Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Corticosteroid 11-beta-dehydrogenase isozyme 2 (EC 1.1.1.-) (11-beta-hydroxysteroid dehydrogenase type 2) (11-DH2) (11-beta-HSD2) (11-beta-hydroxysteroid dehydrogenase type II) (11-HSD type II) (11-beta-HSD type II) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase) (11-beta-HSD) (Short chain dehydrogenase/reductase family 9C member 3)

 DHI2_HUMAN              Reviewed;         405 AA.
P80365; A7LB28; C5HTY7; Q13194; Q6P2G9; Q8N439; Q96QN8; Q9UC50;
Q9UC51; Q9UCW5; Q9UCW6; Q9UCW7; Q9UCW8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
30-APR-2003, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 2;
EC=1.1.1.-;
AltName: Full=11-beta-hydroxysteroid dehydrogenase type 2;
Short=11-DH2;
Short=11-beta-HSD2;
AltName: Full=11-beta-hydroxysteroid dehydrogenase type II;
Short=11-HSD type II;
Short=11-beta-HSD type II;
AltName: Full=NAD-dependent 11-beta-hydroxysteroid dehydrogenase;
Short=11-beta-HSD;
AltName: Full=Short chain dehydrogenase/reductase family 9C member 3;
Name=HSD11B2; Synonyms=HSD11K {ECO:0000303|PubMed:8530071}, SDR9C3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=7859916; DOI=10.1016/0303-7207(94)90176-7;
Albiston A.L., Obeyesekere V.R., Smith R.E., Krozowski Z.S.;
"Cloning and tissue distribution of the human 11 beta-hydroxysteroid
dehydrogenase type 2 enzyme.";
Mol. Cell. Endocrinol. 105:R11-R17(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8530071; DOI=10.1006/geno.1995.1231;
Agarwal A.K., Rogerson F.M., Mune T., White P.C.;
"Gene structure and chromosomal localization of the human HSD11K gene
encoding the kidney (type 2) isozyme of 11 beta-hydroxysteroid
dehydrogenase.";
Genomics 29:195-199(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8611140; DOI=10.1042/bj3131007;
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.;
"Cloning and production of antisera to human placental 11 beta-
hydroxysteroid dehydrogenase type 2.";
Biochem. J. 313:1007-1017(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
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;
PubMed=8611186; DOI=10.1042/bj3130997;
Brown R.W., Chapman K.E., Murad P., Edwards C.R., Seckl J.R.;
"Purification of 11 beta-hydroxysteroid dehydrogenase type 2 from
human placenta utilizing a novel affinity labelling technique.";
Biochem. J. 313:997-1005(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-221.
Amin H.K., Hoeppner W.;
"Human hydroxysteroid dehydrogenase type 2 HSD11B2.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-211; 235-264 AND 325-354, AND
VARIANTS AME CYS-186; CYS-208; 250-PRO-SER-251 AND 337-ARG-TYR-338
DELINS HIS.
PubMed=7593417; DOI=10.1210/jcem.80.11.7593417;
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.;
"Several homozygous mutations in the gene for 11 beta-hydroxysteroid
dehydrogenase type 2 in patients with apparent mineralocorticoid
excess.";
J. Clin. Endocrinol. Metab. 80:3145-3150(1995).
[11]
CHARACTERIZATION.
PubMed=2889032; DOI=10.1016/S0140-6736(87)91014-2;
Stewart P.M., Wallace A.M., Valentino R., Burt D., Shackleton C.H.L.,
Edwards C.R.W.;
"Mineralocorticoid activity of liquorice: 11-beta-hydroxysteroid
dehydrogenase deficiency comes of age.";
Lancet 2:821-824(1987).
[12]
INTERACTION WITH NR3C2.
PubMed=11350956; DOI=10.1074/jbc.M100374200;
Odermatt A., Arnold P., Frey F.J.;
"The intracellular localization of the mineralocorticoid receptor is
regulated by 11beta-hydroxysteroid dehydrogenase type 2.";
J. Biol. Chem. 276:28484-28492(2001).
[13]
VARIANT AME CYS-337.
PubMed=7608290; DOI=10.1210/jcem.80.7.7608290;
Wilson R.C., Krozowski Z.S., Li K., Obeyesekere V.R.,
Razzaghy-Azar M., Harbison M.D., Wei J.-Q., Shackleton C.H.L.,
Funder J.W., New M.I.;
"A mutation in the HSD11B2 gene in a family with apparent
mineralocorticoid excess.";
J. Clin. Endocrinol. Metab. 80:2263-2266(1995).
[14]
CHARACTERIZATION OF VARIANTS AME CYS-208; CYS-213; 250-PRO-SER-251 AND
337-ARG-TYR-338 DELINS HIS.
