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P80365

- DHI2_HUMAN

UniProt

P80365 - DHI2_HUMAN

Protein

Corticosteroid 11-beta-dehydrogenase isozyme 2

Gene

HSD11B2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of cortisol to the inactive metabolite cortisone. Modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids.

    Catalytic activityi

    An 11-beta-hydroxysteroid + NAD+ = an 11-oxosteroid + NADH.

    Enzyme regulationi

    Inhibited by glycyrrhetinic acid (derived from liquorice), carbenoloxone and 11-alpha-OH-progesterone.By similarity

    Kineticsi

    X.

    1. KM=26.1 nM for cortisol2 Publications
    2. KM=785 nM for cortisol2 Publications
    3. KM=77 nM for cortisterone2 Publications

    Vmax=64.1 nmol/h/mg enzyme toward cortisterone2 Publications

    Vmax=66 nmol/h/mg enzyme toward cortisol2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei219 – 2191SubstrateBy similarity
    Active sitei232 – 2321Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi82 – 11130NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Source: Ensembl
    2. NAD binding Source: Ensembl
    3. steroid binding Source: Ensembl

    GO - Biological processi

    1. female pregnancy Source: Ensembl
    2. glucocorticoid biosynthetic process Source: ProtInc
    3. regulation of blood volume by renal aldosterone Source: Ensembl
    4. response to drug Source: Ensembl
    5. response to food Source: Ensembl
    6. response to glucocorticoid Source: Ensembl
    7. response to hypoxia Source: Ensembl
    8. response to insulin Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.1.1.146. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Corticosteroid 11-beta-dehydrogenase isozyme 2 (EC:1.1.1.-)
    Alternative name(s):
    11-beta-hydroxysteroid dehydrogenase type 2
    Short name:
    11-DH2
    Short name:
    11-beta-HSD2
    11-beta-hydroxysteroid dehydrogenase type II
    Short name:
    -HSD11 type II
    NAD-dependent 11-beta-hydroxysteroid dehydrogenase
    Short name:
    11-beta-HSD
    Gene namesi
    Name:HSD11B2
    Synonyms:HSD11K
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:5209. HSD11B2.

    Subcellular locationi

    Microsome 1 Publication. Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Apparent mineralocorticoid excess (AME) [MIM:218030]: An autosomal recessive form of low-renin hypertension. It is usually diagnosed within the first years of life and is characterized by polyuria and polydipsia, failure to thrive, hypernatremia, severe hypertension with low renin and aldosterone levels, profound hypokalemia with metabolic alkalosis, and most often nephrocalcinosis.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1152Missing in AME; reduces enzyme activity by at least 95%.
    VAR_015634
    Natural varianti179 – 1791L → R in AME; abolishes enzyme activity.
    VAR_015635
    Natural varianti180 – 1801S → F in AME; reduces enzyme activity.
    VAR_015636
    Natural varianti186 – 1861R → C in AME. 2 Publications
    VAR_015637
    Natural varianti208 – 2081R → C in AME; reduces enzyme activity by at least 95%. 2 Publications
    VAR_006958
    Natural varianti208 – 2081R → H in AME; abolishes enzyme activity.
    VAR_015638
    Natural varianti213 – 2131R → C in AME; reduces enzyme activity by ca. 90%.
    VAR_006959
    Natural varianti223 – 2231D → N in AME; reduces enzyme activity to about 6% of wild type. 1 Publication
    VAR_066514
    Natural varianti237 – 2371A → V in AME; reduces enzyme activity.
    VAR_015640
    Natural varianti244 – 2441D → N in AME; associated with R-250. 1 Publication
    VAR_015641
    Natural varianti250 – 2512LL → PS in AME; abolishes enzyme activity.
    VAR_015643
    Natural varianti250 – 2501L → R in AME; associated with N-244. 1 Publication
    VAR_015642
    Natural varianti279 – 2791R → C in AME; decreases enzyme activity by ca. 33%.
    VAR_015644
    Natural varianti328 – 3281A → V in AME; abolishes enzyme activity.
    VAR_015645
    Natural varianti337 – 3382RY → H in AME; abolishes enzyme activity. 1 Publication
    VAR_015647
    Natural varianti337 – 3371R → C in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 3 Publications
    VAR_066515
    Natural varianti338 – 3381Y → H in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 1 Publication
    VAR_015646

