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UniProtKB - P04150 (GCR_HUMAN)

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Protein

Glucocorticoid receptor

Gene

NR3C1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Receptor for glucocorticoids (GC) (PubMed:27120390). 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:9590696). 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 (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity).By similarity3 Publications
Isoform Alpha: Has transcriptional activation and repression activity (PubMed:15866175, PubMed:19248771, PubMed:20484466, PubMed:23820903, PubMed:11435610, PubMed:15769988, PubMed:17635946, PubMed:19141540, PubMed:21664385). Mediates glucocorticoid-induced apoptosis (PubMed:23303127). 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 (By similarity).By similarity11 Publications
Isoform Beta: Acts as a dominant negative inhibitor of isoform Alpha (PubMed:7769088, PubMed:8621628, PubMed:20484466). Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed (PubMed:19248771, PubMed:26711253). Loses this transcription modulator function on its own (PubMed:20484466). Has no hormone-binding activity (PubMed:8621628). May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner (PubMed:26711253). Directly regulates STAT1 expression in isoform Alpha-independent manner (PubMed:26711253).By similarity5 Publications
Isoform Alpha-2: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism (PubMed:20484466).
Isoform GR-P: Increases activity of isoform Alpha.1 Publication
Isoform Alpha-B: More effective than isoform Alpha in transcriptional activation, but not repression activity.2 Publications
Isoform 10: Has transcriptional activation activity.1 Publication
Isoform Alpha-C1: Has transcriptional activation activity.1 Publication
Isoform Alpha-C2: Has transcriptional activation activity.1 Publication
Isoform Alpha-C3: Has highest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127). Mediates glucocorticoid-induced apoptosis (PubMed:23303127, PubMed:23820903).3 Publications
Isoform Alpha-D1: Has transcriptional activation activity.1 Publication
Isoform Alpha-D2: Has transcriptional activation activity.1 Publication
Isoform Alpha-D3: Has lowest transcriptional activation activity of all isoforms created by alternative initiation (PubMed:15866175, PubMed:23820903). Has transcriptional repression activity (PubMed:23303127).3 Publications

Miscellaneous

Isoform Beta: High constitutive expression by neutrophils may provide a mechanism by which these cells escape glucocorticoid-induced cell death and up-regulation by proinflammatory cytokines such as IL8 further enhances their survival in the presence of glucocorticoids during inflammation.1 Publication
Can up- or down-modulate aggregation and nuclear localization of expanded polyglutamine polypeptides derived from AR and HD through specific regulation of gene expression. Aggregation and nuclear localization of expanded polyglutamine proteins are regulated cellular processes that can be modulated by this receptor, a well-characterized transcriptional regulator.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi418 – 493Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
Zinc fingeri421 – 441NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri457 – 476NR C4-typePROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

  • core promoter binding Source: CAFA
  • DNA binding transcription factor activity Source: UniProtKB
  • glucocorticoid receptor activity Source: ProtInc
  • Hsp90 protein binding Source: UniProtKB
  • nuclear receptor activity Source: UniProtKB
  • protein kinase binding Source: ARUK-UCL
  • RNA binding Source: UniProtKB-KW
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, glucocorticoid-activated sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • steroid binding Source: UniProtKB
  • steroid hormone binding Source: UniProtKB
  • SUMO binding Source: CAFA
  • transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular response to dexamethasone stimulus Source: CAFA
  • cellular response to glucocorticoid stimulus Source: UniProtKB
  • cellular response to steroid hormone stimulus Source: UniProtKB
  • cellular response to transforming growth factor beta stimulus Source: CAFA
  • chromatin organization Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB-KW
  • negative regulation of transcription by RNA polymerase II Source: CAFA
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: CAFA
  • transcription by RNA polymerase II Source: ProtInc
  • transcription initiation from RNA polymerase II promoter Source: Reactome
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Receptor, RNA-binding
Biological processApoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis, Transcription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-400253 Circadian Clock
R-HSA-8849473 PTK6 Expression
R-HSA-8939902 Regulation of RUNX2 expression and activity
SignaLinkiP04150
SIGNORiP04150

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113580.14
HGNCiHGNC:7978 NR3C1
MIMi138040 gene
neXtProtiNX_P04150

