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P08235 (MCR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mineralocorticoid receptor

Short name=MR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 2
Gene names
Name:NR3C2
Synonyms:MCR, MLR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length984 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.18

Subcellular location

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. Ref.7 Ref.15 Ref.16

Tissue specificity

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. Ref.2 Ref.10

Domain

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

Post-translational modification

Phosphorylated. Ref.7

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.21 Ref.24 Ref.25 Ref.27

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.17 Ref.19 Ref.22

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P08235-1)

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.
Isoform 2 (identifier: P08235-2)

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.
Isoform 3 (identifier: P08235-3)

The sequence of this isoform differs from the canonical sequence as follows:
     633-633: G → GKCSW
Isoform 4 (identifier: P08235-4)

Also known as: Delta;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 984984Mineralocorticoid receptor
PRO_0000053682

Regions

DNA binding603 – 66866Nuclear receptor
Zinc finger603 – 62321NR C4-type
Zinc finger639 – 66325NR C4-type
Region1 – 602602Modulating
Region669 – 73264Hinge
Region733 – 984252Steroid-binding
Region782 – 7854Important for coactivator binding

Sites

Binding site7701Steroid
Binding site7761Steroid
Binding site8171Steroid
Binding site9451Steroid

Amino acid modifications

Modified residue2991Phosphoserine By similarity

Natural variations

Alternative sequence6331G → GKCSW in isoform 3.
VSP_007357
Alternative sequence672 – 788117Missing in isoform 4.
VSP_007360
Alternative sequence672 – 70635ARKSK…QSPEE → ERRCISLPCMNYARGCTKSA FSSFDCSSPLKNTPS in isoform 2.
VSP_007358
Alternative sequence707 – 984278Missing in isoform 2.
VSP_007359
Natural variant71H → Q in a colorectal cancer sample; somatic mutation. Ref.26
VAR_036063
Natural variant1801I → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; increases transcription transactivation at low aldosterone concentrations. Ref.2 Ref.3 Ref.4 Ref.5 Ref.20 Ref.23
Corresponds to variant rs5522 [ dbSNP | Ensembl ].
VAR_014623
Natural variant2411A → V High frequency in healthy individuals; found in a patient with sporadic pseudohypoaldosteronism type I; reduces transcription transactivation upon aldosterone binding. Ref.2 Ref.3 Ref.4 Ref.5 Ref.23
VAR_015625
Natural variant4441N → T. Ref.20
Corresponds to variant rs5523 [ dbSNP | Ensembl ].
VAR_014624
Natural variant5371R → Q. Ref.20
Corresponds to variant rs5526 [ dbSNP | Ensembl ].
VAR_014625
Natural variant5541N → S. Ref.20
Corresponds to variant rs5527 [ dbSNP | Ensembl ].
VAR_014626
Natural variant6331G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. Ref.24
VAR_031268
Natural variant6451C → S in PHA1A. Ref.27
VAR_031269
Natural variant6591R → S in PHA1A. Ref.27
VAR_031270
Natural variant7591P → S in PHA1A. Ref.27
VAR_031271
Natural variant7691L → P in PHA1A. Ref.27
VAR_031272
Natural variant7701N → K in PHA1A. Ref.27
VAR_031273
Natural variant7761Q → R in PHA1A; reduces aldosterone binding. Ref.24
VAR_031274
Natural variant8051S → P in PHA1A. Ref.27
VAR_031275
Natural variant8101S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. Ref.17 Ref.19 Ref.22
Corresponds to variant rs41511344 [ dbSNP | Ensembl ].
VAR_015626
Natural variant8151S → R in PHA1A. Ref.27
VAR_031276
Natural variant8181S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. Ref.25
VAR_031277
Natural variant8261F → Y.
Corresponds to variant rs13306592 [ dbSNP | Ensembl ].
VAR_029311
Natural variant9241L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. Ref.21 Ref.24
VAR_015627
Natural variant9721E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. Ref.25
VAR_031278
Natural variant9791L → P in PHA1A; loss of aldosterone binding and transcription transactivation. Ref.24
VAR_031279