PubMed=7670488; DOI=10.1038/ng0895-394;
Mune T., Rogerson F.M., Nikkilae H., Agarwal A.K., White P.C.;
"Human hypertension caused by mutations in the kidney isozyme of 11
beta-hydroxysteroid dehydrogenase.";
Nat. Genet. 10:394-399(1995).
[15]
CHARACTERIZATION OF VARIANTS AME HIS-208 AND 337-ARG-TYR-338 DELINS
HIS.
PubMed=9398712; DOI=10.1210/jcem.82.12.4455;
Kitanaka S., Katsumata N., Tanae A., Hibi I., Takeyama K., Fuse H.,
Kato S., Tanaka T.;
"A new compound heterozygous mutation in the 11 beta-hydroxysteroid
dehydrogenase type 2 gene in a case of apparent mineralocorticoid
excess.";
J. Clin. Endocrinol. Metab. 82:4054-4058(1997).
[16]
CHARACTERIZATION OF VARIANT AME CYS-279.
PubMed=9683587; DOI=10.1086/301955;
Li A., Tedde R., Krozowski Z.S., Pala A., Li K.X.Z.,
Shackleton C.H.L., Mantero F., Palermo M., Stewart P.M.;
"Molecular basis for hypertension in the 'type II variant' of apparent
mineralocorticoid excess.";
Am. J. Hum. Genet. 63:370-379(1998).
[17]
VARIANTS AME CYS-186; CYS-208; ASN-244; ARG-250; 250-PRO-SER-251;
CYS-337 AND 337-ARG-TYR-338 DELINS HIS.
PubMed=9661590; DOI=10.1210/jcem.83.7.4986;
Dave-Sharma S., Wilson R.C., Harbison M.D., Newfield R., Azar M.R.,
Krozowski Z.S., Funder J.W., Shackleton C.H.L., Bradlow H.L.,
Wei J.-Q., Hertecant J., Moran A., Neiberger R.E., Balfe J.W.,
Fattah A., Daneman D., Akkurt H.I., De Santis C., New M.I.;
"Examination of genotype and phenotype relationships in 14 patients
with apparent mineralocorticoid excess.";
J. Clin. Endocrinol. Metab. 83:2244-2254(1998).
[18]
CHARACTERIZATION OF VARIANT AME CYS-213.
PubMed=9851783; DOI=10.1210/jcem.83.12.5329;
Rogoff D., Smolenicka Z., Bergada I., Vallejo G., Barontini M.,
Heinrich J.J., Ferrari P.;
"The codon 213 of the 11beta-hydroxysteroid dehydrogenase type 2 gene
is a hot spot for mutations in apparent mineralocorticoid excess.";
J. Clin. Endocrinol. Metab. 83:4391-4393(1998).
[19]
CHARACTERIZATION OF VARIANT HYPERTENSION LEU-227.
PubMed=9707624; DOI=10.1073/pnas.95.17.10200;
Wilson R.C., Dave-Sharma S., Wei J.-Q., Obeyesekere V.R., Li K.,
Ferrari P., Krozowski Z.S., Shackleton C.H.L., Bradlow L., Wiens T.,
New M.I.;
"A genetic defect resulting in mild low-renin hypertension.";
Proc. Natl. Acad. Sci. U.S.A. 95:10200-10205(1998).
[20]
CHARACTERIZATION OF VARIANTS AME CYS-213 AND VAL-328.
PubMed=10489390; DOI=10.1161/01.HYP.34.3.435;
Morineau G., Marc J.-M., Boudi A., Galons H., Gourmelen M., Corvol P.,
Pascoe L., Fiet J.;
"Genetic, biochemical, and clinical studies of patients with A328V or
R213C mutations in 11betaHSD2 causing apparent mineralocorticoid
excess.";
Hypertension 34:435-441(1999).
[21]
CHARACTERIZATION OF VARIANTS AME ARG-179; PHE-180; HIS-208; VAL-237
AND VAL-328.
PubMed=10523339; DOI=10.1161/01.HYP.34.4.638;
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.;
"Mutants of 11beta-hydroxysteroid dehydrogenase (11-HSD2) with partial
activity: improved correlations between genotype and biochemical
phenotype in apparent mineralocorticoid excess.";
Hypertension 34:638-642(1999).
[22]
CHARACTERIZATION OF VARIANT AME 114-LEU-GLU-115 DEL, AND MUTAGENESIS
OF GLU-115.