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi115 – 1151E → K or Q: Abolishes cofactor specificity. 1 Publication
    Mutagenesisi335 – 3351R → A or Q: Reduced enzyme activity. 1 Publication
    Mutagenesisi335 – 3351R → K: No effect on enzyme activity. 1 Publication
    Mutagenesisi336 – 3361R → A or Q: Almost complete loss of enzyme activity. 1 Publication
    Mutagenesisi336 – 3361R → K: Reduced enzyme activity. 1 Publication
    Mutagenesisi337 – 3371R → A or Q: Almost complete loss of enzyme activity. 1 Publication
    Mutagenesisi337 – 3371R → K: Reduced enzyme activity. 1 Publication
    Mutagenesisi338 – 3381Y → F or A: Complete loss of enzyme activity. 1 Publication
    Mutagenesisi339 – 3391Y → A, F or H: Reduced enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi218030. phenotype.
    Orphaneti320. Apparent mineralocorticoid excess.
    PharmGKBiPA29477.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405Corticosteroid 11-beta-dehydrogenase isozyme 2PRO_0000054627Add
    BLAST

    Proteomic databases

    MaxQBiP80365.
    PaxDbiP80365.
    PRIDEiP80365.

    PTM databases

    PhosphoSiteiP80365.

    Expressioni

    Tissue specificityi

    Found in placenta, kidney, pancreas, prostate, ovary, small intestine and colon.

    Gene expression databases

    ArrayExpressiP80365.
    BgeeiP80365.
    CleanExiHS_HSD11B2.
    GenevestigatoriP80365.

    Organism-specific databases

    HPAiCAB032443.

    Interactioni

    Subunit structurei

    Interacts with ligand-free cytoplasmic NR3C2.1 Publication

    Protein-protein interaction databases

    BioGridi109524. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP80365.
    SMRiP80365. Positions 81-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni335 – 3395Essential for protein stability

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG005482.
    InParanoidiP80365.
    KOiK00071.
    OMAiCFKTESV.
    OrthoDBiEOG7FXZZX.
    PhylomeDBiP80365.
    TreeFamiTF325617.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P80365-1 [UniParc]FASTAAdd to Basket

