MMU-383280, Nuclear Receptor transcription pathway R-MMU-4090294, SUMOylation of intracellular receptors |
Names & Taxonomyi
Protein namesi | Recommended name: Glucocorticoid receptorShort 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 | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:95824, Nr3c1 |
VEuPathDBi | HostDB:ENSMUSG00000024431 |
Subcellular locationi
Nucleus
- Nucleus 4 Publications
Cytoplasm and Cytosol
- Cytoplasm 3 Publications
Note: Cytoplasmic in the absence of ligand, nuclear after ligand-binding (PubMed:11278753). The hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment (PubMed:10678832). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (PubMed:27686098). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (PubMed:27686098).3 Publications
Nucleus
- Nucleus By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Mitochondrion
- Mitochondrion By similarity
Cytoskeleton
- spindle By similarity
- centrosome By similarity
Note: After ligand activation, translocates from the cytoplasm to the nucleus.By similarity
Cytoskeleton
- microtubule organizing center Source: UniProtKB-SubCell
- spindle Source: UniProtKB-SubCell
Cytosol
- cytosol Source: MGI
Mitochondrion
- mitochondrion Source: UniProtKB-SubCell
Nucleus
- nuclear speck Source: UniProtKB
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- cytoplasm Source: UniProtKB
- dendritic spine Source: MGI
- glutamatergic synapse Source: MGI
- membrane Source: MGI
- neuron projection Source: MGI
- postsynaptic density Source: MGI
- postsynaptic density, intracellular component Source: MGI
- protein-containing complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, Mitochondrion, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | 435 | K → A: Abolishes glucocorticoid-mediated degradation and enhances transcription trans-activation. 1 Publication | 1 | |
Mutagenesisi | 493 | R → A: Abolishes transactivation activity. 1 Publication | 1 | |
Mutagenesisi | 493 | R → C: Abolishes transcriptional activity. Does not impair ligand binding. 1 Publication | 1 | |
Mutagenesisi | 493 | R → K: Does not change transactivation activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3144 |
DrugCentrali | P06537 |
GuidetoPHARMACOLOGYi | 625 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000019939 | 1 – 792 | Glucocorticoid receptorAdd BLAST | 792 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 24 | Omega-N-methylarginineCombined sources | 1 | |
Modified residuei | 46 | PhosphoserineBy similarity | 1 | |
Modified residuei | 131 | Phosphoserine1 Publication | 1 | |
Modified residuei | 152 | PhosphoserineBy similarity | 1 | |
Modified residuei | 159 | Phosphoserine1 Publication | 1 | |
Modified residuei | 168 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 221 | Phosphoserine2 Publications | 1 | |
Modified residuei | 229 | Phosphoserine2 Publications | 1 | |
Modified residuei | 243 | Phosphoserine2 Publications | 1 | |
Modified residuei | 284 | PhosphoserineBy similarity | 1 | |
Cross-linki | 294 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity | ||
Cross-linki | 294 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Cross-linki | 310 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity | ||
Cross-linki | 310 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 324 | Phosphoserine1 Publication | 1 | |
Modified residuei | 421 | PhosphoserineCombined sources | 1 | |
Cross-linki | 435 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication | ||
Modified residuei | 496 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 508 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 510 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 511 | N6-acetyllysineBy similarity | 1 | |
Cross-linki | 718 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P06537 |
jPOSTi | P06537 |
MaxQBi | P06537 |
PaxDbi | P06537 |
PeptideAtlasi | P06537 |
PRIDEi | P06537 |
ProteomicsDBi | 271197 [P06537-1] 271198 [P06537-2] 271199 [P06537-3] 271200 [P06537-4] 271201 [P06537-5] 333325 355014 |
PTM databases
iPTMneti | P06537 |
PhosphoSitePlusi | P06537 |
SwissPalmi | P06537 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000024431, Expressed in brain blood vessel and 330 other tissues |
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 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, PubMed:28751364).
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).
Interacts with MCM3AP (By similarity).
Interacts (via domain NR LBD) with HSP90AA1 and HSP90AB1 (PubMed:27686098). In the absence of hormonal ligand, interacts with TACC1 (By similarity).