PubMed=11238516; DOI=10.1210/jcem.86.3.7334;
Odermatt A., Dick B., Arnold P., Zaehner T., Plueschke V.,
Deregibus M.N., Repetto H., Frey B.M., Frey F.J., Ferrari P.;
"A mutation in the cofactor-binding domain of 11beta-hydroxysteroid
dehydrogenase type 2 associated with mineralocorticoid hypertension.";
J. Clin. Endocrinol. Metab. 86:1247-1252(2001).
[23]
VARIANT AME ASN-223, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12788846; DOI=10.1210/jc.2002-021909;
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.;
"Two homozygous mutations in the 11 beta-hydroxysteroid dehydrogenase
type 2 gene in a case of apparent mineralocorticoid excess.";
J. Clin. Endocrinol. Metab. 88:2501-2507(2003).
[24]
VARIANTS AME CYS-337 AND HIS-338, SUBCELLULAR LOCATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-335; ARG-336;
ARG-337; TYR-338 AND TYR-339.
PubMed=17314322; DOI=10.1681/ASN.2006111235;
Atanasov A.G., Ignatova I.D., Nashev L.G., Dick B., Ferrari P.,
Frey F.J., Odermatt A.;
"Impaired protein stability of 11beta-hydroxysteroid dehydrogenase
type 2: a novel mechanism of apparent mineralocorticoid excess.";
J. Am. Soc. Nephrol. 18:1262-1270(2007).
-!- FUNCTION: 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 ACTIVITY: An 11-beta-hydroxysteroid + NAD(+) = an 11-
oxosteroid + NADH.
-!- ENZYME REGULATION: Inhibited by glycyrrhetinic acid (derived from
liquorice), carbenoloxone and 11-alpha-OH-progesterone.
{ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=26.1 nM for cortisol {ECO:0000269|PubMed:12788846,
ECO:0000269|PubMed:17314322};
KM=785 nM for cortisol {ECO:0000269|PubMed:12788846,
ECO:0000269|PubMed:17314322};
KM=77 nM for cortisterone {ECO:0000269|PubMed:12788846,
ECO:0000269|PubMed:17314322};
Vmax=64.1 nmol/h/mg enzyme toward cortisterone
{ECO:0000269|PubMed:12788846, ECO:0000269|PubMed:17314322};
Vmax=66 nmol/h/mg enzyme toward cortisol
{ECO:0000269|PubMed:12788846, ECO:0000269|PubMed:17314322};
-!- SUBUNIT: Interacts with ligand-free cytoplasmic NR3C2.
{ECO:0000269|PubMed:11350956}.
-!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:17314322}.
Endoplasmic reticulum {ECO:0000269|PubMed:17314322}.
-!- TISSUE SPECIFICITY: 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).
{ECO:0000269|PubMed:8530071}.
-!- DISEASE: 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. {ECO:0000269|PubMed:10489390,
ECO:0000269|PubMed:10523339, ECO:0000269|PubMed:11238516,
ECO:0000269|PubMed:12788846, ECO:0000269|PubMed:17314322,
ECO:0000269|PubMed:7593417, ECO:0000269|PubMed:7608290,
ECO:0000269|PubMed:7670488, ECO:0000269|PubMed:9398712,
ECO:0000269|PubMed:9661590, ECO:0000269|PubMed:9683587,
ECO:0000269|PubMed:9851783}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Consumption of large amounts of liquorice can lead
to apparent mineralocorticoid excess and hypertension.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U14631; AAA91969.1; -; mRNA.
EMBL; U27317; AAB48544.1; -; Genomic_DNA.
EMBL; U26726; AAC50356.1; -; mRNA.
EMBL; EF694683; ABS29267.1; -; Genomic_DNA.
EMBL; FJ515828; ACS13714.1; -; Genomic_DNA.
EMBL; CH471092; EAW83134.1; -; Genomic_DNA.
EMBL; BC036780; AAH36780.1; -; mRNA.
EMBL; BC064536; AAH64536.1; -; mRNA.
EMBL; AY046280; AAK91586.1; -; Genomic_DNA.
CCDS; CCDS10837.1; -.
PIR; S62789; S62789.
RefSeq; NP_000187.3; NM_000196.3.
UniGene; Hs.1376; -.
ProteinModelPortal; P80365; -.
SMR; P80365; -.
BioGrid; 109524; 4.
STRING; 9606.ENSP00000316786; -.
BindingDB; P80365; -.
ChEMBL; CHEMBL3746; -.
DrugBank; DB01569; Formebolone.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000810; -.
iPTMnet; P80365; -.
PhosphoSitePlus; P80365; -.
BioMuta; HSD11B2; -.
