NR3C2

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	603	Zinc 1Combined sources1 Publication	1
Metal bindingⁱ	606	Zinc 1Combined sources1 Publication	1
Metal bindingⁱ	620	Zinc 1Combined sources1 Publication	1
Metal bindingⁱ	623	Zinc 1Combined sources1 Publication	1
Metal bindingⁱ	639	Zinc 2Combined sources1 Publication	1
Metal bindingⁱ	645	Zinc 2Combined sources1 Publication	1
Metal bindingⁱ	655	Zinc 2Combined sources1 Publication	1
Metal bindingⁱ	658	Zinc 2Combined sources1 Publication	1
Binding siteⁱ	770	11-deoxycorticosteroneCombined sources2 Publications	1
Binding siteⁱ	770	AldosteroneCombined sources1 Publication	1
Binding siteⁱ	770	ProgesteroneCombined sources2 Publications	1
Binding siteⁱ	776	11-deoxycorticosteroneCombined sources2 Publications	1
Binding siteⁱ	776	AldosteroneCombined sources1 Publication	1
Binding siteⁱ	776	ProgesteroneCombined sources2 Publications	1
Binding siteⁱ	817	11-deoxycorticosteroneCombined sources2 Publications	1
Binding siteⁱ	817	AldosteroneCombined sources1 Publication	1
Binding siteⁱ	817	ProgesteroneCombined sources2 Publications	1
Binding siteⁱ	945	11-deoxycorticosteroneCombined sources2 Publications	1
Binding siteⁱ	945	AldosteroneCombined sources1 Publication	1
Binding siteⁱ	945	ProgesteroneCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
DNA bindingⁱ	603 – 668	Nuclear receptorPROSITE-ProRule annotationAdd BLAST	66
Zinc fingerⁱ	603 – 623	NR C4-typePROSITE-ProRule annotationAdd BLAST	21
Zinc fingerⁱ	639 – 663	NR C4-typePROSITE-ProRule annotationAdd BLAST	25

GO - Molecular functionⁱ

DNA-binding transcription factor activity
Source: ProtInc
Traceable author statementⁱ
- Ref.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, VARIANTS ILE-180 AND ALA-241.
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
nuclear receptor activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
RNA polymerase II cis-regulatory region sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
sequence-specific double-stranded DNA binding
Source: ARUK-UCL
Inferred from direct assayⁱ
- "Impact of cytosine methylation on DNA binding specificities of human transcription factors."
  Yin Y., Morgunova E., Jolma A., Kaasinen E., Sahu B., Khund-Sayeed S., Das P.K., Kivioja T., Dave K., Zhong F., Nitta K.R., Taipale M., Popov A., Ginno P.A., Domcke S., Yan J., Schubeler D., Vinson C., Taipale J.
  Science 356:0-0(2017) [PubMed] [Europe PMC] [Abstract]
steroid binding Source: UniProtKB-KW
steroid hormone receptor activity
Source: ProtInc
Traceable author statementⁱ
- Ref.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.
zinc ion binding Source: InterPro

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Receptor
Biological process	Transcription, Transcription regulation
Ligand	Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

PathwayCommonsⁱ	P08235
Reactomeⁱ	R-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-4090294, SUMOylation of intracellular receptors
SignaLinkⁱ	P08235
SIGNORⁱ	P08235

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7979, NR3C2
MIMⁱ	600983, gene
neXtProtⁱ	NX_P08235
VEuPathDBⁱ	HostDB:ENSG00000151623

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Pseudohypoaldosteronism 1, autosomal dominant (PHA1A)4 Publications