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Glucocorticoid resistance, generalized (GCCR)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by increased plasma cortisol concentration and high urinary free cortisol, resistance to adrenal suppression by dexamethasone, and the absence of Cushing syndrome typical signs. Clinical features include hypoglycemia, hypertension, metabolic alkalosis, chronic fatigue and profound anxiety.
See also OMIM:615962
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075799423V → A in GCCR; unknown pathological significance; reduces transactivation activity; delays nuclear translocation; does not exert a dominant negative effect; impairs DNA binding. 1 Publication1
Natural variantiVAR_013472477R → H in GCCR. 1 PublicationCorresponds to variant dbSNP:rs104893913EnsemblClinVar.1
Natural variantiVAR_077143477R → S in GCCR; loss of DNA-binding and of transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type. 1 Publication1
Natural variantiVAR_077144478Y → C in GCCR; decreased DNA-binding and transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type. 1 Publication1
Natural variantiVAR_075800556T → I in GCCR; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding. 2 Publications1
Natural variantiVAR_015632559I → N in GCCR; interferes with translocation to the nucleus and thereby strongly reduces transcription activation; is equally impaired in nuclear export; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893909EnsemblClinVar.1
Natural variantiVAR_075801575V → G in GCCR; unknown pathological significance; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding. 1 Publication1
Natural variantiVAR_004676641D → V in GCCR. 1 PublicationCorresponds to variant dbSNP:rs104893908EnsemblClinVar.1
Natural variantiVAR_077145672L → P in GCCR; loss of dexamethasone-binding, dexamethasone-induced translocation to the nucleus and of transactivation activity. 1 Publication1
Natural variantiVAR_013473679G → S in GCCR; has 50% binding affinity. 1 PublicationCorresponds to variant dbSNP:rs104893914EnsemblClinVar.1
Natural variantiVAR_075802714R → Q in GCCR; unknown pathological significance; reduces transactivation; reduces affinity for ligand; exerts a dominant negative effect; does not impair DNA binding. 1 Publication1
Natural variantiVAR_075803726H → R in GCCR; unknown pathological significance; reduces transactivation and transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not impair DNA binding. 1 Publication1
Natural variantiVAR_004677729V → I in GCCR. 1 PublicationCorresponds to variant dbSNP:rs1027058734Ensembl.1
Natural variantiVAR_071935737F → L in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs121909727EnsemblClinVar.1
Natural variantiVAR_015633747I → M in GCCR; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893910EnsemblClinVar.1
Natural variantiVAR_071936773L → P in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893912EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → T: Abolishes expression of A-type isoforms. 2 Publications1
Mutagenesisi27M → T: Abolishes expression of B-type isoforms. 2 Publications1
Mutagenesisi86M → I: Abolishes expression of C-type isoforms; when associated with I-90 and I-98. 1 Publication1
Mutagenesisi90M → I: Abolishes expression of C-type isoforms; when associated with I-86 and I-98. 1 Publication1
Mutagenesisi98M → I: Abolishes expression of C-type isoforms; when associated with I-86 and I-90. 1 Publication1
Mutagenesisi101D → A: Reduces transcription activation activity of isoform Alpha-C3 by half. 1 Publication1
Mutagenesisi101D → K: Reduces transcription activation activity of isoform Alpha-C3 by half. Suppresses apoptosis-inducing activity of isoform Alpha-C3. Impairs recruitment of selected coregulators onto DNA binding sites. 1 Publication1
Mutagenesisi106 – 107QQ → LL: Reduces activity of isoform Alpha-C3 by half. 1 Publication2
Mutagenesisi113 – 114SS → AA: Does not affect the activity of isoform Alpha-C3. 1 Publication2
Mutagenesisi191F → D: Reduces transactivation by the ADA complex. 1 Publication1
Mutagenesisi193I → D: Reduces transactivation by the ADA complex. 1 Publication1
Mutagenesisi194L → A: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225. 1 Publication1
Mutagenesisi197L → E: Reduces transactivation by the ADA complex. 1 Publication1
Mutagenesisi211S → A: Reduces expression of target genes IGFBP1 and IRF8. 1 Publication1
Mutagenesisi213W → A: Strongly reduces transactivation by the ADA complex. 1 Publication1
Mutagenesisi224L → V: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225. 1 Publication1
Mutagenesisi225L → F: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224. 1 Publication1
Mutagenesisi226S → A: Abolishes phosphorylation and enhances transcriptional activation. 1 Publication1
Mutagenesisi235F → L: Strongly reduces transactivation by the ADA complex; when associated with V-236. 1 Publication1
Mutagenesisi236L → V: Strongly reduces transactivation by the ADA complex; when associated with L-235. 1 Publication1
Mutagenesisi277K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293. 1 Publication1
Mutagenesisi293K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277. 1 Publication1
Mutagenesisi316M → I: Abolishes expression of D-type isoforms; when associated with I-331 and I-336. 1 Publication1
Mutagenesisi331M → I: Abolishes expression of D-type isoforms; when associated with I-316 and I-336. 1 Publication1
Mutagenesisi336M → I: Abolishes expression of D-type isoforms; when associated with I-316 and I-331. 1 Publication1
Mutagenesisi404S → A: Abolishes phosphorylation. Does not affect translocation to the nucleus following ligand stimulation. Increases protein half-life and transcriptional repressor activity. Alters repertoire of regulated genes. Increases cell death. 1 Publication1
Mutagenesisi404S → D: Does not affect translocation to the nucleus following ligand stimulation. 1 Publication1
Mutagenesisi480K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-492; A-494 and A-495. 1 Publication1
Mutagenesisi492K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-494 and A-495. 1 Publication1
Mutagenesisi494K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-495. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-492 and A-495. 1 Publication1
Mutagenesisi495K → A: Decrease in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-494. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-ARNTL/BMAL1 heterodimer; when associated with A-480; A-492 and A-494. 1 Publication1
Mutagenesisi585R → A: Reduces activation mediated by ligand binding domain; when associated with A-590. 1 Publication1
Mutagenesisi590D → A: Reduces activation mediated by ligand binding domain; when associated with A-585. 1 Publication1
Mutagenesisi602F → S: Increases solubility. No effect on transactivation by dexamethasone. 1 Publication1
Mutagenesisi625P → A: Decreases transactivation by dexamethasone by 95%. 1 Publication1
Mutagenesisi628I → A: Decreases dimerization and transactivation by dexamethasone; when associated with S-602. 1 Publication1
Mutagenesisi703K → R: Slightly reduces sumoylation. Inhibits the stimulatory effect of RWDD3 on its transcriptional activity. 2 Publications1