By similarity11 PublicationsBinary interactionsi
P06537
With | #Exp. | IntAct |
---|---|---|
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 |
Isoform 1 [P06537-1]
With | #Exp. | IntAct |
---|---|---|
Cry1 [P97784] | 3 | EBI-15959147,EBI-1266607 |
Cry2 [Q9R194] | 3 | EBI-15959147,EBI-1266619 |
GO - Molecular functioni
- heat shock protein binding Source: MGI
- Hsp70 protein binding Source: MGI
- Hsp90 protein binding Source: MGI
- identical protein binding Source: MGI
- protein kinase binding Source: ARUK-UCL
- receptor tyrosine kinase binding Source: MGI
Protein-protein interaction databases
CORUMi | P06537 |
DIPi | DIP-11N |
IntActi | P06537, 12 interactors |
MINTi | P06537 |
STRINGi | 10090.ENSMUSP00000095199 |
Chemistry databases
BindingDBi | P06537 |
Miscellaneous databases
RNActi | P06537, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P06537 |
SMRi | P06537 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06537 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 539 – 773 | NR LBDPROSITE-ProRule annotationAdd BLAST | 235 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 436 | ModulatingAdd BLAST | 436 | |
Regioni | 1 – 25 | DisorderedSequence analysisAdd BLAST | 25 | |
Regioni | 67 – 98 | DisorderedSequence analysisAdd BLAST | 32 | |
Regioni | 148 – 201 | DisorderedSequence analysisAdd BLAST | 54 | |
Regioni | 501 – 792 | Interaction with CLOCKBy similarityAdd BLAST | 292 | |
Regioni | 503 – 538 | HingeAdd BLAST | 36 | |
Regioni | 547 – 712 | Interaction with CRY1By similarityAdd BLAST | 166 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 437 – 457 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 473 – 497 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000156385 |
HOGENOMi | CLU_020317_0_0_1 |
InParanoidi | P06537 |
OMAi | NLPCMYD |
OrthoDBi | 333292at2759 |
TreeFami | TF106510 |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 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 |
s (5+)i Sequence
Sequence statusi: Complete.
This entry describes 5 produced by isoformsialternative splicing and alternative initiation. AlignAdd to basketThis entry has 5 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MDSKESLAPP GRDEVPSSLL GRGRGSVMDL YKTLRGGATV KVSASSPSVA
60 70 80 90 100
AASQADSKQQ RILLDFSKGS ASNAQQQQQQ QQQQQQQQQQ QPQPDLSKAV
110 120 130 140 150
SLSMGLYMGE TETKVMGNDL GYPQQGQLGL SSGETDFRLL EESIANLNRS
160 170 180 190 200
TSRPENPKSS TPAAGCATPT EKEFPQTHSD PSSEQQNRKS QPGTNGGSVK
210 220 230 240 250
LYTTDQSTFD ILQDLEFSAG SPGKETNESP WRSDLLIDEN LLSPLAGEDD
260 270 280 290 300
PFLLEGDVNE DCKPLILPDT KPKIQDTGDT ILSSPSSVAL PQVKTEKDDF
310 320 330 340 350
IELCTPGVIK QEKLGPVYCQ ASFSGTNIIG NKMSAISVHG VSTSGGQMYH
360 370 380 390 400
YDMNTASLSQ QQDQKPVFNV IPPIPVGSEN WNRCQGSGED NLTSLGAMNF
410 420 430 440 450
AGRSVFSNGY SSPGMRPDVS SPPSSSSTAT GPPPKLCLVC SDEASGCHYG
460 470 480 490 500
VLTCGSCKVF FKRAVEGQHN YLCAGRNDCI IDKIRRKNCP ACRYRKCLQA
510 520 530 540 550
GMNLEARKTK KKIKGIQQAT AGVSQDTSEN ANKTIVPAAL PQLTPTLVSL
560 570 580 590 600
LEVIEPEVLY AGYDSSVPDS AWRIMTTLNM LGGRQVIAAV KWAKAIPGFR
610 620 630 640 650
NLHLDDQMTL LQYSWMFLMA FALGWRSYRQ ASGNLLCFAP DLIINEQRMT
660 670 680 690 700
LPCMYDQCKH MLFISTELQR LQVSYEEYLC MKTLLLLSSV PKEGLKSQEL
710 720 730 740 750
FDEIRMTYIK ELGKAIVKRE GNSSQNWQRF YQLTKLLDSM HDVVENLLSY
760 770 780 790
CFQTFLDKSM SIEFPEMLAE IITNQIPKYS NGNIKKLLFH QK
The sequence of this isoform differs from the canonical sequence as follows:
1-27: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
1-27: Missing.