The disease is caused by variants 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_031268	633	G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912566EnsemblClinVar.	1
Natural variantⁱVAR_031269	645	C → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031270	659	R → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031271	759	P → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031272	769	L → P in PHA1A. 1 Publication	1
Natural variantⁱVAR_031273	770	N → K in PHA1A. 1 Publication	1
Natural variantⁱVAR_031274	776	Q → R in PHA1A; reduces aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912565EnsemblClinVar.	1
Natural variantⁱVAR_031275	805	S → P in PHA1A. 1 Publication	1
Natural variantⁱVAR_031276	815	S → R in PHA1A. 1 Publication	1
Natural variantⁱVAR_031277	818	S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912573EnsemblClinVar.	1
Natural variantⁱVAR_015627	924	L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 PublicationsCorresponds to variant dbSNP:rs121912563EnsemblClinVar.	1
Natural variantⁱVAR_031278	972	E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912574EnsemblClinVar.	1
Natural variantⁱVAR_031279	979	L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912567EnsemblClinVar.	1

Early-onset hypertension with severe exacerbation in pregnancy (EOHSEP)3 Publications

The disease is caused by variants 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_015626	810	S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant dbSNP:rs41511344EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	767	S → N: Loss of transcription transactivation. 1 Publication	1
Mutagenesisⁱ	767	S → Q: Strong decrease of transcription transactivation. 1 Publication	1
Mutagenesisⁱ	770	N → A, D, H, Q, S or T: Abolishes aldosterone binding and transcription transactivation. 2 Publications	1
Mutagenesisⁱ	776	Q → A: Reduces aldosterone binding and transcription transactivation. 2 Publications	1
Mutagenesisⁱ	782	K → E: Decreased coactivator binding. 1 Publication	1
Mutagenesisⁱ	785	K → E: Loss of coactivator binding. 1 Publication	1
Mutagenesisⁱ	796	E → R: Decreased coactivator binding. 1 Publication	1
Mutagenesisⁱ	808	C → S: Increases aldosterone-binding. 1 Publication	1
Mutagenesisⁱ	810	S → M: Alters receptor specificity. 1 Publication	1
Mutagenesisⁱ	817	R → A: Reduces aldosterone binding and transcription transactivation. 2 Publications	1
Mutagenesisⁱ	849	C → S: Strongly decreases affinity for aldosterone and transcription transactivation. 1 Publication	1
Mutagenesisⁱ	942	C → S: Abolishes steroid binding and transcription transactivation. 1 Publication	1
Mutagenesisⁱ	945	T → A: Decreases aldosterone-binding and cortisol-binding. 2 Publications	1
Mutagenesisⁱ	952	L → A: Reduces transcription transactivation. 1 Publication	1
Mutagenesisⁱ	953	K → A: Slightly reduces aldosterone binding and abolishes transcription transactivation. 1 Publication	1
Mutagenesisⁱ	954	V → A: Reduces aldosterone binding and abolishes transcription transactivation. 1 Publication	1
Mutagenesisⁱ	956	F → A: Abolishes aldosterone binding and transcription transactivation. 1 Publication	1
Mutagenesisⁱ	957	P → A: Slightly reduces aldosterone binding and transcription transactivation. 1 Publication	1

Keywords - Diseaseⁱ

Disease variant

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4306
MalaCards human disease database More...MalaCardsⁱ	NR3C2
MIMⁱ	177735, phenotype 605115, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000151623
Orphanetⁱ	171871, Renal pseudohypoaldosteronism type 1
PharmGKBⁱ	PA242

Miscellaneous databases

Pharosⁱ	P08235, Tclin

Pharosⁱ

P08235, Tclin

Chemistry databases

ChEMBLⁱ	CHEMBL1994
Drug and drug target database More...DrugBankⁱ	DB04630, Aldosterone DB01013, Clobetasol propionate DB04652, Corticosterone DB06780, Desoxycorticosterone acetate DB01134, Desoxycorticosterone pivalate DB01395, Drospirenone DB00700, Eplerenone DB01023, Felodipine DB00687, Fludrocortisone DB13867, Fluticasone DB08906, Fluticasone furoate DB00588, Fluticasone propionate DB02998, Metribolone DB00393, Nimodipine DB00396, Progesterone DB00421, Spironolactone DB02901, Stanolone DB13951, Stanolone acetate DB00624, Testosterone DB13943, Testosterone cypionate DB13944, Testosterone enanthate DB13946, Testosterone undecanoate
DrugCentral More...DrugCentralⁱ	P08235
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	626