Keywords - Diseasei

Disease mutation, Pseudohermaphroditism

Organism-specific databases

DisGeNETi2908
MalaCardsiNR3C1
MIMi615962 phenotype
OpenTargetsiENSG00000113580
Orphaneti786 Glucocorticoid resistance
PharmGKBiPA181

Chemistry databases

ChEMBLiCHEMBL2034
DrugBankiDB00240 Alclometasone
DB00288 Amcinonide
DB00394 Beclomethasone dipropionate
DB00443 Betamethasone
DB01222 Budesonide
DB01410 Ciclesonide
DB01013 Clobetasol propionate
DB13158 Clobetasone
DB00838 Clocortolone
DB01380 Cortisone acetate
DB01260 Desonide
DB00547 Desoximetasone
DB01234 Dexamethasone
DB00223 Diflorasone
DB06781 Difluprednate
DB00687 Fludrocortisone
DB00663 Flumethasone
DB00180 Flunisolide
DB00591 Fluocinolone Acetonide
DB01047 Fluocinonide
DB00324 Fluorometholone
DB01185 Fluoxymesterone
DB00846 Flurandrenolide
DB08906 Fluticasone furoate
DB00588 Fluticasone Propionate
DB00769 Hydrocortamate
DB00741 Hydrocortisone
DB00873 Loteprednol
DB00253 Medrysone
DB00351 Megestrol acetate
DB00959 Methylprednisolone
DB00834 Mifepristone
DB00764 Mometasone
DB05423 ORG-34517
DB01384 Paramethasone
DB01130 Prednicarbate
DB00860 Prednisolone
DB00635 Prednisone
DB00896 Rimexolone
DB00421 Spironolactone
DB00620 Triamcinolone
DB08867 Ulipristal
DB00596 Ulobetasol
GuidetoPHARMACOLOGYi625

Polymorphism and mutation databases

BioMutaiNR3C1
DMDMi121069

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000199371 – 777Glucocorticoid receptorAdd BLAST777

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphothreonineCombined sources1
Modified residuei23Omega-N-methylarginineBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei113PhosphoserineBy similarity1
Modified residuei134PhosphoserineCombined sources1
Modified residuei141PhosphoserineBy similarity1
Modified residuei203PhosphoserineCombined sources3 Publications1
Modified residuei211Phosphoserine3 Publications1
Modified residuei226PhosphoserineCombined sources1 Publication1
Cross-linki258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei267PhosphoserineCombined sources1
Cross-linki277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei404Phosphoserine; by GSK3-beta1 Publication1
Cross-linki419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei480N6-acetyllysine1 Publication1
Modified residuei492N6-acetyllysine1 Publication1
Modified residuei494N6-acetyllysine1 Publication1
Modified residuei495N6-acetyllysine1 Publication1
Cross-linki703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Isoform Alpha-B (identifier: P04150-8)
Modified residuei1N-acetylmethionineCombined sources1
Isoform Beta-B (identifier: P04150-9)
Modified residuei1N-acetylmethionineCombined sources1 Publication1

Post-translational modificationi

Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity.2 Publications
Increased proteasome-mediated degradation in response to glucocorticoids (PubMed:11555652). Isoform Alpha-B appears to be more susceptible to proteolytic degradation than isoform Alpha (PubMed:11435610).2 Publications
Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203, Ser-226 and Ser-404-phosphorylated forms are mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear (PubMed:12000743, PubMed:18838540). Phosphorylation at Ser-211 increases transcriptional activity (PubMed:12000743, PubMed:18483179). Phosphorylation at Ser-203, Ser-226 and Ser-404 decreases signaling capacity (PubMed:12000743, PubMed:18483179, PubMed:18838540). Phosphorylation at Ser-404 may protect from glucocorticoid-induced apoptosis (PubMed:18838540). Phosphorylation at Ser-203 and Ser-211 is not required in regulation of chromosome segregation (PubMed:25847991). May be dephosphorylated by PPP5C, attenuates NR3C1 action (By similarity).By similarity4 Publications
Sumoylation at Lys-277 and Lys-293 negatively regulates its transcriptional activity (PubMed:12144530). Sumoylation at Lys-703 positively regulates its transcriptional activity in the presence of RWDD3 (By similarity). Sumoylation at Lys-277 and Lys-293 is dispensable whereas sumoylation at Lys-703 is critical for the stimulatory effect of RWDD3 on its transcriptional activity (By similarity). Heat shock increases sumoylation in a RWDD3-dependent manner (By similarity).By similarity1 Publication
Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP04150
PaxDbiP04150
PeptideAtlasiP04150
PRIDEiP04150
ProteomicsDBi51657
51658 [P04150-10]
51659 [P04150-2]
51660 [P04150-3]
51661 [P04150-5]
51662 [P04150-6]
51663 [P04150-7]
51664 [P04150-8]
51665 [P04150-9]

PTM databases

iPTMnetiP04150
PhosphoSitePlusiP04150

Expressioni

Tissue specificityi

Widely expressed including bone, stomach, lung, liver, colon, breast, ovary, pancreas and kidney (PubMed:25847991). In the heart, detected in left and right atria, left and right ventricles, aorta, apex, intraventricular septum, and atrioventricular node as well as whole adult and fetal heart (PubMed:10902803). Isoform Beta: Widely expressed including brain, bone marrow, thymus, spleen, liver, kidney, pancreas, lung, fat, skeletal muscle, heart, placenta and blood leukocytes (PubMed:7769088, PubMed:8621628). Isoform Alpha-2: Expressed at low level.4 Publications

Inductioni

Isoform Alpha: Up-regulated by TNF (at protein level). Isoform Beta: Up-regulated by TNF and becomes the predominant isoform which may lead to glucocorticoid resistance (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000113580
CleanExiHS_NR3C1
ExpressionAtlasiP04150 baseline and differential
GenevisibleiP04150 HS

Organism-specific databases

HPAiCAB010435
HPA004248

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:21730050). Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes its place, thereby linking the complex to dynein and mediating transport to the nucleus, where the complex dissociates (By similarity). 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 (PubMed:29127155). Directly interacts with UNC45A (PubMed:16478993). Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers (By similarity). Interacts with NRIP1, POU2F1, POU2F2 and TRIM28 (By similarity). Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6 (PubMed:10866662, PubMed:12151000, PubMed:12686538, PubMed:9154805, PubMed:9590696). Interaction with BAG1 inhibits transactivation (PubMed:10477749). Interacts with HEXIM1, PELP1 and TGFB1I1 (PubMed:12415108, PubMed:15211577, PubMed:15941832). Interacts with NCOA1 (PubMed:9590696). Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1 (By similarity). Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion (PubMed:19141540, PubMed:21980503, PubMed:22170608). Interacts with CIART (By similarity). Interacts with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity). Interacts with GRIP1 (PubMed:15769988, PubMed:17635946). Interacts with NR4A3 (via nuclear receptor DNA-binding domain), represses transcription activity of NR4A3 on the POMC promoter Nur response element (NurRE) (PubMed:15591535). Directly interacts with PNRC2 to attract and form a complex with UPF1 and DCP1A; the interaction leads to rapid mRNA degradation (PubMed:25775514). Interacts with GSK3B (PubMed:18838540). Interacts with FNIP1 and FNIP2 (PubMed:27353360). Interacts (via C-terminus) with HNRNPU (via C-terminus) (PubMed:9353307).By similarity22 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • Hsp90 protein binding Source: UniProtKB
  • protein kinase binding Source: ARUK-UCL
  • SUMO binding Source: CAFA
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109165, 225 interactors
CORUMiP04150
DIPiDIP-576N
ELMiP04150
IntActiP04150, 77 interactors
MINTiP04150
STRINGi9606.ENSP00000231509