Experimental info

Mutagenesis7671S → N: Loss of transcription transactivation. Ref.17
Mutagenesis7671S → Q: Strong decrease of transcription transactivation. Ref.17
Mutagenesis7701N → A, D, H, Q, S or T: Abolishes aldosterone binding and transcription transactivation. Ref.13 Ref.17
Mutagenesis7761Q → A: Reduces aldosterone binding and transcription transactivation. Ref.13 Ref.19
Mutagenesis7821K → E: Decreased coactivator binding. Ref.18
Mutagenesis7851K → E: Loss of coactivator binding. Ref.18
Mutagenesis7961E → R: Decreased coactivator binding. Ref.18
Mutagenesis8081C → S: Increases aldosterone-binding. Ref.12
Mutagenesis8101S → M: Alters receptor specificity. Ref.22
Mutagenesis8171R → A: Reduces aldosterone binding and transcription transactivation. Ref.13 Ref.19
Mutagenesis8491C → S: Strongly decreases affinity for aldosterone and transcription transactivation. Ref.12
Mutagenesis9421C → S: Abolishes steroid binding and transcription transactivation. Ref.12
Mutagenesis9451T → A: Decreases aldosterone-binding and cortisol-binding. Ref.13 Ref.17
Mutagenesis9521L → A: Reduces transcription transactivation. Ref.14
Mutagenesis9531K → A: Slightly reduces aldosterone binding and abolishes transcription transactivation. Ref.14
Mutagenesis9541V → A: Reduces aldosterone binding and abolishes transcription transactivation. Ref.14
Mutagenesis9561F → A: Abolishes aldosterone binding and transcription transactivation. Ref.14
Mutagenesis9571P → A: Slightly reduces aldosterone binding and transcription transactivation. Ref.14
Sequence conflict9461F → I in AAI11759. Ref.5

Secondary structure

................................... 984
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 8300CD1A18C1858A

FASTA984107,067
        10         20         30         40         50         60 
METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC VSGAIPNNST 

        70         80         90        100        110        120 
QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT VAESMGLYMD SVRDADYSYE 

       130        140        150        160        170        180 
QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR PSTLSCVNTP LRSFMSDSGS SVNGGVMRAI 

       190        200        210        220        230        240 
VKSPIMCHEK SPSVCSPLNM TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN 

       250        260        270        280        290        300 
AENRGSRSHS PAHASNVGSP LSSPLSSMKS SISSPPSHCS VKSPVSSPNN VTLRSSVSSP 

       310        320        330        340        350        360 
ANINNSRCSV SSPSNTNNRS TLSSPAASTV GSICSPVNNA FSYTASGTSA GSSTLRDVVP 

       370        380        390        400        410        420 
SPDTQEKGAQ EVPFPKTEEV ESAISNGVTG QLNIVQYIKP EPDGAFSSSC LGGNSKINSD 

       430        440        450        460        470        480 
SSFSVPIKQE STKHSCSGTS FKGNPTVNPF PFMDGSYFSF MDDKDYYSLS GILGPPVPGF 

       490        500        510        520        530        540 
DGNCEGSGFP VGIKQEPDDG SYYPEASIPS SAIVGVNSGG QSFHYRIGAQ GTISLSRSAR 

       550        560        570        580        590        600 
DQSFQHLSSF PPVNTLVESW KSHGDLSSRR SDGYPVLEYI PENVSSSTLR SVSTGSSRPS 

       610        620        630        640        650        660 
KICLVCGDEA SGCHYGVVTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI RRKNCPACRL 

       670        680        690        700        710        720 
QKCLQAGMNL GARKSKKLGK LKGIHEEQPQ QQQPPPPPPP PQSPEEGTTY IAPAKEPSVN 

       730        740        750        760        770        780 
TALVPQLSTI SRALTPSPVM VLENIEPEIV YAGYDSSKPD TAENLLSTLN RLAGKQMIQV 