Genetic variation databases

BioMutaⁱ	NR3C2
DMDMⁱ	126885

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000053682	1 – 984	Mineralocorticoid receptorAdd BLAST		984

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	250	PhosphoserineBy similarity	1
Modified residueⁱ	259	PhosphoserineBy similarity	1
Modified residueⁱ	283	PhosphoserineBy similarity	1
Modified residueⁱ	287	PhosphoserineBy similarity	1
Modified residueⁱ	299	PhosphoserineBy similarity	1

Post-translational modificationⁱ

Phosphorylated.1 Publication

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

jPOSTⁱ	P08235
MassIVEⁱ	P08235
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P08235
PaxDbⁱ	P08235
PeptideAtlas More...PeptideAtlasⁱ	P08235
PRIDEⁱ	P08235
ProteomicsDBⁱ	2889 2891 52088 [P08235-1] 52089 [P08235-2] 52090 [P08235-3] 52091 [P08235-4]

PTM databases

iPTMnetⁱ	P08235
PhosphoSitePlusⁱ	P08235

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

Bgeeⁱ	ENSG00000151623, Expressed in colonic mucosa and 231 other tissues
ExpressionAtlasⁱ	P08235, baseline and differential

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000151623, Low tissue specificity

HPAⁱ

ENSG00000151623, Low tissue specificity

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

BioGRIDⁱ	110451, 33 interactors
CORUMⁱ	P08235
IntActⁱ	P08235, 7 interactors
STRINGⁱ	9606.ENSP00000350815

Chemistry databases

BindingDBⁱ

P08235

Miscellaneous databases

RNActⁱ	P08235, protein

RNActⁱ

P08235, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	604 – 606	Combined sources	3
Beta strandⁱ	612 – 614	Combined sources	3
Helixⁱ	621 – 632	Combined sources	12
Beta strandⁱ	640 – 643	Combined sources	4
Turnⁱ	649 – 654	Combined sources	6
Helixⁱ	656 – 665	Combined sources	10
Helixⁱ	728 – 733	Combined sources	6
Helixⁱ	738 – 745	Combined sources	8
Helixⁱ	762 – 785	Combined sources	24
Helixⁱ	790 – 792	Combined sources	3
Helixⁱ	795 – 822	Combined sources	28
Beta strandⁱ	825 – 830	Combined sources	6
Beta strandⁱ	833 – 835	Combined sources	3
Helixⁱ	837 – 842	Combined sources	6
Helixⁱ	846 – 862	Combined sources	17
Helixⁱ	866 – 877	Combined sources	12
Beta strandⁱ	879 – 881	Combined sources	3
Helixⁱ	889 – 909	Combined sources	21
Helixⁱ	911 – 913	Combined sources	3
Turnⁱ	914 – 916	Combined sources	3
Helixⁱ	917 – 947	Combined sources	31
Helixⁱ	949 – 952	Combined sources	4
Helixⁱ	958 – 972	Combined sources	15
Beta strandⁱ	976 – 978	Combined sources	3

Show more details

3D structure databases

SMRⁱ	P08235
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P08235

EvolutionaryTraceⁱ

P08235

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	726 – 964	NR LBDPROSITE-ProRule annotationAdd BLAST		239

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 602	ModulatingAdd BLAST	602
Regionⁱ	231 – 329	DisorderedSequence analysisAdd BLAST	99
Regionⁱ	347 – 373	DisorderedSequence analysisAdd BLAST	27
Regionⁱ	669 – 725	HingeAdd BLAST	57
Regionⁱ	684 – 710	DisorderedSequence analysisAdd BLAST	27
Regionⁱ	782 – 785	Important for coactivator binding	4

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	690 – 706	Pro residuesSequence analysisAdd BLAST		17

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the nuclear hormone receptor family. NR3 subfamily.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	603 – 623	NR C4-typePROSITE-ProRule annotationAdd BLAST		21
Zinc fingerⁱ	639 – 663	NR C4-typePROSITE-ProRule annotationAdd BLAST		25

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG3575, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000159333
InParanoidⁱ	P08235
OMAⁱ	CFGPLCS
Database of Orthologous Groups More...OrthoDBⁱ	146963at2759
PhylomeDBⁱ	P08235

Family and domain databases

Database of protein disorder More...DisProtⁱ	DP01561
Gene3Dⁱ	1.10.565.10, 1 hit 3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00104, Hormone_recep, 1 hit PF00105, zf-C4, 1 hit
PRINTSⁱ	PR00047, STROIDFINGER
SMARTⁱ	View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508, SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit

Sequences (4)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P08235-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        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 SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM 
       210        220        230        240        250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS 
       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):107,082

Last modified:September 12, 2018 - v2

Checksum:ⁱ833D900F2CB27390

GO

Isoform 2 (identifier: P08235-2) [UniParc]FASTA Add to basket

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

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        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 SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM 
       210        220        230        240        250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS 
       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 GERRCISLPC MNYARGCTKS AFSSFDCSSP 

LKNTPS

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

Show »

Length:706

Mass (Da):75,066

Checksum:ⁱ03CF63D0ACEE981C

GO

Isoform 3 (identifier: P08235-3) [UniParc]FASTA Add to basket

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

« 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 SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM 
       210        220        230        240        250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS 
       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 VEGKCSWQHN YLCAGRNDCI 
       660        670        680        690        700
IDKIRRKNCP ACRLQKCLQA GMNLGARKSK KLGKLKGIHE EQPQQQQPPP 
       710        720        730        740        750
PPPPPQSPEE GTTYIAPAKE PSVNTALVPQ LSTISRALTP SPVMVLENIE 
       760        770        780        790        800
PEIVYAGYDS SKPDTAENLL STLNRLAGKQ MIQVVKWAKV LPGFKNLPLE 
       810        820        830        840        850
DQITLIQYSW MCLSSFALSW RSYKHTNSQF LYFAPDLVFN EEKMHQSAMY 
       860        870        880        890        900
ELCQGMHQIS LQFVRLQLTF EEYTIMKVLL LLSTIPKDGL KSQAAFEEMR 
       910        920        930        940        950
TNYIKELRKM VTKCPNNSGQ SWQRFYQLTK LLDSMHDLVS DLLEFCFYTF 
       960        970        980 
RESHALKVEF PAMLVEIISD QLPKVESGNA KPLYFHRK

Show »

Length:988

Mass (Da):107,586

Checksum:ⁱFDA63FAC05757193

GO

Isoform 4 (identifier: P08235-4) [UniParc]FASTA Add to basket

Also known as: Delta

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

« 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 SVNGGVMRAV VKSPIMCHEK SPSVCSPLNM 
       210        220        230        240        250
TSSVCSPAGI NSVSSTTASF GSFPVHSPIT QGTPLTCSPN VENRGSRSHS 
       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 GGFKNLPLED QITLIQYSWM CLSSFALSWR 
       710        720        730        740        750
SYKHTNSQFL YFAPDLVFNE EKMHQSAMYE LCQGMHQISL QFVRLQLTFE 
       760        770        780        790        800
EYTIMKVLLL LSTIPKDGLK SQAAFEEMRT NYIKELRKMV TKCPNNSGQS 
       810        820        830        840        850
WQRFYQLTKL LDSMHDLVSD LLEFCFYTFR ESHALKVEFP AMLVEIISDQ 
       860 
LPKVESGNAK PLYFHRK

Show »