Chemistry databases

BindingDBiP04150

Structurei

Secondary structure

1777
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni422 – 424Combined sources3
Beta strandi430 – 432Combined sources3
Beta strandi435 – 437Combined sources3
Helixi439 – 450Combined sources12
Beta strandi458 – 461Combined sources4
Turni467 – 472Combined sources6
Helixi474 – 484Combined sources11
Turni525 – 527Combined sources3
Helixi532 – 538Combined sources7
Beta strandi550 – 552Combined sources3
Helixi556 – 579Combined sources24
Helixi584 – 586Combined sources3
Helixi589 – 615Combined sources27
Beta strandi617 – 619Combined sources3
Beta strandi621 – 624Combined sources4
Beta strandi627 – 629Combined sources3
Helixi631 – 634Combined sources4
Helixi639 – 655Combined sources17
Helixi660 – 671Combined sources12
Beta strandi673 – 675Combined sources3
Helixi683 – 702Combined sources20
Beta strandi704 – 706Combined sources3
Helixi708 – 741Combined sources34
Helixi743 – 745Combined sources3
Helixi751 – 765Combined sources15
Beta strandi769 – 771Combined sources3

3D structure databases

DisProtiDP00030
ProteinModelPortaliP04150
SMRiP04150
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04150

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini524 – 758NR LBDPROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 420ModulatingAdd BLAST420
Regioni98 – 115Required for high transcriptional activity of isoform Alpha-C31 PublicationAdd BLAST18
Regioni485 – 777Interaction with CLOCKAdd BLAST293
Regioni487 – 523HingeAdd BLAST37
Regioni532 – 697Interaction with CRY11 PublicationAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi399 – 418Glu/Pro/Ser/Thr-rich (PEST region)Add BLAST20

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain (PubMed:3841189). The ligand-binding domain is required for correct chromosome segregation during mitosis although ligand binding is not required (PubMed:25847991).2 Publications

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri421 – 441NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri457 – 476NR C4-typePROSITE-ProRule annotationAdd BLAST20

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00760000118887
HOGENOMiHOG000037950
HOVERGENiHBG007583
InParanoidiP04150
KOiK05771
OMAiQSTFDIL
PhylomeDBiP04150
TreeFamiTF106510

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF02155 GCR, 1 hit
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR00528 GLCORTICOIDR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (16)i

Sequence statusi: Complete.

This entry describes 16 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform Alpha (identifier: P04150-1) [UniParc]FASTAAdd to basket
Also known as: Alpha-A, GR-alphaA

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
MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV 
        60         70         80         90        100
ASQSDSKQRR LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN 
       110        120        130        140        150
DLGFPQQGQI SLSSGETDLK LLEESIANLN RSTSVPENPK SSASTAVSAA 
       160        170        180        190        200
PTEKEFPKTH SDVSSEQQHL KGQTGTNGGN VKLYTTDQST FDILQDLEFS 
       210        220        230        240        250
SGSPGKETNE SPWRSDLLID ENCLLSPLAG EDDSFLLEGN SNEDCKPLIL 
       260        270        280        290        300
PDTKPKIKDN GDLVLSSPSN VTLPQVKTEK EDFIELCTPG VIKQEKLGTV 
       310        320        330        340        350
YCQASFPGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI 
       360        370        380        390        400
FNVIPPIPVG SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP 
       410        420        430        440        450
DVSSPPSSSS TATTGPPPKL CLVCSDEASG CHYGVLTCGS CKVFFKRAVE 
       460        470        480        490        500
GQHNYLCAGR NDCIIDKIRR KNCPACRYRK CLQAGMNLEA RKTKKKIKGI 
       510        520        530        540        550
QQATTGVSQE TSENPGNKTI VPATLPQLTP TLVSLLEVIE PEVLYAGYDS 
       560        570        580        590        600
SVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW 
       610        620        630        640        650
MFLMAFALGW RSYRQSSANL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS 
       660        670        680        690        700
SELHRLQVSY EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA 
       710        720        730        740        750
IVKREGNSSQ NWQRFYQLTK LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP 
       760        770 
EMLAEIITNQ IPKYSNGNIK KLLFHQK
Note: Predominant physiological form.1 Publication
Length:777
Mass (Da):85,659
Last modified:November 1, 1986 - v1
Checksum:iC5C90C9A5DD16AAB
GO
Isoform Beta (identifier: P04150-2) [UniParc]FASTAAdd to basket
Also known as: Beta-A

The sequence of this isoform differs from the canonical sequence as follows:
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI

Show »
Length:742
Mass (Da):81,509
Checksum:iE2D1F6EA0EE14704
GO
Isoform Alpha-2 (identifier: P04150-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     451-451: G → GR

Note: Due to a partial intron retention.
Show »
Length:778
Mass (Da):85,815
Checksum:i23048D99B60B169C
GO
Isoform Beta-2 (identifier: P04150-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     451-451: G → GR
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI

Note: Due to a partial intron retention.
Show »
Length:743
Mass (Da):81,666
Checksum:i329BE98BCC1DC0E5
GO
Isoform GR-A alpha (identifier: P04150-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-674: Missing.