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    MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR    50
    LLPPPAALAV LAAAGWIALS RLARPQRLPV ATRAVLITGC DSGFGKETAK 100
    KLDSMGFTVL ATVLELNSPG AIELRTCCSP RLRLLQMDLT KPGDISRVLE 150
    FTKAHTTSTG LWGLVNNAGH NEVVADAELS PVATFRSCME VNFFGALELT 200
    KGLLPLLRSS RGRIVTVGSP AGDMPYPCLG AYGTSKAAVA LLMDTFSCEL 250
    LPWGVKVSII QPGCFKTESV RNVGQWEKRK QLLLANLPQE LLQAYGKDYI 300
    EHLHGQFLHS LRLAMSDLTP VVDAITDALL AARPRRRYYP GQGLGLMYFI 350
    HYYLPEGLRR RFLQAFFISH CLPRALQPGQ PGTTPPQDAA QDPNLSPGPS 400
    PAVAR 405
    Length:405
    Mass (Da):44,127
    Last modified:April 30, 2003 - v2
    Checksum:i4AB269E269982D24
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti148 – 1481V → F in AAB48544. (PubMed:8530071)Curated
    Sequence conflicti148 – 1481V → L in AAA91969. (PubMed:7859916)Curated
    Sequence conflicti350 – 3501I → T in AAH64536. (PubMed:15489334)Curated
    Sequence conflicti392 – 3921D → G in AAH36780. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1152Missing in AME; reduces enzyme activity by at least 95%.
    VAR_015634
    Natural varianti147 – 1471R → H.
    Corresponds to variant rs13306425 [ dbSNP | Ensembl ].
    VAR_052317
    Natural varianti179 – 1791L → R in AME; abolishes enzyme activity.
    VAR_015635
    Natural varianti180 – 1801S → F in AME; reduces enzyme activity.
    VAR_015636
    Natural varianti186 – 1861R → C in AME. 2 Publications
    VAR_015637
    Natural varianti208 – 2081R → C in AME; reduces enzyme activity by at least 95%. 2 Publications
    VAR_006958
    Natural varianti208 – 2081R → H in AME; abolishes enzyme activity.
    VAR_015638
    Natural varianti213 – 2131R → C in AME; reduces enzyme activity by ca. 90%.
    VAR_006959
    Natural varianti223 – 2231D → N in AME; reduces enzyme activity to about 6% of wild type. 1 Publication
    VAR_066514
    Natural varianti227 – 2271P → L in hypertension; decreases affinity for cortisol.
    VAR_015639
    Natural varianti237 – 2371A → V in AME; reduces enzyme activity.
    VAR_015640
    Natural varianti244 – 2441D → N in AME; associated with R-250. 1 Publication
    VAR_015641
    Natural varianti250 – 2512LL → PS in AME; abolishes enzyme activity.
    VAR_015643
    Natural varianti250 – 2501L → R in AME; associated with N-244. 1 Publication
    VAR_015642
    Natural varianti279 – 2791R → C in AME; decreases enzyme activity by ca. 33%.
    VAR_015644
    Natural varianti328 – 3281A → V in AME; abolishes enzyme activity.
    VAR_015645
    Natural varianti337 – 3382RY → H in AME; abolishes enzyme activity. 1 Publication
    VAR_015647
    Natural varianti337 – 3371R → C in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 3 Publications
    VAR_066515
    Natural varianti338 – 3381Y → H in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway. 1 Publication
    VAR_015646

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14631 mRNA. Translation: AAA91969.1.
    U27317 Genomic DNA. Translation: AAB48544.1.
    U26726 mRNA. Translation: AAC50356.1.
    EF694683 Genomic DNA. Translation: ABS29267.1.
    FJ515828 Genomic DNA. Translation: ACS13714.1.
    CH471092 Genomic DNA. Translation: EAW83134.1.
    BC036780 mRNA. Translation: AAH36780.1.
    BC064536 mRNA. Translation: AAH64536.1.
    AY046280 Genomic DNA. Translation: AAK91586.1.
    CCDSiCCDS10837.1.
    PIRiS62789.
    RefSeqiNP_000187.3. NM_000196.3.
    UniGeneiHs.1376.

    Genome annotation databases

    EnsembliENST00000326152; ENSP00000316786; ENSG00000176387.
    GeneIDi3291.
    KEGGihsa:3291.
    UCSCiuc002etd.3. human.

    Polymorphism databases

    DMDMi30316367.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14631 mRNA. Translation: AAA91969.1 .
    U27317 Genomic DNA. Translation: AAB48544.1 .
    U26726 mRNA. Translation: AAC50356.1 .
    EF694683 Genomic DNA. Translation: ABS29267.1 .
    FJ515828 Genomic DNA. Translation: ACS13714.1 .
    CH471092 Genomic DNA. Translation: EAW83134.1 .
    BC036780 mRNA. Translation: AAH36780.1 .
    BC064536 mRNA. Translation: AAH64536.1 .
    AY046280 Genomic DNA. Translation: AAK91586.1 .
    CCDSi CCDS10837.1.
    PIRi S62789.
    RefSeqi NP_000187.3. NM_000196.3.
    UniGenei Hs.1376.

    3D structure databases

    ProteinModelPortali P80365.
    SMRi P80365. Positions 81-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109524. 4 interactions.

    Chemistry

    BindingDBi P80365.
    ChEMBLi CHEMBL3746.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P80365.

    Polymorphism databases

    DMDMi 30316367.

    Proteomic databases

    MaxQBi P80365.
    PaxDbi P80365.
    PRIDEi P80365.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326152 ; ENSP00000316786 ; ENSG00000176387 .
    GeneIDi 3291.
    KEGGi hsa:3291.
    UCSCi uc002etd.3. human.