Length:867

Mass (Da):94,373

Checksum:ⁱ0F5055BFD6337578

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	946	F → I in AAI11759 (PubMed:15489334).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_036063	7	H → Q in a colorectal cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_014623	180	V → I Decreased mineralocorticoid receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs5522EnsemblClinVar.	1
Natural variantⁱVAR_015625	241	V → A Variant of uncertain significance; changed mineralocorticoid receptor activity; changed response curve to aldosterone stimulation. 2 Publications	1
Natural variantⁱVAR_014624	444	N → T1 PublicationCorresponds to variant dbSNP:rs5523EnsemblClinVar.	1
Natural variantⁱVAR_014625	537	R → Q1 PublicationCorresponds to variant dbSNP:rs5526Ensembl.	1
Natural variantⁱVAR_014626	554	N → S1 PublicationCorresponds to variant dbSNP:rs5527EnsemblClinVar.	1
Natural variantⁱVAR_031268	633	G → R in PHA1A; reduces transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912566EnsemblClinVar.	1
Natural variantⁱVAR_031269	645	C → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031270	659	R → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031271	759	P → S in PHA1A. 1 Publication	1
Natural variantⁱVAR_031272	769	L → P in PHA1A. 1 Publication	1
Natural variantⁱVAR_031273	770	N → K in PHA1A. 1 Publication	1
Natural variantⁱVAR_031274	776	Q → R in PHA1A; reduces aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912565EnsemblClinVar.	1
Natural variantⁱVAR_031275	805	S → P in PHA1A. 1 Publication	1
Natural variantⁱVAR_015626	810	S → L in EOHSEP; alters receptor specificity and leads to constitutive activation. 3 PublicationsCorresponds to variant dbSNP:rs41511344EnsemblClinVar.	1
Natural variantⁱVAR_031276	815	S → R in PHA1A. 1 Publication	1
Natural variantⁱVAR_031277	818	S → L in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding. 1 PublicationCorresponds to variant dbSNP:rs121912573EnsemblClinVar.	1
Natural variantⁱVAR_029311	826	F → Y. Corresponds to variant dbSNP:rs13306592Ensembl.	1
Natural variantⁱVAR_015627	924	L → P in PHA1A; abolishes transcription transactivation upon aldosterone binding. 2 PublicationsCorresponds to variant dbSNP:rs121912563EnsemblClinVar.	1
Natural variantⁱVAR_031278	972	E → G in PHA1A; reduces affinity for aldosterone and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912574EnsemblClinVar.	1
Natural variantⁱVAR_031279	979	L → P in PHA1A; loss of aldosterone binding and transcription transactivation. 1 PublicationCorresponds to variant dbSNP:rs121912567EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_007357	633	G → GKCSW in isoform 3. Curated	1
Alternative sequenceⁱVSP_007360	672 – 788	Missing in isoform 4. 2 PublicationsAdd BLAST	117
Alternative sequenceⁱVSP_007358	672 – 706	ARKSK…QSPEE → ERRCISLPCMNYARGCTKSA FSSFDCSSPLKNTPS in isoform 2. 1 PublicationAdd BLAST	35
Alternative sequenceⁱVSP_007359	707 – 984	Missing in isoform 2. 1 PublicationAdd BLAST	278

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3772.1 [P08235-1] CCDS54811.1 [P08235-4]
PIRⁱ	A29513
NCBI Reference Sequences More...RefSeqⁱ	NP_000892.2, NM_000901.4 [P08235-1] NP_001159576.1, NM_001166104.1 [P08235-4] XP_011530277.1, XM_011531975.1 [P08235-3] XP_011530278.1, XM_011531976.2 XP_011530279.1, XM_011531977.2 XP_016863706.1, XM_017008217.1

Genome annotation databases

Ensemblⁱ	ENST00000342437; ENSP00000343907; ENSG00000151623 [P08235-2] ENST00000344721; ENSP00000341390; ENSG00000151623 [P08235-1] ENST00000358102; ENSP00000350815; ENSG00000151623 [P08235-1] ENST00000511528; ENSP00000421481; ENSG00000151623 [P08235-3] ENST00000512865; ENSP00000423510; ENSG00000151623 [P08235-4] ENST00000625323; ENSP00000486719; ENSG00000151623 [P08235-3]
GeneIDⁱ	4306
KEGGⁱ	hsa:4306
UCSC genome browser More...UCSCⁱ	uc003ilk.5, human [P08235-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P08235	Mineralocorticoid receptor		HUMAN		984	UniRef100_P08235
P08235-2	Mineralocorticoid receptor 3		HUMAN		706	UniRef100_B0ZBF8

