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P04150

- GCR_HUMAN

UniProt

P04150 - GCR_HUMAN

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Protein
Glucocorticoid receptor
Gene
NR3C1, GRL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi421 – 48666Nuclear receptor
Add
BLAST
Zinc fingeri421 – 44121NR C4-type
Add
BLAST
Zinc fingeri457 – 48125NR C4-type
Add
BLAST

GO - Molecular functioni

  1. glucocorticoid receptor activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. sequence-specific DNA binding Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc
  5. steroid binding Source: UniProtKB-KW
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. adrenal gland development Source: Ensembl
  2. chromatin modification Source: UniProtKB-KW
  3. gene expression Source: Reactome
  4. glucocorticoid metabolic process Source: Ensembl
  5. mammary gland duct morphogenesis Source: Ensembl
  6. positive regulation of neuron apoptotic process Source: Ensembl
  7. regulation of glucocorticoid biosynthetic process Source: Ensembl
  8. regulation of gluconeogenesis Source: Ensembl
  9. regulation of transcription, DNA-templated Source: UniProtKB
  10. signal transduction Source: ProtInc
  11. transcription from RNA polymerase II promoter Source: ProtInc
  12. transcription initiation from RNA polymerase II promoter Source: Reactome
  13. transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP04150.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7978. NR3C1.

Subcellular locationi

Cytoplasm. Mitochondrion. Nucleus
Note: Cytoplasmic in the absence of ligand, nuclear after ligand-binding.2 Publications
Isoform Beta : Nucleus
Note: Localized largely in the nucleus.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Ensembl
  3. membrane Source: Ensembl
  4. mitochondrial matrix Source: ProtInc
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Glucocorticoid resistance (GCRES) [MIM:138040]: Hypertensive, hyperandrogenic disorder characterized by increased serum cortisol concentrations. Inheritance is autosomal dominant.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti477 – 4771R → H in GCRES. 1 Publication
VAR_013472
Natural varianti559 – 5591I → N in GCRES; interferes with translocation to the nucleus and thereby strongly reduces transcription activation. Is equally impaired in nuclear export. Acts as dominant negative mutant. 1 Publication
VAR_015632
Natural varianti641 – 6411D → V in GCRES. 1 Publication
VAR_004676
Natural varianti679 – 6791G → S in GCRES; has 50% binding affinity. 1 Publication
VAR_013473
Natural varianti729 – 7291V → I in GCRES. 1 Publication
VAR_004677
Natural varianti747 – 7471I → M in GCRES; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. 1 Publication
VAR_015633

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → T: Abolishes expression of A-type isoforms. 1 Publication
Mutagenesisi27 – 271M → T: Abolishes expression of B-type isoforms. 1 Publication
Mutagenesisi191 – 1911F → D: Reduces transactivation by the ADA complex. 1 Publication
Mutagenesisi193 – 1931I → D: Reduces transactivation by the ADA complex. 1 Publication
Mutagenesisi194 – 1941L → A: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225. 1 Publication
Mutagenesisi197 – 1971L → E: Reduces transactivation by the ADA complex. 1 Publication
Mutagenesisi213 – 2131W → A: Strongly reduces transactivation by the ADA complex. 1 Publication
Mutagenesisi224 – 2241L → V: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225. 1 Publication
Mutagenesisi225 – 2251L → F: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224. 1 Publication
Mutagenesisi235 – 2351F → L: Strongly reduces transactivation by the ADA complex; when associated with V-236. 1 Publication
Mutagenesisi236 – 2361L → V: Strongly reduces transactivation by the ADA complex; when associated with L-235. 1 Publication
Mutagenesisi277 – 2771K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293. 1 Publication
Mutagenesisi293 – 2931K → R: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277. 1 Publication
Mutagenesisi480 – 4801K → 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 Publication
Mutagenesisi492 – 4921K → 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 Publication
Mutagenesisi494 – 4941K → 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 Publication
Mutagenesisi495 – 4951K → 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 Publication
Mutagenesisi585 – 5851R → A: Reduces activation mediated by ligand binding domain; when associated with A-590. 1 Publication
Mutagenesisi590 – 5901D → A: Reduces activation mediated by ligand binding domain; when associated with A-585. 1 Publication
Mutagenesisi602 – 6021F → S: Increases solubility. No effect on transactivation by dexamethasone. 1 Publication
Mutagenesisi625 – 6251P → A: Decreases transactivation by dexamethasone by 95%. 1 Publication
Mutagenesisi628 – 6281I → A: Decreases dimerization and transactivation by dexamethasone; when associated with S-602. 1 Publication
Mutagenesisi703 – 7031K → R: Slightly reduces sumoylation. 1 Publication