    Organism-specific databases

    CTDi 3291.
    GeneCardsi GC16P067465.
    HGNCi HGNC:5209. HSD11B2.
    HPAi CAB032443.
    MIMi 218030. phenotype.
    614232. gene.
    neXtProti NX_P80365.
    Orphaneti 320. Apparent mineralocorticoid excess.
    PharmGKBi PA29477.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG005482.
    InParanoidi P80365.
    KOi K00071.
    OMAi CFKTESV.
    OrthoDBi EOG7FXZZX.
    PhylomeDBi P80365.
    TreeFami TF325617.

    Enzyme and pathway databases

    BRENDAi 1.1.1.146. 2681.

    Miscellaneous databases

    ChiTaRSi HSD11B2. human.
    GeneWikii Corticosteroid_11-beta-dehydrogenase_isozyme_2.
    GenomeRNAii 3291.
    NextBioi 13055.
    PROi P80365.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P80365.
    Bgeei P80365.
    CleanExi HS_HSD11B2.
    Genevestigatori P80365.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and tissue distribution of the human 11 beta-hydroxysteroid dehydrogenase type 2 enzyme."
      Albiston A.L., Obeyesekere V.R., Smith R.E., Krozowski Z.S.
      Mol. Cell. Endocrinol. 105:R11-R17(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Gene structure and chromosomal localization of the human HSD11K gene encoding the kidney (type 2) isozyme of 11 beta-hydroxysteroid dehydrogenase."
      Agarwal A.K., Rogerson F.M., Mune T., White P.C.
      Genomics 29:195-199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Kidney.
    3. "Cloning and production of antisera to human placental 11 beta-hydroxysteroid dehydrogenase type 2."
      Brown R.W., Chapman K.E., Kotelevtsev Y., Yau J.L., Lindsay R.S., Brett L., Leckie C., Murad P., Lyons V., Mullins J.J., Edwards C.R.W., Seckl J.R.
      Biochem. J. 313:1007-1017(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. SeattleSNPs variation discovery resource
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Ovary.
    8. "Purification of 11 beta-hydroxysteroid dehydrogenase type 2 from human placenta utilizing a novel affinity labelling technique."
      Brown R.W., Chapman K.E., Murad P., Edwards C.R., Seckl J.R.
      Biochem. J. 313:997-1005(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-24; 77-84; 102-112; 134-154; 191-198; 214-227; 229-235; 256-266; 272-278 AND 375-401.
      Tissue: Placenta.
    9. "Human hydroxysteroid dehydrogenase type 2 HSD11B2."
      Amin H.K., Hoeppner W.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-221.
    10. "Several homozygous mutations in the gene for 11 beta-hydroxysteroid dehydrogenase type 2 in patients with apparent mineralocorticoid excess."
      Wilson R.C., Harbison M.D., Krozowski Z.S., Funder J.W., Shackleton C.H.L., Hanauske-Abel H.M., Wei J.-Q., Hertecant J., Moran A., Neiberger R.E., Balfe J.W., Fattah A., Daneman D., Licholai T., New M.I.
      J. Clin. Endocrinol. Metab. 80:3145-3150(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-211; 235-264 AND 325-354, VARIANTS AME CYS-186; CYS-208; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS.
    11. "Mineralocorticoid activity of liquorice: 11-beta-hydroxysteroid dehydrogenase deficiency comes of age."
      Stewart P.M., Wallace A.M., Valentino R., Burt D., Shackleton C.H.L., Edwards C.R.W.
      Lancet 2:821-824(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    12. "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: INTERACTION WITH NR3C2.
    13. Cited for: VARIANT AME CYS-337.
    14. "Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase."
      Mune T., Rogerson F.M., Nikkilae H., Agarwal A.K., White P.C.
      Nat. Genet. 10:394-399(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS AME CYS-208; CYS-213; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS.
    15. "A new compound heterozygous mutation in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent mineralocorticoid excess."
