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P08235

- MCR_HUMAN

UniProt

P08235 - MCR_HUMAN

Protein

Mineralocorticoid receptor

Gene

NR3C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. steroid binding Source: UniProtKB-KW
    5. steroid hormone receptor activity Source: ProtInc
    6. 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

    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 membrane Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. receptor complex Source: MGI

    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

    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

    ArrayExpressiP08235.
    BgeeiP08235.
    CleanExiHS_NR3C2.
    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. 22 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[»]
    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.
    HOGENOMiHOG000247011.
    HOVERGENiHBG006336.
    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

    METKGYHSLP EGLDMERRWG QVSQAVERSS LGPTERTDEN NYMEIVNVSC    50
    VSGAIPNNST QGSSKEKQEL LPCLQQDNNR PGILTSDIKT ELESKELSAT 100
    VAESMGLYMD SVRDADYSYE QQNQQGSMSP AKIYQNVEQL VKFYKGNGHR 150
    PSTLSCVNTP LRSFMSDSGS SVNGGVMRAI VKSPIMCHEK SPSVCSPLNM 200
    TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN AENRGSRSHS 250
    PAHASNVGSP LSSPLSSMKS SISSPPSHCS VKSPVSSPNN VTLRSSVSSP 300
    ANINNSRCSV SSPSNTNNRS TLSSPAASTV GSICSPVNNA FSYTASGTSA 350
    GSSTLRDVVP SPDTQEKGAQ EVPFPKTEEV ESAISNGVTG QLNIVQYIKP 400
    EPDGAFSSSC LGGNSKINSD SSFSVPIKQE STKHSCSGTS FKGNPTVNPF 450
    PFMDGSYFSF MDDKDYYSLS GILGPPVPGF DGNCEGSGFP VGIKQEPDDG 500
    SYYPEASIPS SAIVGVNSGG QSFHYRIGAQ GTISLSRSAR DQSFQHLSSF 550
    PPVNTLVESW KSHGDLSSRR SDGYPVLEYI PENVSSSTLR SVSTGSSRPS 600
    KICLVCGDEA SGCHYGVVTC GSCKVFFKRA VEGQHNYLCA GRNDCIIDKI 650
    RRKNCPACRL QKCLQAGMNL GARKSKKLGK LKGIHEEQPQ QQQPPPPPPP 700
    PQSPEEGTTY IAPAKEPSVN TALVPQLSTI SRALTPSPVM VLENIEPEIV 750
    YAGYDSSKPD TAENLLSTLN RLAGKQMIQV VKWAKVLPGF KNLPLEDQIT 800
    LIQYSWMCLS SFALSWRSYK HTNSQFLYFA PDLVFNEEKM HQSAMYELCQ 850
    GMHQISLQFV RLQLTFEEYT IMKVLLLLST IPKDGLKSQA AFEEMRTNYI 900
    KELRKMVTKC PNNSGQSWQR FYQLTKLLDS MHDLVSDLLE FCFYTFRESH 950
    ALKVEFPAML VEIISDQLPK VESGNAKPLY FHRK 984
    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 [» ]
    ProteinModelPortali P08235.
    SMRi P08235. Positions 596-984.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110451. 22 interactions.
    IntActi P08235. 4 interactions.
    STRINGi 9606.ENSP00000350815.

    Chemistry

    BindingDBi P08235.
    ChEMBLi CHEMBL1994.
    DrugBanki DB01134. Desoxycorticosterone Pivalate.
    DB00700. Eplerenone.
    DB00687. Fludrocortisone.
    DB00421. Spironolactone.
    GuidetoPHARMACOLOGYi 626.

    PTM databases

    PhosphoSitei P08235.

    Polymorphism databases

    DMDMi 126885.

    Proteomic databases

    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.
    HOGENOMi HOG000247011.
    HOVERGENi HBG006336.
    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

    ArrayExpressi P08235.
    Bgeei P08235.
    CleanExi HS_NR3C2.
    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

    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 1, 2014
    This is version 169 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