Keywords - Diseasei

Disease mutation, Pseudohermaphroditism

Organism-specific databases

MIMi138040. gene+phenotype.
Orphaneti786. Glucocorticoid resistance.
PharmGKBiPA181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 777777Glucocorticoid receptor
PRO_0000019937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphoserine By similarity
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei141 – 1411Phosphoserine By similarity
Modified residuei203 – 2031Phosphoserine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei226 – 2261Phosphoserine By similarity
Modified residuei267 – 2671Phosphoserine1 Publication
Cross-linki277 – 277Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki419 – 419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Inferred
Modified residuei480 – 4801N6-acetyllysine1 Publication
Modified residuei492 – 4921N6-acetyllysine1 Publication
Modified residuei494 – 4941N6-acetyllysine1 Publication
Modified residuei495 – 4951N6-acetyllysine1 Publication

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.
Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203-phosphorylated form is mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear. Transcriptional activity correlates with the amount of phosphorylation at Ser-211. May be dephosphorylated by PPP5C, attenuates NR3C1 action.1 Publication
Sumoylated; this reduces transcription transactivation.1 Publication
Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP04150.
PaxDbiP04150.
PRIDEiP04150.

PTM databases

PhosphoSiteiP04150.

Expressioni

Tissue specificityi

Widely expressed. 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.1 Publication

Gene expression databases

ArrayExpressiP04150.
BgeeiP04150.
CleanExiHS_NR3C1.
GenevestigatoriP04150.

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. Upon ligand binding FKBP5 dissociates from the complex and FKBP4 takes its place, thereby linking the complex to dynein and mediating transport to the nucleus, where the complex dissociates. Directly interacts with UNC45A. Binds to DNA as a homodimer, and as heterodimer with NR3C2 or the retinoid X receptor. Binds STAT5A and STAT5B homodimers and heterodimers. Interacts with NRIP1, POU2F1, POU2F2 and TRIM28. Interacts with several coactivator complexes, including the SMARCA4 complex, CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as NCOA2 and NCOA6. Interaction with BAG1 inhibits transactivation. Interacts with HEXIM1, PELP1 and TGFB1I1. Interacts with NCOA1, NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1. Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion. Interacts with CIART.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317495EBI-493507,EBI-296087
Asxl1P595982EBI-493507,EBI-5743705From a different organism.
CD4P017302EBI-493507,EBI-353826
KIAA0408Q6ZU522EBI-493507,EBI-739493
LCKP062393EBI-493507,EBI-1348
MvpQ626672EBI-493507,EBI-918333From a different organism.
TMF1P820943EBI-493507,EBI-949763

Protein-protein interaction databases

BioGridi109165. 146 interactions.
DIPiDIP-576N.
IntActiP04150. 53 interactions.
MINTiMINT-150603.
STRINGi9606.ENSP00000231509.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni422 – 4243
Beta strandi430 – 4323
Beta strandi435 – 4373
Helixi439 – 44911
Beta strandi458 – 4614
Turni467 – 4726
Helixi474 – 48411
Turni525 – 5273
Helixi532 – 5398
Beta strandi550 – 5523
Helixi556 – 57924
Helixi584 – 5863
Helixi589 – 61527
Beta strandi617 – 6193
Beta strandi621 – 6244
Beta strandi627 – 6293
Helixi633 – 6353
Turni637 – 6393
Helixi640 – 65516
Helixi660 – 67112
Beta strandi673 – 6753
Helixi683 – 70321
Beta strandi704 – 7063
Helixi708 – 7103
Helixi711 – 74131
Turni743 – 7453
Helixi751 – 76616
Beta strandi769 – 7713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2ZX-ray2.50A/D521-777[»]
1NHZX-ray2.30A500-777[»]
1P93X-ray2.70A/B/C/D500-777[»]
3BQDX-ray2.50A525-777[»]
3CLDX-ray2.84A/B521-777[»]
3E7CX-ray2.15A/B521-777[»]
3H52X-ray2.80A/B/C/D528-777[»]
3K22X-ray2.10A/B521-777[»]
3K23X-ray3.00A/B/C521-777[»]
4CSJX-ray2.30A500-777[»]
4HN5X-ray1.90A/B417-506[»]
4HN6X-ray2.55A/B417-506[»]
4LSJX-ray2.35A522-777[»]
4P6WX-ray1.95A526-777[»]
4P6XX-ray2.50A/C/E/G/I/K523-777[»]
DisProtiDP00030.
ProteinModelPortaliP04150.
SMRiP04150. Positions 418-777.

Miscellaneous databases

EvolutionaryTraceiP04150.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 420420Modulating
Add
BLAST
Regioni485 – 777293Interaction with CLOCK
Add
BLAST
Regioni487 – 52741Hinge
Add
BLAST
Regioni528 – 777250Steroid-binding
Add
BLAST
Regioni532 – 697166Interaction with CRY1
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi399 – 41820Glu/Pro/Ser/Thr-rich (PEST region)
Add
BLAST

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.1 Publication

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG270250.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
KOiK05771.
OMAiQSTFDIL.
OrthoDBiEOG7B31M9.
PhylomeDBiP04150.
TreeFamiTF106510.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR001409. Glcrtcd_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02155. GCR. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing and alternative initiation. Align

Note: At least 4 isoforms, Alpha (shown here), Alpha-B, Beta and Beta-B, are produced by alternative initiation at Met-1 and Met-27. The existence of isoform Alpha and isoform Alpha-B has been proved by mutagenesis. As the sequence environment of the 2 potential ATG initiator codons is the same for the other alternatively spliced isoforms, alternative initiation of translation could also occur on these transcripts. Additional isoforms seem to exist.

Isoform Alpha (identifier: P04150-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha-A

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

MDSKESLTPG REENPSSVLA QERGDVMDFY KTLRGGATVK VSASSPSLAV    50
ASQSDSKQRR LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN 100
DLGFPQQGQI SLSSGETDLK LLEESIANLN RSTSVPENPK SSASTAVSAA 150
PTEKEFPKTH SDVSSEQQHL KGQTGTNGGN VKLYTTDQST FDILQDLEFS 200
SGSPGKETNE SPWRSDLLID ENCLLSPLAG EDDSFLLEGN SNEDCKPLIL 250
PDTKPKIKDN GDLVLSSPSN VTLPQVKTEK EDFIELCTPG VIKQEKLGTV 300
YCQASFPGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI 350
FNVIPPIPVG SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP 400
DVSSPPSSSS TATTGPPPKL CLVCSDEASG CHYGVLTCGS CKVFFKRAVE 450
GQHNYLCAGR NDCIIDKIRR KNCPACRYRK CLQAGMNLEA RKTKKKIKGI 500
QQATTGVSQE TSENPGNKTI VPATLPQLTP TLVSLLEVIE PEVLYAGYDS 550
SVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW 600
MFLMAFALGW RSYRQSSANL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS 650
SELHRLQVSY EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA 700
IVKREGNSSQ NWQRFYQLTK LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP 750
EMLAEIITNQ IPKYSNGNIK KLLFHQK 777

Note: Predominant physiological form. Isoform Alpha-B is produced by alternative initiation at Met-27 of isoform Alpha. Both isoforms exhibit similar subcellular location and nuclear translocation after ligand activation. Isoform Alpha-B appears to be more susceptible to degradation, at least when expressed in mammalian cells, but more effective in transcriptional activation and not in transrepression.

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

Note: No hormone-binding activity. Widely expressed at low level.

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. Lower transcriptional activity. Expressed at low level.

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.

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.

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.

Length:
Mass (Da):
Isoform Alpha-B (identifier: P04150-8) [UniParc]FASTAAdd to Basket

Also known as: Beta-B

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. Both isoforms exhibit similar subcellular location and nuclear translocation after ligand activation. Isoform Alpha-B appears to be more susceptible to degradation, at least when expressed in mammalian cells, but more effective in transcriptional activation and not in transrepression.

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.

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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231R → K.7 Publications
Corresponds to variant rs6190 [ dbSNP | Ensembl ].
VAR_014140
Natural varianti29 – 291F → L.1 Publication
VAR_015628
Natural varianti65 – 651F → V.2 Publications
Corresponds to variant rs6192 [ dbSNP | Ensembl ].
VAR_014622
Natural varianti112 – 1121L → F.1 Publication
VAR_015629
Natural varianti233 – 2331D → N.1 Publication
VAR_015630
Natural varianti363 – 3631N → S 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. 5 Publications
Corresponds to variant rs6195 [ dbSNP | Ensembl ].
VAR_004675
Natural varianti421 – 4211C → Y in a glucocorticoid resistant leukemia cell line. 1 Publication
VAR_015631
Natural varianti477 – 4771R → H in GCRES. 1 Publication
VAR_013472
Natural varianti559 – 5591I → N in GCRES; interferes with translocation to the nucleus and thereby strongly reduces transcription activation. Is equally impaired in nuclear export. Acts as dominant negative mutant. 1 Publication
VAR_015632
Natural varianti571 – 5711V → A in pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor. 1 Publication
VAR_025014
Natural varianti641 – 6411D → V in GCRES. 1 Publication
VAR_004676
Natural varianti679 – 6791G → S in GCRES; has 50% binding affinity. 1 Publication
VAR_013473
Natural varianti729 – 7291V → I in GCRES. 1 Publication
VAR_004677
Natural varianti747 – 7471I → M in GCRES; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant. 1 Publication
VAR_015633
Natural varianti753 – 7531L → F in two glucocorticoid resistant leukemia cell lines lacking the normal allele. 2 Publications
VAR_004678

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform Alpha-B and isoform Beta-B.
VSP_018773Add
BLAST
Alternative sequencei313 – 33826Missing in isoform 10.
VSP_043908Add
BLAST
Alternative sequencei451 – 4511G → GR in isoform Alpha-2 and isoform Beta-2.
VSP_007363
Alternative sequencei491 – 674184Missing in isoform GR-A alpha and isoform GR-A beta.
VSP_013340Add
BLAST
Alternative sequencei728 – 77750VVENL…LFHQK → NVMWLKPESTSHTLI in isoform Beta, isoform Beta-B, isoform Beta-2 and isoform GR-A beta.
VSP_003703Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991R → G in BAD97314. 1 Publication
Sequence conflicti754 – 7541A → T in BAD97314. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03225 mRNA. Translation: CAA26976.1.
X03348 mRNA. Translation: CAA27054.1.
U80946
, U78506, U78507, U78508, U78509, U78510, U78511, U78512 Genomic DNA. Translation: AAB64353.1.
U80947
, U78506, U78507, U78508, U78509, U78510, U78511, U78512 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.
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.
NP_001191189.1. NM_001204260.1.
NP_001191190.1. NM_001204261.1.
NP_001191191.1. NM_001204262.1.
NP_001191192.1. NM_001204263.1.
NP_001191193.1. NM_001204264.1.
XP_005268476.1. XM_005268419.2. [P04150-3]
XP_005268477.1. XM_005268420.2. [P04150-3]
XP_005268478.1. XM_005268421.2. [P04150-3]
XP_005268479.1. XM_005268422.2. [P04150-3]
XP_005268480.1. XM_005268423.2. [P04150-3]
UniGeneiHs.122926.

Genome annotation databases

EnsembliENST00000231509; ENSP00000231509; ENSG00000113580. [P04150-3]
ENST00000343796; ENSP00000343205; ENSG00000113580. [P04150-1]
ENST00000394464; ENSP00000377977; ENSG00000113580. [P04150-1]
ENST00000394466; ENSP00000377979; ENSG00000113580. [P04150-3]
ENST00000415690; ENSP00000387672; ENSG00000113580. [P04150-2]
ENST00000424646; ENSP00000405282; ENSG00000113580. [P04150-10]
ENST00000503201; ENSP00000427672; ENSG00000113580. [P04150-1]
ENST00000504572; ENSP00000422518; ENSG00000113580. [P04150-3]
GeneIDi2908.
KEGGihsa:2908.
UCSCiuc003lmz.3. human. [P04150-1]