Note: Lacks exons 5, 6 and 7. Found in glucocorticoid-resistant myeloma patients.1 Publication
Show »
Length:593
Mass (Da):64,752
Checksum:i8CB72DE6B0593EFD
GO
Isoform GR-A beta (identifier: P04150-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-674: Missing.
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI

Note: Lacks exons 5, 6 and 7.1 Publication
Show »
Length:558
Mass (Da):60,602
Checksum:i7C1C30CD84689FBE
GO
Isoform GR-P (identifier: P04150-4)
Sequence is not available
Note: Encoded by exons 2-7 plus several basepairs from the subsequent intron region. Lacks the ligand binding domain. Accounts for up to 10-20% of mRNAs.1 Publication
Length:–
Mass (Da):–
Isoform Alpha-B (identifier: P04150-8) [UniParc]FASTAAdd to basket
Also known as: GR-alphaB

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.

Note: Produced by alternative initiation at Met-27 of isoform Alpha.Combined sources
Show »
Length:751
Mass (Da):82,845
Checksum:iC6D7A2D88B4025C1
GO
Isoform Beta-B (identifier: P04150-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     728-777: VVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK → NVMWLKPESTSHTLI

Note: Produced by alternative initiation at Met-27 of isoform Beta.Combined sources1 Publication
Show »
Length:716
Mass (Da):78,695
Checksum:iBCF1D97EFD06AB74
GO
Isoform 10 (identifier: P04150-10) [UniParc]FASTAAdd to basket
Also known as: hGRDelta313-338

The sequence of this isoform differs from the canonical sequence as follows:
     313-338: Missing.

Show »
Length:751
Mass (Da):82,904
Checksum:i39C4B6A962632545
GO
Isoform Alpha-C1 (identifier: P04150-11) [UniParc]FASTAAdd to basket
Also known as: GR-alphaC1

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: Produced by alternative initiation at Met-86 of isoform Alpha.1 Publication
Show »
Length:692
Mass (Da):76,650
Checksum:iF73B43BE6F312683
GO
Isoform Alpha-C2 (identifier: P04150-12) [UniParc]FASTAAdd to basket
Also known as: GR-alphaC2

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: Produced by alternative initiation at Met-90 of isoform Alpha.1 Publication
Show »
Length:688
Mass (Da):76,186
Checksum:i7A51C90C4FAC4A95
GO
Isoform Alpha-C3 (identifier: P04150-13) [UniParc]FASTAAdd to basket
Also known as: GR-alphaC3

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Note: Produced by alternative initiation at Met-98 of isoform Alpha.1 Publication
Show »
Length:680
Mass (Da):75,310
Checksum:iF56474496CCAB832
GO
Isoform Alpha-D1 (identifier: P04150-14) [UniParc]FASTAAdd to basket
Also known as: GR-alphaD1

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Note: Produced by alternative initiation at Met-316 of isoform Alpha.1 Publication
Show »
Length:462
Mass (Da):51,912
Checksum:i25B86AA2128DA764
GO
Isoform Alpha-D2 (identifier: P04150-15) [UniParc]FASTAAdd to basket
Also known as: GR-alphaD2

The sequence of this isoform differs from the canonical sequence as follows:
     1-330: Missing.

Note: Produced by alternative initiation at Met-331 of isoform Alpha.1 Publication
Show »
Length:447
Mass (Da):50,512
Checksum:i5FD4D80AFE4572D1
GO
Isoform Alpha-D3 (identifier: P04150-16) [UniParc]FASTAAdd to basket
Also known as: GR-alphaD3

The sequence of this isoform differs from the canonical sequence as follows:
     1-335: Missing.

Note: Produced by alternative initiation at Met-336 of isoform Alpha.1 Publication
Show »
Length:442
Mass (Da):49,802
Checksum:iFE52994682DE7E41
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti399R → G in BAD97314 (Ref. 7) Curated1
Sequence conflicti754A → T in BAD97314 (Ref. 7) Curated1

Polymorphismi

Carriers of the 22-Glu-Lys-23 allele are relatively more resistant to the effects of GCs with respect to the sensitivity of the adrenal feedback mechanism than non-carriers, resulting in a better metabolic health profile. Carriers have a better survival than non-carriers, as well as lower serum CRP levels. The 22-Glu-Lys-23 polymorphism is associated with a sex-specific, beneficial body composition at young-adult age, as well as greater muscle strength in males.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01414023R → K Polymorphism; reduces transactivation activity; does not affect transrepression activity. 8 PublicationsCorresponds to variant dbSNP:rs6190EnsemblClinVar.1
Natural variantiVAR_01562829F → L1 PublicationCorresponds to variant dbSNP:rs148102613Ensembl.1
Natural variantiVAR_01462265F → V2 PublicationsCorresponds to variant dbSNP:rs6192Ensembl.1
Natural variantiVAR_07579772N → D Polymorphism; associated in cis with A-321 and S-766 in one individual; doubles transactivation potential. 1 Publication1
Natural variantiVAR_015629112L → F1 PublicationCorresponds to variant dbSNP:rs542110718Ensembl.1
Natural variantiVAR_015630233D → N1 Publication1
Natural variantiVAR_075798321V → A Polymorphism; associated in cis with D-72 and S-766 in one individual; doubles transactivation potential. 1 Publication1
Natural variantiVAR_004675363N → S Enhances transactivation activity; does not affect transrepression activity; may increase sensitivity to exogenously administered glucocorticoids; may contribute to central obesity in men and show lack of association with other risk factors for coronary heart disease and diabetes mellitus. 6 PublicationsCorresponds to variant dbSNP:rs56149945EnsemblClinVar.1
Natural variantiVAR_015631421C → Y1 Publication1
Natural variantiVAR_075799423V → A in GCCR; unknown pathological significance; reduces transactivation activity; delays nuclear translocation; does not exert a dominant negative effect; impairs DNA binding. 1 Publication1
Natural variantiVAR_013472477R → H in GCCR. 1 PublicationCorresponds to variant dbSNP:rs104893913EnsemblClinVar.1
Natural variantiVAR_077143477R → S in GCCR; loss of DNA-binding and of transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type. 1 Publication1
Natural variantiVAR_077144478Y → C in GCCR; decreased DNA-binding and transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type. 1 Publication1
Natural variantiVAR_075800556T → I in GCCR; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding. 2 Publications1
Natural variantiVAR_015632559I → N in GCCR; interferes with translocation to the nucleus and thereby strongly reduces transcription activation; is equally impaired in nuclear export; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893909EnsemblClinVar.1
Natural variantiVAR_025014571V → A in pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor. 1 PublicationCorresponds to variant dbSNP:rs104893911EnsemblClinVar.1
Natural variantiVAR_075801575V → G in GCCR; unknown pathological significance; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding. 1 Publication1
Natural variantiVAR_004676641D → V in GCCR. 1 PublicationCorresponds to variant dbSNP:rs104893908EnsemblClinVar.1
Natural variantiVAR_077145672L → P in GCCR; loss of dexamethasone-binding, dexamethasone-induced translocation to the nucleus and of transactivation activity. 1 Publication1
Natural variantiVAR_013473679G → S in GCCR; has 50% binding affinity. 1 PublicationCorresponds to variant dbSNP:rs104893914EnsemblClinVar.1
Natural variantiVAR_075802714R → Q in GCCR; unknown pathological significance; reduces transactivation; reduces affinity for ligand; exerts a dominant negative effect; does not impair DNA binding. 1 Publication1
Natural variantiVAR_075803726H → R in GCCR; unknown pathological significance; reduces transactivation and transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not impair DNA binding. 1 Publication1
Natural variantiVAR_004677729V → I in GCCR. 1 PublicationCorresponds to variant dbSNP:rs1027058734Ensembl.1
Natural variantiVAR_071935737F → L in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs121909727EnsemblClinVar.1
Natural variantiVAR_015633747I → M in GCCR; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893910EnsemblClinVar.1
Natural variantiVAR_004678753L → F2 PublicationsCorresponds to variant dbSNP:rs121909726EnsemblClinVar.1
Natural variantiVAR_075804766N → S Polymorphism; associated in cis with D-72 and A-321 in one individual; doubles transactivation potential. 1 Publication1
Natural variantiVAR_071936773L → P in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant. 1 PublicationCorresponds to variant dbSNP:rs104893912EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0583121 – 335Missing in isoform Alpha-D3. 1 PublicationAdd BLAST335
Alternative sequenceiVSP_0583131 – 330Missing in isoform Alpha-D2. 1 PublicationAdd BLAST330
Alternative sequenceiVSP_0583141 – 315Missing in isoform Alpha-D1. 1 PublicationAdd BLAST315
Alternative sequenceiVSP_0583151 – 97Missing in isoform Alpha-C3. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_0583161 – 89Missing in isoform Alpha-C2. 1 PublicationAdd BLAST89
Alternative sequenceiVSP_0583171 – 85Missing in isoform Alpha-C1. 1 PublicationAdd BLAST85
Alternative sequenceiVSP_0187731 – 26Missing in isoform Alpha-B and isoform Beta-B. CuratedAdd BLAST26
Alternative sequenceiVSP_043908313 – 338Missing in isoform 10. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_007363451G → GR in isoform Alpha-2 and isoform Beta-2. 1 Publication1
Alternative sequenceiVSP_013340491 – 674Missing in isoform GR-A alpha and isoform GR-A beta. CuratedAdd BLAST184
Alternative sequenceiVSP_003703728 – 777VVENL…LFHQK → NVMWLKPESTSHTLI in isoform Beta, isoform Beta-B, isoform Beta-2 and isoform GR-A beta. 1 PublicationAdd BLAST50