Protein	Similar proteins		Species	Score	Length	Source
P08235	Mineralocorticoid receptor		AOTNA		984	UniRef90_P08235
Mineralocorticoid receptor		SAISC		982
Mineralocorticoid receptor		HUMAN		984
Uncharacterized protein		NOMLE		988
NR3C2 isoform 2		PANTR		988
+68
P08235-2	Mineralocorticoid receptor 3		HUMAN		706	UniRef90_B0ZBF8
mineralocorticoid receptor		VULVU		864

Protein	Similar proteins		Species	Score	Length	Source
P08235	Mineralocorticoid receptor		AOTNA		984	UniRef50_P08235
Mineralocorticoid receptor		SAISC		982
Mineralocorticoid receptor		TUPBE		977
Mineralocorticoid receptor		SAIBB		982
Mineralocorticoid receptor (Fragment)		XENLA		612
+689
P08235-2	Mineralocorticoid receptor (Fragment)		CHICK		147	UniRef50_Q8QHI2
NR LBD domain-containing protein		CHLGU		145
MCR protein (Fragment)		CATFU		982
Mineralocorticoid receptor (Fragment)		PASDO		181
NR LBD domain-containing protein (Fragment)		CALSU		103
+190

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
CCDSⁱ	CCDS3772.1 [P08235-1] CCDS54811.1 [P08235-4]
PIRⁱ	A29513
RefSeqⁱ	NP_000892.2, NM_000901.4 [P08235-1] NP_001159576.1, NM_001166104.1 [P08235-4] XP_011530277.1, XM_011531975.1 [P08235-3] XP_011530278.1, XM_011531976.2 XP_011530279.1, XM_011531977.2 XP_016863706.1, XM_017008217.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4PF3	X-ray	1.10	A	712-984	[»]
	4TNT	X-ray	2.39	A/B	593-671	[»]
	4UDA	X-ray	2.03	A	735-984	[»]
	4UDB	X-ray	2.36	A	735-984	[»]
	5HCV	X-ray	2.50	A/B/C	732-984	[»]
	5L7E	X-ray	1.86	A	735-984	[»]
	5L7G	X-ray	2.01	A	735-984	[»]
	5L7H	X-ray	1.84	A	735-984	[»]
	5MWP	X-ray	1.82	A	735-984	[»]
	5MWY	X-ray	1.75	A	735-984	[»]
	6GEV	X-ray	1.54	A	735-984	[»]
	6GG8	X-ray	1.80	A	735-984	[»]
	6GGG	X-ray	1.71	A	735-984	[»]
	6L88	X-ray	3.00	A/B/C/D	735-984	[»]
SMRⁱ	P08235
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	110451, 33 interactors
CORUMⁱ	P08235
IntActⁱ	P08235, 7 interactors
STRINGⁱ	9606.ENSP00000350815

Chemistry databases

BindingDBⁱ	P08235
ChEMBLⁱ	CHEMBL1994
DrugBankⁱ	DB04630, Aldosterone DB01013, Clobetasol propionate DB04652, Corticosterone DB06780, Desoxycorticosterone acetate DB01134, Desoxycorticosterone pivalate DB01395, Drospirenone DB00700, Eplerenone DB01023, Felodipine DB00687, Fludrocortisone DB13867, Fluticasone DB08906, Fluticasone furoate DB00588, Fluticasone propionate DB02998, Metribolone DB00393, Nimodipine DB00396, Progesterone DB00421, Spironolactone DB02901, Stanolone DB13951, Stanolone acetate DB00624, Testosterone DB13943, Testosterone cypionate DB13944, Testosterone enanthate DB13946, Testosterone undecanoate
DrugCentralⁱ	P08235
GuidetoPHARMACOLOGYⁱ	626

PTM databases

iPTMnetⁱ	P08235
PhosphoSitePlusⁱ	P08235

Genetic variation databases

BioMutaⁱ	NR3C2
DMDMⁱ	126885

Proteomic databases

jPOSTⁱ	P08235
MassIVEⁱ	P08235
MaxQBⁱ	P08235
PaxDbⁱ	P08235
PeptideAtlasⁱ	P08235
PRIDEⁱ	P08235
ProteomicsDBⁱ	2889 2891 52088 [P08235-1] 52089 [P08235-2] 52090 [P08235-3] 52091 [P08235-4]