      Kitanaka S., Katsumata N., Tanae A., Hibi I., Takeyama K., Fuse H., Kato S., Tanaka T.
      J. Clin. Endocrinol. Metab. 82:4054-4058(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS AME HIS-208 AND 337-ARG-TYR-338 DELINS HIS.
    16. "Molecular basis for hypertension in the 'type II variant' of apparent mineralocorticoid excess."
      Li A., Tedde R., Krozowski Z.S., Pala A., Li K.X.Z., Shackleton C.H.L., Mantero F., Palermo M., Stewart P.M.
      Am. J. Hum. Genet. 63:370-379(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT AME CYS-279.
    17. Cited for: VARIANTS AME CYS-186; CYS-208; ASN-244; ARG-250; 250-PRO-SER-251; CYS-337 AND 337-ARG-TYR-338 DELINS HIS.
    18. "The codon 213 of the 11beta-hydroxysteroid dehydrogenase type 2 gene is a hot spot for mutations in apparent mineralocorticoid excess."
      Rogoff D., Smolenicka Z., Bergada I., Vallejo G., Barontini M., Heinrich J.J., Ferrari P.
      J. Clin. Endocrinol. Metab. 83:4391-4393(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT AME CYS-213.
    19. Cited for: CHARACTERIZATION OF VARIANT HYPERTENSION LEU-227.
    20. "Genetic, biochemical, and clinical studies of patients with A328V or R213C mutations in 11betaHSD2 causing apparent mineralocorticoid excess."
      Morineau G., Marc J.-M., Boudi A., Galons H., Gourmelen M., Corvol P., Pascoe L., Fiet J.
      Hypertension 34:435-441(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS AME CYS-213 AND VAL-328.
    21. "Mutants of 11beta-hydroxysteroid dehydrogenase (11-HSD2) with partial activity: improved correlations between genotype and biochemical phenotype in apparent mineralocorticoid excess."
      Nunez B.S., Rogerson F.M., Mune T., Igarashi Y., Nakagawa Y., Phillipov G., Moudgil A., Travis L.B., Palermo M., Shackleton C.H.L., White P.C.
      Hypertension 34:638-642(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS AME ARG-179; PHE-180; HIS-208; VAL-237 AND VAL-328.
    22. "A mutation in the cofactor-binding domain of 11beta-hydroxysteroid dehydrogenase type 2 associated with mineralocorticoid hypertension."
      Odermatt A., Dick B., Arnold P., Zaehner T., Plueschke V., Deregibus M.N., Repetto H., Frey B.M., Frey F.J., Ferrari P.
      J. Clin. Endocrinol. Metab. 86:1247-1252(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT AME 114-LEU-GLU-115 DEL, MUTAGENESIS OF GLU-115.
    23. "Two homozygous mutations in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent mineralocorticoid excess."
      Carvajal C.A., Gonzalez A.A., Romero D.G., Gonzalez A., Mosso L.M., Lagos E.T., Hevia Mdel P., Rosati M.P., Perez-Acle T.O., Gomez-Sanchez C.E., Montero J.A., Fardella C.E.
      J. Clin. Endocrinol. Metab. 88:2501-2507(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AME ASN-223, BIOPHYSICOCHEMICAL PROPERTIES.
    24. "Impaired protein stability of 11beta-hydroxysteroid dehydrogenase type 2: a novel mechanism of apparent mineralocorticoid excess."
      Atanasov A.G., Ignatova I.D., Nashev L.G., Dick B., Ferrari P., Frey F.J., Odermatt A.
      J. Am. Soc. Nephrol. 18:1262-1270(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AME CYS-337 AND HIS-338, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; ARG-336; ARG-337; TYR-338 AND TYR-339.

    Entry informationi

    Entry nameiDHI2_HUMAN
    AccessioniPrimary (citable) accession number: P80365
    Secondary accession number(s): A7LB28
    , C5HTY7, Q13194, Q6P2G9, Q8N439, Q96QN8, Q9UC50, Q9UC51, Q9UCW5, Q9UCW6, Q9UCW7, Q9UCW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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

    Miscellaneous

    Consumption of large amounts of liquorice can lead to apparent mineralocorticoid excess and hypertension.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3