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03225 mRNA Translation: CAA26976.1
X03348 mRNA Translation: CAA27054.1
AH005496 Genomic DNA Translation: AAB64353.1
AH005496 Genomic DNA Translation: AAB64354.1
HQ205546 Genomic DNA Translation: ADP91135.1
HQ205547 Genomic DNA Translation: ADP91138.1
HQ205548 Genomic DNA Translation: ADP91141.1
HQ205549 Genomic DNA Translation: ADP91144.1
HQ205550 Genomic DNA Translation: ADP91147.1
HQ205551 Genomic DNA Translation: ADP91150.1
HQ205552 Genomic DNA Translation: ADP91153.1
HQ205553 Genomic DNA Translation: ADP91156.1
HQ205554 Genomic DNA Translation: ADP91159.1
HQ205555 Genomic DNA Translation: ADP91162.1
HQ205556 Genomic DNA Translation: ADP91165.1
HQ205557 Genomic DNA Translation: ADP91168.1
HQ205558 Genomic DNA Translation: ADP91171.1
HQ205559 Genomic DNA Translation: ADP91174.1
HQ205560 Genomic DNA Translation: ADP91177.1
HQ205561 Genomic DNA Translation: ADP91180.1
HQ205562 Genomic DNA Translation: ADP91183.1
HQ205563 Genomic DNA Translation: ADP91186.1
HQ205564 Genomic DNA Translation: ADP91189.1
HQ205565 Genomic DNA Translation: ADP91192.1
HQ205566 Genomic DNA Translation: ADP91195.1
HQ205567 Genomic DNA Translation: ADP91198.1
HQ205568 Genomic DNA Translation: ADP91201.1
HQ205569 Genomic DNA Translation: ADP91204.1
HQ205570 Genomic DNA Translation: ADP91207.1
HQ205571 Genomic DNA Translation: ADP91210.1
HQ205572 Genomic DNA Translation: ADP91213.1
HQ205573 Genomic DNA Translation: ADP91216.1
HQ205574 Genomic DNA Translation: ADP91219.1
HQ205575 Genomic DNA Translation: ADP91222.1
HQ205576 Genomic DNA Translation: ADP91225.1
HQ205577 Genomic DNA Translation: ADP91228.1
HQ205578 Genomic DNA Translation: ADP91231.1
HQ205579 Genomic DNA Translation: ADP91234.1
HQ205580 Genomic DNA Translation: ADP91237.1
HQ205581 Genomic DNA Translation: ADP91240.1
HQ205582 Genomic DNA Translation: ADP91243.1
HQ205583 Genomic DNA Translation: ADP91246.1
HQ205584 Genomic DNA Translation: ADP91249.1
HQ205585 Genomic DNA Translation: ADP91252.1
AM183262 mRNA Translation: CAJ65924.1
HQ450643 mRNA Translation: AED99114.1
U01351 mRNA Translation: AAA16603.1
AK223594 mRNA Translation: BAD97314.1
BX640610 mRNA Translation: CAE45716.1
AY436590 Genomic DNA Translation: AAQ97180.1
EU332858 Genomic DNA Translation: ABY87547.1
AC005601 Genomic DNA Translation: AAC34207.1
AC004782 Genomic DNA No translation available.
AC091925 Genomic DNA No translation available.
CH471062 Genomic DNA Translation: EAW61872.1
CH471062 Genomic DNA Translation: EAW61873.1
BC015610 mRNA Translation: AAH15610.1
M69104 Genomic DNA Translation: AAA88049.1
AH002750 Genomic DNA Translation: AAA53151.1
S68378 Genomic DNA Translation: AAB20466.1
CCDSiCCDS34258.1 [P04150-3]
CCDS4278.1 [P04150-1]
CCDS47298.1 [P04150-2]
PIRiA93370 QRHUGA
B93370 QRHUGB
RefSeqiNP_000167.1, NM_000176.2 [P04150-1]
NP_001018084.1, NM_001018074.1 [P04150-1]
NP_001018085.1, NM_001018075.1 [P04150-1]
NP_001018086.1, NM_001018076.1 [P04150-1]
NP_001018087.1, NM_001018077.1 [P04150-1]
NP_001018661.1, NM_001020825.1 [P04150-2]
NP_001019265.1, NM_001024094.1 [P04150-3]
NP_001191187.1, NM_001204258.1 [P04150-8]
NP_001191188.1, NM_001204259.1 [P04150-11]
NP_001191189.1, NM_001204260.1 [P04150-12]
NP_001191190.1, NM_001204261.1 [P04150-13]
NP_001191191.1, NM_001204262.1 [P04150-14]
NP_001191192.1, NM_001204263.1 [P04150-15]
NP_001191193.1, NM_001204264.1 [P04150-16]
XP_005268476.1, XM_005268419.3 [P04150-3]