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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 2

Gene

HSD11B2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  1. KM=26.1 nM for cortisol2 Publications
  2. KM=785 nM for cortisol2 Publications
  3. KM=77 nM for cortisterone2 Publications
  1. Vmax=64.1 nmol/h/mg enzyme toward cortisterone2 Publications
  2. 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.B40. 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:
11-HSD type II
Short name:
11-beta-HSD type II
NAD-dependent 11-beta-hydroxysteroid dehydrogenase
Short name:
11-beta-HSD
Short chain dehydrogenase/reductase family 9C member 3
Gene namesi
Name:HSD11B2
Synonyms:HSD11K1 Publication, SDR9C3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:5209. HSD11B2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

Pathology & Biotechi

Involvement in diseasei

Apparent mineralocorticoid excess (AME)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:218030
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1152Missing in AME; reduces enzyme activity by at least 95%. 1 Publication
VAR_015634
Natural varianti179 – 1791L → R in AME; abolishes enzyme activity. 1 Publication
VAR_015635
Natural varianti180 – 1801S → F in AME; reduces enzyme activity. 1 Publication
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%. 3 Publications
VAR_006958
Natural varianti208 – 2081R → H in AME; abolishes enzyme activity. 2 Publications
VAR_015638
Natural varianti213 – 2131R → C in AME; reduces enzyme activity by ca. 90%. 3 Publications
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. 1 Publication
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%. 1 Publication
VAR_015644
Natural varianti328 – 3281A → V in AME; abolishes enzyme activity. 2 Publications
VAR_015645
Natural varianti337 – 3382RY → H in AME; abolishes enzyme activity. 4 Publications
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.

Polymorphism and mutation databases

BioMutaiHSD11B2.
DMDMi30316367.

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

Expressed in kidney, pancreas, prostate, ovary, small intestine and colon. At midgestation, expressed at high levels in placenta and in fetal kidney and, at much lower levels, in fetal lung and testis (PubMed:8530071).1 Publication

Gene expression databases

BgeeiP80365.
CleanExiHS_HSD11B2.
ExpressionAtlasiP80365. baseline and differential.
GenevisibleiP80365. HS.

Organism-specific databases

HPAiCAB032443.
HPA042186.
HPA056385.

Interactioni

Subunit structurei

Interacts with ligand-free cytoplasmic NR3C2.1 Publication

Protein-protein interaction databases

BioGridi109524. 4 interactions.
STRINGi9606.ENSP00000316786.

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.
GeneTreeiENSGT00800000124016.
HOVERGENiHBG005482.
InParanoidiP80365.
KOiK00071.
OMAiERWPWPS.
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

« Hide

        10         20         30         40         50
MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR
60 70 80 90 100
LLPPPAALAV LAAAGWIALS RLARPQRLPV ATRAVLITGC DSGFGKETAK
110 120 130 140 150
KLDSMGFTVL ATVLELNSPG AIELRTCCSP RLRLLQMDLT KPGDISRVLE
160 170 180 190 200
FTKAHTTSTG LWGLVNNAGH NEVVADAELS PVATFRSCME VNFFGALELT
210 220 230 240 250
KGLLPLLRSS RGRIVTVGSP AGDMPYPCLG AYGTSKAAVA LLMDTFSCEL
260 270 280 290 300
LPWGVKVSII QPGCFKTESV RNVGQWEKRK QLLLANLPQE LLQAYGKDYI
310 320 330 340 350
EHLHGQFLHS LRLAMSDLTP VVDAITDALL AARPRRRYYP GQGLGLMYFI
360 370 380 390 400
HYYLPEGLRR RFLQAFFISH CLPRALQPGQ PGTTPPQDAA QDPNLSPGPS

PAVAR
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%. 1 Publication
VAR_015634
Natural varianti147 – 1471R → H.
Corresponds to variant rs13306425 [ dbSNP | Ensembl ].
VAR_052317
Natural varianti179 – 1791L → R in AME; abolishes enzyme activity. 1 Publication
VAR_015635
Natural varianti180 – 1801S → F in AME; reduces enzyme activity. 1 Publication
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%. 3 Publications
VAR_006958
Natural varianti208 – 2081R → H in AME; abolishes enzyme activity. 2 Publications
VAR_015638
Natural varianti213 – 2131R → C in AME; reduces enzyme activity by ca. 90%. 3 Publications
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. 1 Publication
VAR_015639
Natural varianti237 – 2371A → V in AME; reduces enzyme activity. 1 Publication
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%. 1 Publication
VAR_015644
Natural varianti328 – 3281A → V in AME; abolishes enzyme activity. 2 Publications
VAR_015645
Natural varianti337 – 3382RY → H in AME; abolishes enzyme activity. 4 Publications
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109524. 4 interactions.
STRINGi9606.ENSP00000316786.

Chemistry

BindingDBiP80365.
ChEMBLiCHEMBL3746.

PTM databases

PhosphoSiteiP80365.

Polymorphism and mutation databases

BioMutaiHSD11B2.
DMDMi30316367.

Proteomic databases

MaxQBiP80365.
PaxDbiP80365.
PRIDEiP80365.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3291.
GeneCardsiGC16P067465.
HGNCiHGNC:5209. HSD11B2.
HPAiCAB032443.
HPA042186.
HPA056385.
MIMi218030. phenotype.
614232. gene.
neXtProtiNX_P80365.
Orphaneti320. Apparent mineralocorticoid excess.
PharmGKBiPA29477.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00800000124016.
HOVERGENiHBG005482.
InParanoidiP80365.
KOiK00071.
OMAiERWPWPS.
OrthoDBiEOG7FXZZX.
PhylomeDBiP80365.
TreeFamiTF325617.

Enzyme and pathway databases

BRENDAi1.1.1.B40. 2681.

Miscellaneous databases

ChiTaRSiHSD11B2. human.
GeneWikiiCorticosteroid_11-beta-dehydrogenase_isozyme_2.
GenomeRNAii3291.
NextBioi13055.
PROiP80365.
SOURCEiSearch...

Gene expression databases

BgeeiP80365.
CleanExiHS_HSD11B2.
ExpressionAtlasiP80365. baseline and differential.
GenevisibleiP80365. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 SPECIFICITY.
    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: July 22, 2015
This is version 148 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

Similar proteinsi

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