       790        800        810        820        830        840 
VKWAKVLPGF KNLPLEDQIT LIQYSWMCLS SFALSWRSYK HTNSQFLYFA PDLVFNEEKM 

       850        860        870        880        890        900 
HQSAMYELCQ GMHQISLQFV RLQLTFEEYT IMKVLLLLST IPKDGLKSQA AFEEMRTNYI 

       910        920        930        940        950        960 
KELRKMVTKC PNNSGQSWQR FYQLTKLLDS MHDLVSDLLE FCFYTFRESH ALKVEFPAML 

       970        980 
VEIISDQLPK VESGNAKPLY FHRK 

« Hide

Isoform 2 [UniParc].

Checksum: EEFC58BB02FA0812
Show »

FASTA70675,052
Isoform 3 [UniParc].

Checksum: D6257319E5482C86
Show »

FASTA988107,572
Isoform 4 (Delta) [UniParc].

Checksum: BEC8DD3A6A855903
Show »

FASTA86794,359

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Different inactivating mutations of the mineralocorticoid receptor in fourteen families affected by type I pseudohypoaldosteronism."
Sartorato P., Lapeyraque A.-L., Armanini D., Kuhnle U., Khaldi Y., Salomon R., Abadie V., Di Battista E., Naselli A., Racine A., Bosio M., Caprio M., Poulet-Young V., Chabrolle J.-P., Niaudet P., De Gennes C., Lecornec M.-H., Poisson E. expand/collapse author list , Fusco A.M., Loli P., Lombes M., Zennaro M.-C.
J. Clin. Endocrinol. Metab. 88:2508-2517(2003) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3772.1. [P08235-1]
CCDS54811.1. [P08235-4]
PIRA29513.
RefSeqNP_000892.2. NM_000901.4.
NP_001159576.1. NM_001166104.1.
UniGeneHs.163924.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP08235.
SMRP08235. Positions 596-984.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110451. 22 interactions.
IntActP08235. 4 interactions.
STRING9606.ENSP00000350815.

Chemistry

BindingDBP08235.
ChEMBLCHEMBL1994.
DrugBankDB01134. Desoxycorticosterone Pivalate.
DB00700. Eplerenone.
DB00687. Fludrocortisone.
DB00421. Spironolactone.
GuidetoPHARMACOLOGY626.

PTM databases

PhosphoSiteP08235.

Polymorphism databases

DMDM126885.

Proteomic databases

PaxDbP08235.
PRIDEP08235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355292; ENSP00000347441; ENSG00000151623.
ENST00000511528; ENSP00000421481; ENSG00000151623.
ENST00000512865; ENSP00000423510; ENSG00000151623.
GeneID4306.
KEGGhsa:4306.
UCSCuc003ilk.4. human.

Organism-specific databases

CTD4306.
GeneCardsGC04M148999.
H-InvDBHIX0024570.
HGNCHGNC:7979. NR3C2.
HPACAB009155.
MIM177735. phenotype.
600983. gene.
605115. phenotype.
neXtProtNX_P08235.
Orphanet88660. Pseudohyperaldosteronism type 2.
171871. Renal pseudohypoaldosteronism type 1.
PharmGKBPA242.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294115.
HOGENOMHOG000247011.
HOVERGENHBG006336.
KOK08555.
PhylomeDBP08235.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP08235.

Gene expression databases

ArrayExpressP08235.
BgeeP08235.
CleanExHS_NR3C2.
GenevestigatorP08235.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08235.
GeneWikiMineralocorticoid_receptor.
GenomeRNAi4306.
NextBio16949.
PROP08235.
SOURCESearch...

Entry information

Entry nameMCR_HUMAN
AccessionPrimary (citable) accession number: P08235
Secondary accession number(s): B0ZBF5 expand/collapse secondary AC list , B0ZBF7, Q2NKL1, Q96KQ8, Q96KQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM