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P08235

- MCR_HUMAN

UniProt

P08235 - MCR_HUMAN

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Protein

Mineralocorticoid receptor

Gene

NR3C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei770 – 7701Steroid
Binding sitei776 – 7761Steroid
Binding sitei817 – 8171Steroid
Binding sitei945 – 9451Steroid

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi603 – 66866Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri603 – 62321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri639 – 66325NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. gene expression Source: Reactome
  2. signal transduction Source: ProtInc
  3. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP08235.

Names & Taxonomyi

Protein namesi
Recommended name:
Mineralocorticoid receptor
Short name:
MR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 2
Gene namesi
Name:NR3C2
Synonyms:MCR, MLR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:7979. NR3C2.

Subcellular locationi

Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein
Note: Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
  3. nucleoplasm Source: Reactome
  4. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pseudohypoaldosteronism 1, autosomal dominant (PHA1A) [MIM:177735]: A salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1A is a mild form characterized by target organ defects confined to kidney. Patients may present with neonatal renal salt wasting with hyperkalaemic acidosis despite high aldosterone levels. These patients improve with age and usually become asymptomatic without treatment.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti633 – 6331G → R in PHA1A; reduces transcription transactivation upon aldosterone binding.
VAR_031268
Natural varianti645 – 6451C → S in PHA1A. 1 Publication
VAR_031269
Natural varianti659 – 6591R → S in PHA1A. 1 Publication
VAR_031270
Natural varianti759 – 7591P → S in PHA1A. 1 Publication
VAR_031271
Natural varianti769 – 7691L → P in PHA1A. 1 Publication
VAR_031272
Natural varianti770 – 7701N → K in PHA1A. 1 Publication
VAR_031273
Natural varianti776 – 7761Q → R in PHA1A; reduces aldosterone binding.
VAR_031274
Natural varianti805 – 8051S → P in PHA1A. 1 Publication
VAR_031275
Natural varianti815 – 8151S → R in PHA1A. 1 Publication
VAR_031276
Natural varianti818 – 8181S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding.
VAR_031277
Natural varianti924 – 9241L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding.
VAR_015627
Natural varianti972 – 9721E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation.
VAR_031278
Natural varianti979 – 9791L → P in PHA1A; loss of aldosterone binding and transcription transactivation.
VAR_031279
Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP) [MIM:605115]: Inheritance is autosomal dominant. The disease is characterized by the onset of severe hypertension before the age of 20, and by suppression of aldosterone secretion.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti810 – 8101S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 1 Publication
Corresponds to variant rs41511344 [ dbSNP | Ensembl ].
VAR_015626

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi767 – 7671S → N: Loss of transcription transactivation. 1 Publication
Mutagenesisi767 – 7671S → Q: Strong decrease of transcription transactivation. 1 Publication
Mutagenesisi770 – 7701N → A, D, H, Q, S or T: Abolishes aldosterone binding and transcription transactivation. 2 Publications
Mutagenesisi776 – 7761Q → A: Reduces aldosterone binding and transcription transactivation. 2 Publications
Mutagenesisi782 – 7821K → E: Decreased coactivator binding. 1 Publication
Mutagenesisi785 – 7851K → E: Loss of coactivator binding. 1 Publication
Mutagenesisi796 – 7961E → R: Decreased coactivator binding. 1 Publication
Mutagenesisi808 – 8081C → S: Increases aldosterone-binding. 1 Publication
Mutagenesisi810 – 8101S → M: Alters receptor specificity. 1 Publication
Mutagenesisi817 – 8171R → A: Reduces aldosterone binding and transcription transactivation. 2 Publications
Mutagenesisi849 – 8491C → S: Strongly decreases affinity for aldosterone and transcription transactivation. 1 Publication
Mutagenesisi942 – 9421C → S: Abolishes steroid binding and transcription transactivation. 1 Publication
Mutagenesisi945 – 9451T → A: Decreases aldosterone-binding and cortisol-binding. 2 Publications
Mutagenesisi952 – 9521L → A: Reduces transcription transactivation. 1 Publication
Mutagenesisi953 – 9531K → A: Slightly reduces aldosterone binding and abolishes transcription transactivation. 1 Publication
Mutagenesisi954 – 9541V → A: Reduces aldosterone binding and abolishes transcription transactivation. 1 Publication
Mutagenesisi956 – 9561F → A: Abolishes aldosterone binding and transcription transactivation. 1 Publication
Mutagenesisi957 – 9571P → A: Slightly reduces aldosterone binding and transcription transactivation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi177735. phenotype.
605115. phenotype.
Orphaneti88660. Pseudohyperaldosteronism type 2.
171871. Renal pseudohypoaldosteronism type 1.
PharmGKBiPA242.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 984984Mineralocorticoid receptorPRO_0000053682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08235.
PaxDbiP08235.
PRIDEiP08235.

PTM databases

PhosphoSiteiP08235.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in distal tubules, convoluted tubules and cortical collecting duct in kidney, and in sweat glands. Detected at lower levels in cardiomyocytes, in epidermis and in colon enterocytes.2 Publications

Gene expression databases

BgeeiP08235.
CleanExiHS_NR3C2.
ExpressionAtlasiP08235. baseline and differential.
GenevestigatoriP08235.

Organism-specific databases

HPAiCAB009155.

Interactioni

Subunit structurei

Heteromultimeric cytoplasmic complex with HSP90, HSP70, and FKBP4, in the absence of ligand. After ligand binding, it translocates to the nucleus and binds to DNA as a homodimer and as a heterodimer with NR3C1. May interact with HSD11B2 in the absence of ligand. Binds the coactivators NCOA1, NCOA2, TIF1 and NRIP1.4 Publications

Protein-protein interaction databases

BioGridi110451. 23 interactions.
IntActiP08235. 4 interactions.
STRINGi9606.ENSP00000350815.

Structurei

Secondary structure

1
984
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi728 – 7336
Helixi738 – 7458
Helixi762 – 78524
Helixi790 – 7923
Helixi795 – 82228
Beta strandi825 – 8306
Beta strandi833 – 8353
Helixi837 – 8426
Helixi846 – 86217
Helixi866 – 87712
Beta strandi879 – 8824
Helixi889 – 90820
Helixi911 – 9133
Helixi917 – 94731
Helixi949 – 9524
Helixi958 – 97215
Beta strandi976 – 9783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9RX-ray1.96A/B731-984[»]
1YA3X-ray2.34A/B/C731-984[»]
2A3IX-ray1.95A732-984[»]
2AA2X-ray1.95A712-984[»]
2AA5X-ray2.20A/B712-984[»]
2AA6X-ray1.95A/B712-984[»]
2AA7X-ray2.20A712-984[»]
2AAXX-ray1.75A/B712-984[»]
2AB2X-ray1.85A/B712-984[»]
2ABIX-ray2.33A/B/C731-984[»]
2OAXX-ray2.29A/B/C/D/E/F731-984[»]
3VHUX-ray2.11A712-984[»]
3VHVX-ray1.35A727-984[»]
3WFFX-ray2.05A712-984[»]
3WFGX-ray1.40A712-984[»]
4TNTX-ray2.39A/B593-671[»]
ProteinModelPortaliP08235.
SMRiP08235. Positions 596-984.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08235.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 602602ModulatingAdd
BLAST
Regioni669 – 73264HingeAdd
BLAST
Regioni733 – 984252Steroid-bindingAdd
BLAST
Regioni782 – 7854Important for coactivator binding

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri603 – 62321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri639 – 66325NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG294115.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000247011.
HOVERGENiHBG006336.
InParanoidiP08235.
KOiK08555.
PhylomeDBiP08235.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00047. 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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P08235-1) [UniParc]FASTAAdd to Basket

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
METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC
60 70 80 90 100
VSGAIPNNST QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT
110 120 130 140 150
VAESMGLYMD SVRDADYSYE QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR
160 170 180 190 200
PSTLSCVNTP LRSFMSDSGS SVNGGVMRAI VKSPIMCHEK SPSVCSPLNM
210 220 230 240 250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN AENRGSRSHS
260 270 280 290 300
PAHASNVGSP LSSPLSSMKS SISSPPSHCS VKSPVSSPNN VTLRSSVSSP
310 320 330 340 350
ANINNSRCSV SSPSNTNNRS TLSSPAASTV GSICSPVNNA FSYTASGTSA
360 370 380 390 400
GSSTLRDVVP SPDTQEKGAQ EVPFPKTEEV ESAISNGVTG QLNIVQYIKP
410 420 430 440 450
EPDGAFSSSC LGGNSKINSD SSFSVPIKQE STKHSCSGTS FKGNPTVNPF
460 470 480 490 500
PFMDGSYFSF MDDKDYYSLS GILGPPVPGF DGNCEGSGFP VGIKQEPDDG
510 520 530 540 550
SYYPEASIPS SAIVGVNSGG QSFHYRIGAQ GTISLSRSAR DQSFQHLSSF
560 570 580 590 600
PPVNTLVESW KSHGDLSSRR SDGYPVLEYI PENVSSSTLR SVSTGSSRPS
610 620 630 640 650
KICLVCGDEA SGCHYGVVTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI
660 670 680 690 700
RRKNCPACRL QKCLQAGMNL GARKSKKLGK LKGIHEEQPQ QQQPPPPPPP
710 720 730 740 750
PQSPEEGTTY IAPAKEPSVN TALVPQLSTI SRALTPSPVM VLENIEPEIV
760 770 780 790 800
YAGYDSSKPD TAENLLSTLN RLAGKQMIQV VKWAKVLPGF KNLPLEDQIT
810 820 830 840 850
LIQYSWMCLS SFALSWRSYK HTNSQFLYFA PDLVFNEEKM HQSAMYELCQ
860 870 880 890 900
GMHQISLQFV RLQLTFEEYT IMKVLLLLST IPKDGLKSQA AFEEMRTNYI
910 920 930 940 950
KELRKMVTKC PNNSGQSWQR FYQLTKLLDS MHDLVSDLLE FCFYTFRESH
960 970 980
ALKVEFPAML VEIISDQLPK VESGNAKPLY FHRK
Length:984
Mass (Da):107,067
Last modified:August 1, 1988 - v1
Checksum:i8300CD1A18C1858A
GO
Isoform 2 (identifier: P08235-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     672-706: ARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEE → ERRCISLPCMNYARGCTKSAFSSFDCSSPLKNTPS
     707-984: Missing.

Note: Lacks steroid-binding activity and acts as ligand-independent transactivator.

Show »
Length:706
Mass (Da):75,052
Checksum:iEEFC58BB02FA0812
GO
Isoform 3 (identifier: P08235-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     633-633: G → GKCSW

Show »
Length:988
Mass (Da):107,572
Checksum:iD6257319E5482C86
GO
Isoform 4 (identifier: P08235-4) [UniParc]FASTAAdd to Basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     672-788: Missing.

Show »
Length:867
Mass (Da):94,359
Checksum:iBEC8DD3A6A855903
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti946 – 9461F → I in AAI11759. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71H → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036063
Natural varianti180 – 1801I → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; increases transcription transactivation at low aldosterone concentrations. 5 Publications
Corresponds to variant rs5522 [ dbSNP | Ensembl ].
VAR_014623
Natural varianti241 – 2411A → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; reduces transcription transactivation upon aldosterone binding. 4 Publications
VAR_015625
Natural varianti444 – 4441N → T.1 Publication
Corresponds to variant rs5523 [ dbSNP | Ensembl ].
VAR_014624
Natural varianti537 – 5371R → Q.1 Publication
Corresponds to variant rs5526 [ dbSNP | Ensembl ].
VAR_014625
Natural varianti554 – 5541N → S.1 Publication
Corresponds to variant rs5527 [ dbSNP | Ensembl ].
VAR_014626
Natural varianti633 – 6331G → R in PHA1A; reduces transcription transactivation upon aldosterone binding.
VAR_031268
Natural varianti645 – 6451C → S in PHA1A. 1 Publication
VAR_031269
Natural varianti659 – 6591R → S in PHA1A. 1 Publication
VAR_031270
Natural varianti759 – 7591P → S in PHA1A. 1 Publication
VAR_031271
Natural varianti769 – 7691L → P in PHA1A. 1 Publication
VAR_031272
Natural varianti770 – 7701N → K in PHA1A. 1 Publication
VAR_031273
Natural varianti776 – 7761Q → R in PHA1A; reduces aldosterone binding.
VAR_031274
Natural varianti805 – 8051S → P in PHA1A. 1 Publication
VAR_031275
Natural varianti810 – 8101S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 1 Publication
Corresponds to variant rs41511344 [ dbSNP | Ensembl ].
VAR_015626
Natural varianti815 – 8151S → R in PHA1A. 1 Publication
VAR_031276
Natural varianti818 – 8181S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding.
VAR_031277
Natural varianti826 – 8261F → Y.
Corresponds to variant rs13306592 [ dbSNP | Ensembl ].
VAR_029311
Natural varianti924 – 9241L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding.
VAR_015627
Natural varianti972 – 9721E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation.
VAR_031278
Natural varianti979 – 9791L → P in PHA1A; loss of aldosterone binding and transcription transactivation.
VAR_031279

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei633 – 6331G → GKCSW in isoform 3. CuratedVSP_007357
Alternative sequencei672 – 788117Missing in isoform 4. 2 PublicationsVSP_007360Add
BLAST
Alternative sequencei672 – 70635ARKSK…QSPEE → ERRCISLPCMNYARGCTKSA FSSFDCSSPLKNTPS in isoform 2. 1 PublicationVSP_007358Add
BLAST
Alternative sequencei707 – 984278Missing in isoform 2. 1 PublicationVSP_007359Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16801 mRNA. Translation: AAA59571.1.
AJ315514 mRNA. Translation: CAC67405.1.
AJ315515 mRNA. Translation: CAC67406.1.
EU326312 Genomic DNA. Translation: ACA05924.1.
EU326312 Genomic DNA. Translation: ACA05925.1.
FJ515829 Genomic DNA. Translation: ACS13716.1.
FJ515829 Genomic DNA. Translation: ACS13717.1.
AC069272 Genomic DNA. No translation available.
AC093678 Genomic DNA. No translation available.
AC093881 Genomic DNA. No translation available.
AC104691 Genomic DNA. No translation available.
AC106899 Genomic DNA. No translation available.
BC111758 mRNA. Translation: AAI11759.1.
AH006913 Genomic DNA. Translation: AAC63513.1.
CCDSiCCDS3772.1. [P08235-1]
CCDS54811.1. [P08235-4]
PIRiA29513.
RefSeqiNP_000892.2. NM_000901.4.
NP_001159576.1. NM_001166104.1.
UniGeneiHs.163924.

Genome annotation databases

EnsembliENST00000511528; ENSP00000421481; ENSG00000151623.
ENST00000512865; ENSP00000423510; ENSG00000151623.
GeneIDi4306.
KEGGihsa:4306.
UCSCiuc003ilk.4. human.

Polymorphism databases

DMDMi126885.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Mineralocorticoid receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16801 mRNA. Translation: AAA59571.1 .
AJ315514 mRNA. Translation: CAC67405.1 .
AJ315515 mRNA. Translation: CAC67406.1 .
EU326312 Genomic DNA. Translation: ACA05924.1 .
EU326312 Genomic DNA. Translation: ACA05925.1 .
FJ515829 Genomic DNA. Translation: ACS13716.1 .
FJ515829 Genomic DNA. Translation: ACS13717.1 .
AC069272 Genomic DNA. No translation available.
AC093678 Genomic DNA. No translation available.
AC093881 Genomic DNA. No translation available.
AC104691 Genomic DNA. No translation available.
AC106899 Genomic DNA. No translation available.
BC111758 mRNA. Translation: AAI11759.1 .
AH006913 Genomic DNA. Translation: AAC63513.1 .
CCDSi CCDS3772.1. [P08235-1 ]
CCDS54811.1. [P08235-4 ]
PIRi A29513.
RefSeqi NP_000892.2. NM_000901.4.
NP_001159576.1. NM_001166104.1.
UniGenei Hs.163924.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y9R X-ray 1.96 A/B 731-984 [» ]
1YA3 X-ray 2.34 A/B/C 731-984 [» ]
2A3I X-ray 1.95 A 732-984 [» ]
2AA2 X-ray 1.95 A 712-984 [» ]
2AA5 X-ray 2.20 A/B 712-984 [» ]
2AA6 X-ray 1.95 A/B 712-984 [» ]
2AA7 X-ray 2.20 A 712-984 [» ]
2AAX X-ray 1.75 A/B 712-984 [» ]
2AB2 X-ray 1.85 A/B 712-984 [» ]
2ABI X-ray 2.33 A/B/C 731-984 [» ]
2OAX X-ray 2.29 A/B/C/D/E/F 731-984 [» ]
3VHU X-ray 2.11 A 712-984 [» ]
3VHV X-ray 1.35 A 727-984 [» ]
3WFF X-ray 2.05 A 712-984 [» ]
3WFG X-ray 1.40 A 712-984 [» ]
4TNT X-ray 2.39 A/B 593-671 [» ]
ProteinModelPortali P08235.
SMRi P08235. Positions 596-984.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110451. 23 interactions.
IntActi P08235. 4 interactions.
STRINGi 9606.ENSP00000350815.

Chemistry

BindingDBi P08235.
ChEMBLi CHEMBL1994.
DrugBanki DB01395. Drospirenone.
DB00700. Eplerenone.
DB01023. Felodipine.
DB00687. Fludrocortisone.
DB00588. Fluticasone Propionate.
DB00393. Nimodipine.
DB00396. Progesterone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi 626.

PTM databases

PhosphoSitei P08235.

Polymorphism databases

DMDMi 126885.

Proteomic databases

MaxQBi P08235.
PaxDbi P08235.
PRIDEi P08235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000511528 ; ENSP00000421481 ; ENSG00000151623 .
ENST00000512865 ; ENSP00000423510 ; ENSG00000151623 .
GeneIDi 4306.
KEGGi hsa:4306.
UCSCi uc003ilk.4. human.

Organism-specific databases

CTDi 4306.
GeneCardsi GC04M148999.
H-InvDB HIX0024570.
HGNCi HGNC:7979. NR3C2.
HPAi CAB009155.
MIMi 177735. phenotype.
600983. gene.
605115. phenotype.
neXtProti NX_P08235.
Orphaneti 88660. Pseudohyperaldosteronism type 2.
171871. Renal pseudohypoaldosteronism type 1.
PharmGKBi PA242.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG294115.
GeneTreei ENSGT00760000118887.
HOGENOMi HOG000247011.
HOVERGENi HBG006336.
InParanoidi P08235.
KOi K08555.
PhylomeDBi P08235.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P08235.

Miscellaneous databases

EvolutionaryTracei P08235.
GeneWikii Mineralocorticoid_receptor.
GenomeRNAii 4306.
NextBioi 16949.
PROi P08235.
SOURCEi Search...

Gene expression databases

Bgeei P08235.
CleanExi HS_NR3C2.
ExpressionAtlasi P08235. baseline and differential.
Genevestigatori P08235.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi 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. "Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor."
    Arriza J.L., Weinberger C., Cerelli G., Glaser T.M., Handelin B.L., Housman D.E., Evans R.M.
    Science 237:268-275(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Kidney.
  2. "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action."
    Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.
    Mol. Endocrinol. 15:1586-1598(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), TISSUE SPECIFICITY, INTERACTION WITH NCOA1; TIF1 AND NRIP1, VARIANTS VAL-180 AND VAL-241.
    Tissue: Heart.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-180 AND VAL-241.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-180 AND VAL-241.
  5. "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 4), VARIANTS VAL-180 AND VAL-241.
  6. "Mutations in the mineralocorticoid receptor gene cause autosomal dominant pseudohypoaldosteronism type I."
    Geller D.S., Rodriguez-Soriano J., Vallo Boado A., Schifter S., Bayer M., Chang S.S., Lifton R.P.
    Nat. Genet. 19:279-281(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 545-984, DISEASE.
  7. "Overexpression and characterization of the human mineralocorticoid receptor."
    Alnemri E.S., Maksymowych A.B., Robertson N.M., Litwack G.
    J. Biol. Chem. 266:18072-18081(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
  8. "Type I pseudohypoaldosteronism includes two clinically and genetically distinct entities with either renal or multiple target organ defects."
    Hanukoglu A.
    J. Clin. Endocrinol. Metab. 73:936-944(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEFINITION OF DIFFERENT FORMS OF PSEUDOHYPOALDOSTERONISM TYPE 1.
  9. "Identification of a splice variant of the rat and human mineralocorticoid receptor genes."
    Bloem L.J., Guo C., Pratt J.H.
    J. Steroid Biochem. Mol. Biol. 55:159-162(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 3).
    Tissue: Leukocyte.
  10. "Tissue-specific expression of alpha and beta messenger ribonucleic acid isoforms of the human mineralocorticoid receptor in normal and pathological states."
    Zennaro M.-C., Farman N., Bonvalet J.-P., Lombes M.
    J. Clin. Endocrinol. Metab. 82:1345-1352(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52."
    Bruner K.L., Derfoul A., Robertson N.M., Guerriero G., Fernandes-Alnemri T., Alnemri E.S., Litwack G.
    Recept. Signal Transduct. 7:85-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TERNARY COMPLEX WITH HSP90; HSP70 AND FKBP4, DISSOCIATION UPON ALDOSTERONE BINDING.
  12. "Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for steroid binding."
    Lupo B., Mesnier D., Auzou G.
    Biochemistry 37:12153-12159(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-808; CYS-849 AND CYS-942.
  13. "Mechanistic aspects of mineralocorticoid receptor activation."
    Hellal-Levy C., Fagart J., Souque A., Rafestin-Oblin M.-E.
    Kidney Int. 57:1250-1255(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-770; GLN-776; ARG-817 AND THR-945.
  14. "Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor."
    Hellal-Levy C., Fagart J., Souque A., Wurtz J.-M., Moras D., Rafestin-Oblin M.-E.
    Mol. Endocrinol. 14:1210-1221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA1; TIF1 AND NRIP1, MUTAGENESIS OF LEU-952; LYS-953; VAL-954; PHE-956 AND PRO-957.
  15. "The intracellular localization of the mineralocorticoid receptor is regulated by 11beta-hydroxysteroid dehydrogenase type 2."
    Odermatt A., Arnold P., Frey F.J.
    J. Biol. Chem. 276:28484-28492(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HSD11B2.
  16. "Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
    Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
    Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor."
    Bledsoe R.K., Madauss K.P., Holt J.A., Apolito C.J., Lambert M.H., Pearce K.H., Stanley T.B., Stewart E.L., Trump R.P., Willson T.M., Williams S.P.
    J. Biol. Chem. 280:31283-31293(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 712-984 OF MUTANT SER-808 IN COMPLEXES WITH AGONIST AND ANTAGONISTS, CHARACTERIZATION OF VARIANT EOHSEP LEU-810, MUTAGENESIS OF SER-767; ASN-770 AND THR-945.
  18. "Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor."
    Li Y., Suino K., Daugherty J., Xu H.E.
    Mol. Cell 19:367-380(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 732-984 OF MUTANT SER-808 IN COMPLEX WITH STEROID LIGAND AND NCOA2, SUBUNIT, MUTAGENESIS OF LYS-782; LYS-785 AND GLU-796.
  19. "Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension."
    Fagart J., Huyet J., Pinon G.M., Rochel M., Mayer C., Rafestin-Oblin M.-E.
    Nat. Struct. Mol. Biol. 12:554-555(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 731-984 OF MUTANT LEU-810 IN COMPLEXES WITH STEROID AGONISTS, CHARACTERIZATION OF VARIANT EOHSEP LEU-810, MUTAGENESIS OF GLN-776 AND ARG-817.
  20. "Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
    Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
    Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-180; THR-444; GLN-537 AND SER-554.
  21. "A novel missense mutation of mineralocorticoid receptor gene in one Japanese family with a renal form of pseudohypoaldosteronism type 1."
    Tajima T., Kitagawa H., Yokoya S., Tachibana K., Adachi M., Nakae J., Suwa S., Katoh S., Fujieda K.
    J. Clin. Endocrinol. Metab. 85:4690-4694(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT PHA1A PRO-924.
  22. "Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy."
    Geller D.S., Farhi A., Pinkerton N., Fradley M., Moritz M., Spitzer A., Meinke G., Tsai F.T.F., Sigler P.B., Lifton R.P.
    Science 289:119-123(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EOHSEP LEU-810, MUTAGENESIS OF SER-810.
  23. "Functional polymorphisms in the mineralocorticoid receptor and amirolide-sensitive sodium channel genes in a patient with sporadic pseudohypoaldosteronism."
    Arai K., Nakagomi Y., Iketani M., Shimura Y., Amemiya S., Ohyama K., Shibasaki T.
    Hum. Genet. 112:91-97(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS VAL-180 AND VAL-241.
  24. Cited for: CHARACTERIZATION OF VARIANTS PHA1A ARG-633; ARG-776; PRO-924 AND PRO-979.
  25. "Elucidating the underlying molecular pathogenesis of NR3C2 mutants causing autosomal dominant pseudohypoaldosteronism type 1."
    Riepe F.G., Finkeldei J., de Sanctis L., Einaudi S., Testa A., Karges B., Peter M., Viemann M., Groetzinger J., Sippell W.G., Fejes-Toth G., Krone N.
    J. Clin. Endocrinol. Metab. 91:4552-4561(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS PHA1A LEU-818 AND GLY-972.
  26. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-7.
  27. "Mineralocorticoid receptor mutations are the principal cause of renal type 1 pseudohypoaldosteronism."
    Pujo L., Fagart J., Gary F., Papadimitriou D.T., Claes A., Jeunemaitre X., Zennaro M.-C.
    Hum. Mutat. 28:33-40(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHA1A SER-645; SER-659; SER-759; PRO-769; LYS-770; PRO-805 AND ARG-815.

Entry informationi

Entry nameiMCR_HUMAN
AccessioniPrimary (citable) accession number: P08235
Secondary accession number(s): B0ZBF5
, B0ZBF7, Q2NKL1, Q96KQ8, Q96KQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 29, 2014
This is version 170 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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