467-467: G → GR
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9Q310 | E9Q310_MOUSE | Glucocorticoid receptor | Nr3c1 | 488 | Annotation score: | ||
E9Q8A6 | E9Q8A6_MOUSE | Glucocorticoid receptor | Nr3c1 | 129 | Annotation score: | ||
D3YTK8 | D3YTK8_MOUSE | Glucocorticoid receptor | Nr3c1 | 49 | Annotation score: | ||
D3Z280 | D3Z280_MOUSE | Glucocorticoid receptor | Nr3c1 | 24 | Annotation score: | ||
A0A494B9W1 | A0A494B9W1_MOUSE | Glucocorticoid receptor | Nr3c1 | 35 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 432 | P → L in BAE33674 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 446 | G → V in CAA28031 (PubMed:3780669).Curated | 1 | |
Sequence conflicti | 792 | K → E in BAE33674 (PubMed:16141072).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 78 – 86 | Missing 4 Publications | 9 | |
Natural varianti | 91 | Missing 1 Publication | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_018774 | 1 – 27 | Missing in isoform 1-B and isoform 2-B. CuratedAdd BLAST | 27 | |
Alternative sequenceiVSP_003704 | 467 | G → GR in isoform 2 and isoform 2-B. 1 Publication | 1 | |
Alternative sequenceiVSP_058320 | 744 – 757 | VENLL…QTFLD → STKHKSKTTAKKKK in isoform 3. Add BLAST | 14 | |
Alternative sequenceiVSP_058321 | 758 – 792 | Missing in isoform 3. Add BLAST | 35 |
Sequence databases
Genome annotation databases
Ensembli | ENSMUST00000025300; ENSMUSP00000025300; ENSMUSG00000024431 [P06537-1] ENSMUST00000097592; ENSMUSP00000095199; ENSMUSG00000024431 [P06537-2] ENSMUST00000115567; ENSMUSP00000111229; ENSMUSG00000024431 [P06537-1] ENSMUST00000115571; ENSMUSP00000111233; ENSMUSG00000024431 [P06537-1] |
GeneIDi | 14815 |
UCSCi | uc008esx.1, mouse |
Keywords - Coding sequence diversityi
Alternative initiation, Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3MNE | X-ray | 1.96 | A | 536-792 | [»] | |
3MNO | X-ray | 1.55 | A | 536-792 | [»] | |
3MNP | X-ray | 1.50 | A | 536-792 | [»] | |
AlphaFoldDBi | P06537 | |||||
SMRi | P06537 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P06537 |
DIPi | DIP-11N |
IntActi | P06537, 12 interactors |
MINTi | P06537 |
STRINGi | 10090.ENSMUSP00000095199 |
Chemistry databases
BindingDBi | P06537 |
ChEMBLi | CHEMBL3144 |
DrugCentrali | P06537 |
GuidetoPHARMACOLOGYi | 625 |
PTM databases
iPTMneti | P06537 |
PhosphoSitePlusi | P06537 |
SwissPalmi | P06537 |
Proteomic databases
EPDi | P06537 |
jPOSTi | P06537 |
MaxQBi | P06537 |
PaxDbi | P06537 |
PeptideAtlasi | P06537 |
PRIDEi | P06537 |
ProteomicsDBi | 271197 [P06537-1] 271198 [P06537-2] 271199 [P06537-3] 271200 [P06537-4] 271201 [P06537-5] 333325 355014 |
Protocols and materials databases
Antibodypediai | 1329, 1310 antibodies from 43 providers |
DNASUi | 14815 |
Genome annotation databases
Organism-specific databases
CTDi | 2908 |
MGIi | MGI:95824, Nr3c1 |
VEuPathDBi | HostDB:ENSMUSG00000024431 |
Phylogenomic databases
eggNOGi | KOG3575, Eukaryota |
GeneTreei | ENSGT00940000156385 |
HOGENOMi | CLU_020317_0_0_1 |
InParanoidi | P06537 |
OMAi | NLPCMYD |
OrthoDBi | 333292at2759 |
TreeFami | TF106510 |
Enzyme and pathway databases
Reactomei | R-MMU-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand R-MMU-383280, Nuclear Receptor transcription pathway R-MMU-4090294, SUMOylation of intracellular receptors |
Miscellaneous databases
BioGRID-ORCSi | 14815, 0 hits in 78 CRISPR screens |
ChiTaRSi | Nr3c1, mouse |
EvolutionaryTracei | P06537 |
PROi | PR:P06537 |
RNActi | P06537, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000024431, Expressed in brain blood vessel and 330 other tissues |
Family and domain databases
Gene3Di | 1.10.565.10, 1 hit 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | GCR_MOUSE | |
Accessioni | P06537Primary (citable) accession number: P06537 Secondary accession number(s): E0ZPU5 Q61629 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | September 29, 2021 | |
Last modified: | May 25, 2022 | |
This is version 225 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families