Polymorphism databases

DMDMi121069.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glucocorticoid receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03225 mRNA. Translation: CAA26976.1 .
X03348 mRNA. Translation: CAA27054.1 .
U80946
, U78506 , U78507 , U78508 , U78509 , U78510 , U78511 , U78512 Genomic DNA. Translation: AAB64353.1 .
U80947
, U78506 , U78507 , U78508 , U78509 , U78510 , U78511 , U78512 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 .
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 .
CCDSi CCDS34258.1. [P04150-3 ]
CCDS4278.1. [P04150-1 ]
CCDS47298.1. [P04150-2 ]
PIRi A93370. QRHUGA.
B93370. QRHUGB.
RefSeqi NP_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.
NP_001191189.1. NM_001204260.1.
NP_001191190.1. NM_001204261.1.
NP_001191191.1. NM_001204262.1.
NP_001191192.1. NM_001204263.1.
NP_001191193.1. NM_001204264.1.
XP_005268476.1. XM_005268419.2. [P04150-3 ]
XP_005268477.1. XM_005268420.2. [P04150-3 ]
XP_005268478.1. XM_005268421.2. [P04150-3 ]
XP_005268479.1. XM_005268422.2. [P04150-3 ]
XP_005268480.1. XM_005268423.2. [P04150-3 ]
UniGenei Hs.122926.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M2Z X-ray 2.50 A/D 521-777 [» ]
1NHZ X-ray 2.30 A 500-777 [» ]
1P93 X-ray 2.70 A/B/C/D 500-777 [» ]
3BQD X-ray 2.50 A 525-777 [» ]
3CLD X-ray 2.84 A/B 521-777 [» ]
3E7C X-ray 2.15 A/B 521-777 [» ]
3H52 X-ray 2.80 A/B/C/D 528-777 [» ]
3K22 X-ray 2.10 A/B 521-777 [» ]
3K23 X-ray 3.00 A/B/C 521-777 [» ]
4CSJ X-ray 2.30 A 500-777 [» ]
4HN5 X-ray 1.90 A/B 417-506 [» ]
4HN6 X-ray 2.55 A/B 417-506 [» ]
4LSJ X-ray 2.35 A 522-777 [» ]
4P6W X-ray 1.95 A 526-777 [» ]
4P6X X-ray 2.50 A/C/E/G/I/K 523-777 [» ]
DisProti DP00030.
ProteinModelPortali P04150.
SMRi P04150. Positions 418-777.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109165. 146 interactions.
DIPi DIP-576N.
IntActi P04150. 53 interactions.
MINTi MINT-150603.
STRINGi 9606.ENSP00000231509.

Chemistry

BindingDBi P04150.
ChEMBLi CHEMBL2034.
DrugBanki DB00288. Amcinonide.
DB00443. Betamethasone.
DB01222. Budesonide.
DB01234. Dexamethasone.
DB00663. Flumethasone Pivalate.
DB00180. Flunisolide.
DB00588. Fluticasone Propionate.
DB00769. Hydrocortamate.
DB00741. Hydrocortisone.
DB00873. Loteprednol Etabonate.
DB00959. Methylprednisolone.
DB00834. Mifepristone.
DB00764. Mometasone.
DB00635. Prednisone.
GuidetoPHARMACOLOGYi 625.

PTM databases

PhosphoSitei P04150.

Polymorphism databases

DMDMi 121069.

Proteomic databases

MaxQBi P04150.
PaxDbi P04150.
PRIDEi P04150.

Protocols and materials databases

DNASUi 2908.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000231509 ; ENSP00000231509 ; ENSG00000113580 . [P04150-3 ]
ENST00000343796 ; ENSP00000343205 ; ENSG00000113580 . [P04150-1 ]
ENST00000394464 ; ENSP00000377977 ; ENSG00000113580 . [P04150-1 ]
ENST00000394466 ; ENSP00000377979 ; ENSG00000113580 . [P04150-3 ]
ENST00000415690 ; ENSP00000387672 ; ENSG00000113580 . [P04150-2 ]
ENST00000424646 ; ENSP00000405282 ; ENSG00000113580 . [P04150-10 ]
ENST00000503201 ; ENSP00000427672 ; ENSG00000113580 . [P04150-1 ]
ENST00000504572 ; ENSP00000422518 ; ENSG00000113580 . [P04150-3 ]
GeneIDi 2908.
KEGGi hsa:2908.
UCSCi uc003lmz.3. human. [P04150-1 ]

Organism-specific databases

CTDi 2908.
GeneCardsi GC05M142639.
HGNCi HGNC:7978. NR3C1.
HPAi CAB010435.
HPA004248.
MIMi 138040. gene+phenotype.
neXtProti NX_P04150.
Orphaneti 786. Glucocorticoid resistance.
PharmGKBi PA181.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270250.
HOGENOMi HOG000037950.
HOVERGENi HBG007583.
KOi K05771.
OMAi QSTFDIL.
OrthoDBi EOG7B31M9.
PhylomeDBi P04150.
TreeFami TF106510.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P04150.

Miscellaneous databases

ChiTaRSi NR3C1. human.
EvolutionaryTracei P04150.
GeneWikii Glucocorticoid_receptor.
GenomeRNAii 2908.
NextBioi 11517.
PROi P04150.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04150.
Bgeei P04150.
CleanExi HS_NR3C1.
Genevestigatori P04150.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR001409. Glcrtcd_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF02155. GCR. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00528. GLCORTICOIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and expression of a functional human glucocorticoid receptor cDNA."
    Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R., Thompson E.B., Rosenfeld M.G., Evans R.M.
    Nature 318:635-641(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    Tissue: Fibroblast.
  2. "The genomic structure of the human glucocorticoid receptor."
    Encio I.J., Detera-Wadleigh S.D.
    J. Biol. Chem. 266:7182-7188(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA AND BETA).
  3. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
    Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
    Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "A new transcript splice variant of the human glucocorticoid receptor: identification and tissue distribution of hGR Delta 313-338, an alternative exon 2 transactivation domain isoform."
    Turner J.D., Schote A.B., Keipes M., Muller C.P.
    Ann. N. Y. Acad. Sci. 1095:334-341(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
  5. "Alternative splicing within the DNA binding domain creates a novel isoform of the human glucocorticoid receptor."
    Munroe D.G., Pang J., Taylor G.R., Lau C., Plante R.K., Zhou L.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
    Tissue: Osteosarcoma.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Kidney.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Uterine endothelium.
  8. NIEHS SNPs program
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-23 AND VAL-65.
  9. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Placenta.
  13. "Purification of a human glucocorticoid receptor gene promoter-binding protein. Production of polyclonal antibodies against the purified factor."
    Leclerc S., Xie B.X., Roy R., Govindan M.V.
    J. Biol. Chem. 266:8711-8719(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
  14. "Human glucocorticoid receptor gene promotor-homologous down regulation."
    Govindan M.V., Pothier F., Leclerc S., Palaniswami R., Xie B.
    J. Steroid Biochem. Mol. Biol. 40:317-323(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
  15. "Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product."
    Weinberger C., Hollenberg S.M., Rosenfeld M.G., Evans R.M.
    Nature 318:670-672(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  16. "Alternatively spliced glucocorticoid receptor messenger RNAs in glucocorticoid-resistant human multiple myeloma cells."
    Moalli P.A., Pillay S., Krett N.L., Rosen S.T.
    Cancer Res. 53:3877-3879(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS GP-P; GP-A ALPHA AND GP-A BETA).
  17. "Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor."
    Henriksson A., Almloef T., Ford J., McEwan I.J., Gustafsson J.-A., Wright A.P.H.
    Mol. Cell. Biol. 17:3065-3073(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TADA2L AND THE ADA COMPLEX, MUTAGENESIS OF PHE-191; ILE-193; LEU-194; LEU-197; TRP-213; LEU-224; LEU-225; PHE-235 AND LEU-236.
  18. "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
    Fryer C.J., Archer T.K.
    Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SMARCA4 COMPLEX; NCOA1; NCOA2 AND THE CREBBP/EP300 COMPLEX.
  19. "A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity."
    Schneikert J., Huebner S., Martin E., Cato A.B.C.
    J. Cell Biol. 146:929-940(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAG1.
  20. "Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing."
    Rivers C., Levy A., Hancock J., Lightman S., Norman M.
    J. Clin. Endocrinol. Metab. 84:4283-4286(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS ALPHA-2 AND BETA-2).
  21. "Steroidogenic enzyme gene expression in the human heart."
    Kayes-Wandover K.M., White P.C.
    J. Clin. Endocrinol. Metab. 85:2519-2525(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  22. "A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
    Mahajan M.A., Samuels H.H.
    Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  23. "Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor."
    Diamond M.I., Robinson M.R., Yamamoto K.R.
    Proc. Natl. Acad. Sci. U.S.A. 97:657-661(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT ON EXPANDED POLYGLUTAMINE PROTEIN.
  24. "Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids."
    Wallace A.D., Cidlowski J.A.
    J. Biol. Chem. 276:42714-42721(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLUCOCORTICOID-MEDIATED DOWN-REGULATION.
  25. "High constitutive glucocorticoid receptor beta in human neutrophils enables them to reduce their spontaneous rate of cell death in response to corticosteroids."