Protocols and materials databases

Antibodypediaⁱ	3971, 295 antibodies
The DNASU plasmid repository More...DNASUⁱ	4306

Genome annotation databases

Ensemblⁱ	ENST00000342437; ENSP00000343907; ENSG00000151623 [P08235-2] ENST00000344721; ENSP00000341390; ENSG00000151623 [P08235-1] ENST00000358102; ENSP00000350815; ENSG00000151623 [P08235-1] ENST00000511528; ENSP00000421481; ENSG00000151623 [P08235-3] ENST00000512865; ENSP00000423510; ENSG00000151623 [P08235-4] ENST00000625323; ENSP00000486719; ENSG00000151623 [P08235-3]
GeneIDⁱ	4306
KEGGⁱ	hsa:4306
UCSCⁱ	uc003ilk.5, human [P08235-1]

Organism-specific databases

CTDⁱ	4306
DisGeNETⁱ	4306
GeneCardsⁱ	NR3C2
HGNCⁱ	HGNC:7979, NR3C2
HPAⁱ	ENSG00000151623, Low tissue specificity
MalaCardsⁱ	NR3C2
MIMⁱ	177735, phenotype 600983, gene 605115, phenotype
neXtProtⁱ	NX_P08235
OpenTargetsⁱ	ENSG00000151623
Orphanetⁱ	171871, Renal pseudohypoaldosteronism type 1
PharmGKBⁱ	PA242
VEuPathDBⁱ	HostDB:ENSG00000151623
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3575, Eukaryota
GeneTreeⁱ	ENSGT00940000159333
InParanoidⁱ	P08235
OMAⁱ	CFGPLCS
OrthoDBⁱ	146963at2759
PhylomeDBⁱ	P08235

Enzyme and pathway databases

PathwayCommonsⁱ	P08235
Reactomeⁱ	R-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-383280, Nuclear Receptor transcription pathway R-HSA-4090294, SUMOylation of intracellular receptors
SignaLinkⁱ	P08235
SIGNORⁱ	P08235

Miscellaneous databases

BioGRID-ORCSⁱ	4306, 7 hits in 1038 CRISPR screens
ChiTaRSⁱ	NR3C2, human
EvolutionaryTraceⁱ	P08235
GeneWikiⁱ	Mineralocorticoid_receptor
GenomeRNAiⁱ	4306
Pharosⁱ	P08235, Tclin
Protein Ontology More...PROⁱ	PR:P08235
RNActⁱ	P08235, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000151623, Expressed in colonic mucosa and 231 other tissues
ExpressionAtlasⁱ	P08235, baseline and differential

Family and domain databases

DisProtⁱ	DP01561
Gene3Dⁱ	1.10.565.10, 1 hit 3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR035500, NHR-like_dom_sf IPR000536, Nucl_hrmn_rcpt_lig-bd IPR001628, Znf_hrmn_rcpt IPR013088, Znf_NHR/GATA
Pfamⁱ	View protein in Pfam PF00104, Hormone_recep, 1 hit PF00105, zf-C4, 1 hit
PRINTSⁱ	PR00047, STROIDFINGER
SMARTⁱ	View protein in SMART SM00430, HOLI, 1 hit SM00399, ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508, SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843, NR_LBD, 1 hit PS00031, NUCLEAR_REC_DBD_1, 1 hit PS51030, NUCLEAR_REC_DBD_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MCR_HUMAN
Accessionⁱ	P08235Primary (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:	September 12, 2018
	Last modified:	September 29, 2021
	This is version 231 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P08235 (MCR_HUMAN)

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Mineralocorticoid receptor

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Endoplasmic reticulum

Cytoplasm and Cytosol

Cytosol

Endoplasmic reticulum

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Proteomic databases

Protocols and materials databases

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Organism-specific databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