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Protein

Mineralocorticoid receptor

Gene

NR3C2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei770Steroid1
Binding sitei776Steroid1
Binding sitei817Steroid1
Binding sitei945Steroid1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi603 – 668Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri603 – 623NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri639 – 663NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • sequence-specific DNA binding Source: InterPro
  • steroid binding Source: UniProtKB-KW
  • steroid hormone receptor activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • signal transduction Source: ProtInc
  • 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

BioCyciZFISH:ENSG00000151623-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiP08235.
SIGNORiP08235.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:7979. NR3C2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:177735
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031268633G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 Publication1
Natural variantiVAR_031269645C → S in PHA1A. 1 Publication1
Natural variantiVAR_031270659R → S in PHA1A. 1 Publication1
Natural variantiVAR_031271759P → S in PHA1A. 1 Publication1
Natural variantiVAR_031272769L → P in PHA1A. 1 Publication1
Natural variantiVAR_031273770N → K in PHA1A. 1 Publication1
Natural variantiVAR_031274776Q → R in PHA1A; reduces aldosterone binding. 1 Publication1
Natural variantiVAR_031275805S → P in PHA1A. 1 Publication1
Natural variantiVAR_031276815S → R in PHA1A. 1 Publication1
Natural variantiVAR_031277818S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 Publication1
Natural variantiVAR_015627924L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 Publications1
Natural variantiVAR_031278972E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 Publication1
Natural variantiVAR_031279979L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 Publication1
Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionInheritance is autosomal dominant. The disease is characterized by the onset of severe hypertension before the age of 20, and by suppression of aldosterone secretion.
See also OMIM:605115
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015626810S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant rs41511344dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi767S → N: Loss of transcription transactivation. 1 Publication1
Mutagenesisi767S → Q: Strong decrease of transcription transactivation. 1 Publication1
Mutagenesisi770N → A, D, H, Q, S or T: Abolishes aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi776Q → A: Reduces aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi782K → E: Decreased coactivator binding. 1 Publication1
Mutagenesisi785K → E: Loss of coactivator binding. 1 Publication1
Mutagenesisi796E → R: Decreased coactivator binding. 1 Publication1
Mutagenesisi808C → S: Increases aldosterone-binding. 1 Publication1
Mutagenesisi810S → M: Alters receptor specificity. 1 Publication1
Mutagenesisi817R → A: Reduces aldosterone binding and transcription transactivation. 2 Publications1
Mutagenesisi849C → S: Strongly decreases affinity for aldosterone and transcription transactivation. 1 Publication1
Mutagenesisi942C → S: Abolishes steroid binding and transcription transactivation. 1 Publication1
Mutagenesisi945T → A: Decreases aldosterone-binding and cortisol-binding. 2 Publications1
Mutagenesisi952L → A: Reduces transcription transactivation. 1 Publication1
Mutagenesisi953K → A: Slightly reduces aldosterone binding and abolishes transcription transactivation. 1 Publication1
Mutagenesisi954V → A: Reduces aldosterone binding and abolishes transcription transactivation. 1 Publication1
Mutagenesisi956F → A: Abolishes aldosterone binding and transcription transactivation. 1 Publication1
Mutagenesisi957P → A: Slightly reduces aldosterone binding and transcription transactivation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4306.
MalaCardsiNR3C2.
MIMi177735. phenotype.
605115. phenotype.
Orphaneti88660. Pseudohyperaldosteronism type 2.
171871. Renal pseudohypoaldosteronism type 1.
PharmGKBiPA242.

Chemistry databases

ChEMBLiCHEMBL1994.
DrugBankiDB01395. Drospirenone.
DB00700. Eplerenone.
DB01023. Felodipine.
DB00687. Fludrocortisone.
DB00588. Fluticasone Propionate.
DB00393. Nimodipine.
DB00396. Progesterone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi626.

Polymorphism and mutation databases

BioMutaiNR3C2.
DMDMi126885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536821 – 984Mineralocorticoid receptorAdd BLAST984

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei250PhosphoserineBy similarity1
Modified residuei259PhosphoserineBy similarity1
Modified residuei283PhosphoserineBy similarity1
Modified residuei287PhosphoserineBy similarity1
Modified residuei299PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08235.
PaxDbiP08235.
PeptideAtlasiP08235.
PRIDEiP08235.

PTM databases

iPTMnetiP08235.
PhosphoSitePlusiP08235.

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

BgeeiENSG00000151623.
CleanExiHS_NR3C2.
ExpressionAtlasiP08235. baseline and differential.

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. 25 interactors.
IntActiP08235. 5 interactors.
STRINGi9606.ENSP00000341390.

Chemistry databases

BindingDBiP08235.

Structurei

Secondary structure

1984
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni604 – 606Combined sources3
Beta strandi612 – 614Combined sources3
Helixi621 – 632Combined sources12
Beta strandi640 – 643Combined sources4
Turni649 – 654Combined sources6
Helixi656 – 665Combined sources10
Helixi728 – 733Combined sources6
Helixi738 – 745Combined sources8
Helixi762 – 785Combined sources24
Helixi790 – 792Combined sources3
Helixi795 – 822Combined sources28
Beta strandi825 – 830Combined sources6
Beta strandi833 – 835Combined sources3
Helixi837 – 842Combined sources6
Helixi846 – 862Combined sources17
Helixi866 – 877Combined sources12
Beta strandi879 – 881Combined sources3
Helixi889 – 909Combined sources21
Helixi911 – 913Combined sources3
Turni914 – 916Combined sources3
Helixi917 – 947Combined sources31
Helixi949 – 952Combined sources4
Helixi958 – 972Combined sources15
Beta strandi976 – 978Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PF3X-ray1.10A712-984[»]
4TNTX-ray2.39A/B593-671[»]
4UDAX-ray2.03A735-984[»]
4UDBX-ray2.36A735-984[»]
5HCVX-ray2.50A/B/C732-984[»]
ProteinModelPortaliP08235.
SMRiP08235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08235.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 602ModulatingAdd BLAST602
Regioni669 – 732HingeAdd BLAST64
Regioni733 – 984Steroid-bindingAdd BLAST252
Regioni782 – 785Important for coactivator binding4

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)DescriptionActionsGraphical viewLength
Zinc fingeri603 – 623NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri639 – 663NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000247011.
HOVERGENiHBG006336.
InParanoidiP08235.
KOiK08555.
PhylomeDBiP08235.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti946F → I in AAI11759 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0360637H → Q in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_014623180I → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; increases transcription transactivation at low aldosterone concentrations. 6 PublicationsCorresponds to variant rs5522dbSNPEnsembl.1
Natural variantiVAR_015625241A → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; reduces transcription transactivation upon aldosterone binding. 5 Publications1
Natural variantiVAR_014624444N → T.1 PublicationCorresponds to variant rs5523dbSNPEnsembl.1
Natural variantiVAR_014625537R → Q.1 PublicationCorresponds to variant rs5526dbSNPEnsembl.1
Natural variantiVAR_014626554N → S.1 PublicationCorresponds to variant rs5527dbSNPEnsembl.1
Natural variantiVAR_031268633G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 Publication1
Natural variantiVAR_031269645C → S in PHA1A. 1 Publication1
Natural variantiVAR_031270659R → S in PHA1A. 1 Publication1
Natural variantiVAR_031271759P → S in PHA1A. 1 Publication1
Natural variantiVAR_031272769L → P in PHA1A. 1 Publication1
Natural variantiVAR_031273770N → K in PHA1A. 1 Publication1
Natural variantiVAR_031274776Q → R in PHA1A; reduces aldosterone binding. 1 Publication1
Natural variantiVAR_031275805S → P in PHA1A. 1 Publication1
Natural variantiVAR_015626810S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant rs41511344dbSNPEnsembl.1
Natural variantiVAR_031276815S → R in PHA1A. 1 Publication1
Natural variantiVAR_031277818S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 Publication1
Natural variantiVAR_029311826F → Y.Corresponds to variant rs13306592dbSNPEnsembl.1
Natural variantiVAR_015627924L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 Publications1
Natural variantiVAR_031278972E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 Publication1
Natural variantiVAR_031279979L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_007357633G → GKCSW in isoform 3. Curated1
Alternative sequenceiVSP_007360672 – 788Missing in isoform 4. 2 PublicationsAdd BLAST117
Alternative sequenceiVSP_007358672 – 706ARKSK…QSPEE → ERRCISLPCMNYARGCTKSA FSSFDCSSPLKNTPS in isoform 2. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_007359707 – 984Missing in isoform 2. 1 PublicationAdd BLAST278

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011530277.1. XM_011531975.1.
XP_011530278.1. XM_011531976.2.
XP_011530279.1. XM_011531977.2.
UniGeneiHs.163924.

Genome annotation databases

EnsembliENST00000511528; ENSP00000421481; ENSG00000151623.
ENST00000512865; ENSP00000423510; ENSG00000151623.
GeneIDi4306.
KEGGihsa:4306.
UCSCiuc003ilk.5. human. [P08235-1]

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:
EMBLi
GenBanki
DDBJi
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.
XP_011530277.1. XM_011531975.1.
XP_011530278.1. XM_011531976.2.
XP_011530279.1. XM_011531977.2.
UniGeneiHs.163924.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PF3X-ray1.10A712-984[»]
4TNTX-ray2.39A/B593-671[»]
4UDAX-ray2.03A735-984[»]
4UDBX-ray2.36A735-984[»]
5HCVX-ray2.50A/B/C732-984[»]
ProteinModelPortaliP08235.
SMRiP08235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110451. 25 interactors.
IntActiP08235. 5 interactors.
STRINGi9606.ENSP00000341390.

Chemistry databases

BindingDBiP08235.
ChEMBLiCHEMBL1994.
DrugBankiDB01395. Drospirenone.
DB00700. Eplerenone.
DB01023. Felodipine.
DB00687. Fludrocortisone.
DB00588. Fluticasone Propionate.
DB00393. Nimodipine.
DB00396. Progesterone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGYi626.

PTM databases

iPTMnetiP08235.
PhosphoSitePlusiP08235.

Polymorphism and mutation databases

BioMutaiNR3C2.
DMDMi126885.

Proteomic databases

MaxQBiP08235.
PaxDbiP08235.
PeptideAtlasiP08235.
PRIDEiP08235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000511528; ENSP00000421481; ENSG00000151623.
ENST00000512865; ENSP00000423510; ENSG00000151623.
GeneIDi4306.
KEGGihsa:4306.
UCSCiuc003ilk.5. human. [P08235-1]

Organism-specific databases

CTDi4306.
DisGeNETi4306.
GeneCardsiNR3C2.
H-InvDBHIX0024570.
HGNCiHGNC:7979. NR3C2.
HPAiCAB009155.
MalaCardsiNR3C2.
MIMi177735. phenotype.
600983. gene.
605115. phenotype.
neXtProtiNX_P08235.
Orphaneti88660. Pseudohyperaldosteronism type 2.
171871. Renal pseudohypoaldosteronism type 1.
PharmGKBiPA242.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000247011.
HOVERGENiHBG006336.
InParanoidiP08235.
KOiK08555.
PhylomeDBiP08235.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000151623-MONOMER.
ReactomeiR-HSA-383280. Nuclear Receptor transcription pathway.
SignaLinkiP08235.
SIGNORiP08235.

Miscellaneous databases

ChiTaRSiNR3C2. human.
EvolutionaryTraceiP08235.
GeneWikiiMineralocorticoid_receptor.
GenomeRNAii4306.
PROiP08235.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000151623.
CleanExiHS_NR3C2.
ExpressionAtlasiP08235. baseline and differential.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 192 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.