    Strickland I., Kisich K., Hauk P.J., Vottero A., Chrousos G.P., Klemm D.J., Leung D.Y.M.
    J. Exp. Med. 193:585-593(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REDUCTION OF CELL DEATH IN RESPONSE TO CORTICOSTEROIDS.
  26. "Molecular identification and characterization of A and B forms of the glucocorticoid receptor."
    Yudt M.R., Cidlowski J.A.
    Mol. Endocrinol. 15:1093-1103(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION, MUTAGENESIS OF MET-1 AND MET-27.
  27. "Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor."
    Tian S., Poukka H., Palvimo J.J., Jaenne O.A.
    Biochem. J. 367:907-911(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, MUTAGENESIS OF LYS-277; LYS-293 AND LYS-703.
  28. "Deciphering the phosphorylation 'code' of the glucocorticoid receptor in vivo."
    Wang Z., Frederick J., Garabedian M.J.
    J. Biol. Chem. 277:26573-26580(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-203 AND SER-211.
  29. "Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
    Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  30. "The origin and functions of multiple human glucocorticoid receptor isoforms."
    Lu N.Z., Cidlowski J.A.
    Ann. N. Y. Acad. Sci. 1024:102-123(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ALTERNATIVE SPLICING, ALTERNATIVE INITIATION.
  31. "Distinct LIM domains of Hic-5/ARA55 are required for nuclear matrix targeting and glucocorticoid receptor binding and coactivation."
    Guerrero-Santoro J., Yang L., Stallcup M.R., DeFranco D.B.
    J. Cell. Biochem. 92:810-819(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  32. "HEXIM1 forms a transcriptionally abortive complex with glucocorticoid receptor without involving 7SK RNA and positive transcription elongation factor b."
    Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H., Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H.
    Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEXIM1.
  33. "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
    Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.
    Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC45A.
  34. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. "Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications."
    Nader N., Chrousos G.P., Kino T.
    FASEB J. 23:1572-1583(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACETYLATION AT LYS-480; LYS-492; LYS-494 AND LYS-495, MUTAGENESIS OF LYS-480; LYS-492; LYS-494 AND LYS-495, INTERACTION WITH CLOCK.
  38. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  39. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Glucocorticoids induce mitochondrial gene transcription in HepG2 cells: role of the mitochondrial glucocorticoid receptor."
    Psarra A.M., Sekeris C.E.
    Biochim. Biophys. Acta 1813:1814-1821(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  42. "The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress."
    Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.
    J. Biol. Chem. 286:30152-30160(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  43. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
    Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
    Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1 AND CRY2.
  44. "Peripheral CLOCK regulates target-tissue glucocorticoid receptor transcriptional activity in a circadian fashion in man."
    Charmandari E., Chrousos G.P., Lambrou G.I., Pavlaki A., Koide H., Ng S.S., Kino T.
    PLoS ONE 6:E25612-E25612(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, INTERACTION WITH CLOCK.
  45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition."
    Bledsoe R.K., Montana V.G., Stanley T.B., Delves C.J., Apolito C.J., McKee D.D., Consler T.G., Parks D.J., Stewart E.L., Willson T.M., Lambert M.H., Moore J.T., Pearce K.H., Xu H.E.
    Cell 110:93-105(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 521-777 OF MUTANT SER-602 IN COMPLEX WITH NCOA2; DEXAMETHASONE AND RU-486, MUTAGENESIS OF ARG-585; ASP-590; PHE-602; PRO-625 AND ILE-628.
  47. "The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism."
    Kauppi B., Jakob C., Faernegaardh M., Yang J., Ahola H., Alarcon M., Calles K., Engstrom O., Harlan J., Muchmore S., Ramqvist A.-K., Thorell S., Oehman L., Greer J., Gustafsson J.-A., Carlstedt-Duke J., Carlquist M.
    J. Biol. Chem. 278:22748-22754(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 500-777 OF MUTANT SER-602 IN COMPLEX WITH COACTIVATOR PEPTIDE; DEXAMETHASONE AND WITH RU-486.
  48. "Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance."
    Hurley D.M., Accili D., Stratakis C.A., Karl M., Vamvakopoulos N., Rorer E., Constantine K., Taylor S.I., Chrousos G.P.
    J. Clin. Invest. 87:680-686(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GCRES VAL-641.
  49. "Cloning and expression of mutant glucocorticoid receptors from glucocorticoid-sensitive and -resistant human leukemic cells."
    Powers J.H., Hillmann A.G., Tang D.C., Harmon J.M.
    Cancer Res. 53:4059-4065(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYR-421 AND PHE-753.
  50. "Familial glucocorticoid resistance caused by a splice site deletion in the human glucocorticoid receptor gene."
    Karl M., Lamberts S.W.J., Detera-Wadleigh S.D., Encio I.J., Stratakis C.A., Hurley D.M., Accili D., Chrousos G.P.
    J. Clin. Endocrinol. Metab. 76:683-689(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-363.
  51. "A mutation of the glucocorticoid receptor in primary cortisol resistance."
    Malchoff D.M., Brufsky A., Reardon G., McDermott P., Javier E.C., Bergh C.H., Rowe D., Malchoff C.D.
    J. Clin. Invest. 91:1918-1925(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GCRES ILE-729.
  52. "Identification of the activation-labile gene: a single point mutation in the human glucocorticoid receptor presents as two distinct receptor phenotypes."
    Ashraf J., Thompson E.B.
    Mol. Endocrinol. 7:631-642(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHE-753.
  53. "Lack of association between five polymorphisms in the human glucocorticoid receptor gene and glucocorticoid resistance."
    Koper J.W., Stolk R.P., de Lange P., Huizenga N.A.T.M., Molijn G.-J., Pols H.A.P., Grobbee D.E., Karl M., de Jong F.H., Brinkmann A.O., Lamberts S.W.J.
    Hum. Genet. 99:663-668(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LYS-23 AND SER-363.
  54. Cited for: VARIANTS LYS-23; VAL-65 AND SER-363.
  55. "Five missense variants in the amino-terminal domain of the glucocorticoid receptor: no association with puerperal psychosis or schizophrenia."
    Feng J., Zheng J., Bennett W.P., Heston L.L., Jones I.R., Craddock N., Sommer S.S.
    Am. J. Med. Genet. 96:412-417(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LYS-23; LEU-29; PHE-112; ASN-233 AND SER-363.
  56. "Characterization of two novel mutations in the glucocorticoid receptor gene in patients with primary cortisol resistance."
    Ruiz M., Lind U., Gaafvels M., Eggertsen G., Carlstedt-Duke J., Nilsson L., Holtmann M., Stierna P., Wikstroem A.-C., Werner S.
    Clin. Endocrinol. (Oxf.) 55:363-371(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GCRES HIS-477 AND SER-679.
  57. "The N363S polymorphism of the glucocorticoid receptor: potential contribution to central obesity in men and lack of association with other risk factors for coronary heart disease and diabetes mellitus."
    Dobson M.G., Redfern C.P.F., Unwin N., Weaver J.U.
    J. Clin. Endocrinol. Metab. 86:2270-2274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-363.
  58. "Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking."
    Kino T., Stauber R.H., Resau J.H., Pavlakis G.N., Chrousos G.P.
    J. Clin. Endocrinol. Metab. 86:5600-5608(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GCRES ASN-559.
  59. "A polymorphism in the glucocorticoid receptor gene, which decreases sensitivity to glucocorticoids in vivo, is associated with low insulin and cholesterol levels."
    van Rossum E.F.C., Koper J.W., Huizenga N.A.T.M., Uitterlinden A.G., Janssen J.A.M.J.L., Brinkmann A.O., Grobbee D.E., de Jong F.H., van Duyn C.M., Pols H.A.P., Lamberts S.W.J.
    Diabetes 51:3128-3134(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-23.
  60. Cited for: VARIANT PSEUDOHERMAPHRODITISM ALA-571.
  61. "A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators."
    Vottero A., Kino T., Combe H., Lecomte P., Chrousos G.P.
    J. Clin. Endocrinol. Metab. 87:2658-2667(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GCRES MET-747, ALTERED INTERACTION WITH THE COACTIVATOR NCOA2.
  62. "Association of the ER22/23EK polymorphism in the glucocorticoid receptor gene with survival and C-reactive protein levels in elderly men."
    van Rossum E.F.C., Feelders R.A., van den Beld A.W., Uitterlinden A.G., Janssen J.A.M.J.L., Ester W., Brinkmann A.O., Grobbee D.E., de Jong F.H., Pols H.A.P., Koper J.W., Lamberts S.W.J.
    Am. J. Med. 117:158-162(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-23.
  63. "The ER22/23EK polymorphism in the glucocorticoid receptor gene is associated with a beneficial body composition and muscle strength in young adults."
    van Rossum E.F.C., Voorhoeve P.G., te Velde S.J., Koper J.W., Delemarre-van de Waal H.A., Kemper H.C.G., Lamberts S.W.J.
    J. Clin. Endocrinol. Metab. 89:4004-4009(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-23.

Entry informationi

Entry nameiGCR_HUMAN
AccessioniPrimary (citable) accession number: P04150
Secondary accession number(s): A0ZXF9
, B0LPG8, D3DQF4, P04151, Q53EP5, Q6N0A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: September 3, 2014
This is version 208 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

High constitutive expression of isoform Beta by neutrophils may provide a mechanism by which these cells escape glucocorticoid-induced cell death. Up-regulation by proinflammatory cytokines such as IL8 further enhances their survival in the presence of glucocorticoids during inflammation.
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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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