DMDM; 30316367; -.
EPD; P80365; -.
MaxQB; P80365; -.
PaxDb; P80365; -.
PeptideAtlas; P80365; -.
PRIDE; P80365; -.
Ensembl; ENST00000326152; ENSP00000316786; ENSG00000176387.
GeneID; 3291; -.
KEGG; hsa:3291; -.
UCSC; uc002etd.4; human.
CTD; 3291; -.
DisGeNET; 3291; -.
EuPathDB; HostDB:ENSG00000176387.6; -.
GeneCards; HSD11B2; -.
HGNC; HGNC:5209; HSD11B2.
HPA; CAB032443; -.
HPA; HPA042186; -.
HPA; HPA056385; -.
MalaCards; HSD11B2; -.
MIM; 218030; phenotype.
MIM; 614232; gene.
neXtProt; NX_P80365; -.
OpenTargets; ENSG00000176387; -.
Orphanet; 320; Apparent mineralocorticoid excess.
PharmGKB; PA29477; -.
eggNOG; KOG1610; Eukaryota.
eggNOG; ENOG410Y7FK; LUCA.
GeneTree; ENSGT00900000140775; -.
HOVERGEN; HBG005482; -.
InParanoid; P80365; -.
KO; K00071; -.
OMA; LQAYGED; -.
OrthoDB; EOG091G0LMI; -.
PhylomeDB; P80365; -.
TreeFam; TF325617; -.
BRENDA; 1.1.1.B40; 2681.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
SABIO-RK; P80365; -.
SIGNOR; P80365; -.
ChiTaRS; HSD11B2; human.
GeneWiki; Corticosteroid_11-beta-dehydrogenase_isozyme_2; -.
GenomeRNAi; 3291; -.
PRO; PR:P80365; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000176387; -.
CleanEx; HS_HSD11B2; -.
ExpressionAtlas; P80365; baseline and differential.
Genevisible; P80365; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0003845; F:11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity; TAS:Reactome.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0005496; F:steroid binding; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0002017; P:regulation of blood volume by renal aldosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disease mutation;
Endoplasmic reticulum; Microsome; NAD; Oxidoreductase; Polymorphism;
Reference proteome.
CHAIN 1 405 Corticosteroid 11-beta-dehydrogenase
isozyme 2.
/FTId=PRO_0000054627.
NP_BIND 82 111 NAD. {ECO:0000250}.
REGION 335 339 Essential for protein stability.
ACT_SITE 232 232 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 219 219 Substrate. {ECO:0000250}.
VARIANT 114 115 Missing (in AME; reduces enzyme activity
by at least 95%).
{ECO:0000269|PubMed:11238516}.
/FTId=VAR_015634.
VARIANT 147 147 R -> H (in dbSNP:rs13306425).
/FTId=VAR_052317.
VARIANT 179 179 L -> R (in AME; abolishes enzyme
activity). {ECO:0000269|PubMed:10523339}.
/FTId=VAR_015635.
VARIANT 180 180 S -> F (in AME; reduces enzyme activity).
{ECO:0000269|PubMed:10523339}.
/FTId=VAR_015636.
VARIANT 186 186 R -> C (in AME; dbSNP:rs768507002).
{ECO:0000269|PubMed:7593417,
ECO:0000269|PubMed:9661590}.
/FTId=VAR_015637.
VARIANT 208 208 R -> C (in AME; reduces enzyme activity
by at least 95%; dbSNP:rs121917780).
{ECO:0000269|PubMed:7593417,
ECO:0000269|PubMed:7670488,
ECO:0000269|PubMed:9661590}.
/FTId=VAR_006958.
VARIANT 208 208 R -> H (in AME; abolishes enzyme
activity; dbSNP:rs28934592).
{ECO:0000269|PubMed:10523339,
ECO:0000269|PubMed:9398712}.
/FTId=VAR_015638.
VARIANT 213 213 R -> C (in AME; reduces enzyme activity
by 90%; dbSNP:rs28934591).
{ECO:0000269|PubMed:10489390,
ECO:0000269|PubMed:7670488,
ECO:0000269|PubMed:9851783}.
/FTId=VAR_006959.
VARIANT 223 223 D -> N (in AME; reduces enzyme activity
to about 6% of wild type;
dbSNP:rs121917833).
{ECO:0000269|PubMed:12788846}.
/FTId=VAR_066514.
VARIANT 227 227 P -> L (in hypertension; decreases
affinity for cortisol;
dbSNP:rs121917782).
{ECO:0000269|PubMed:9707624}.
/FTId=VAR_015639.
VARIANT 237 237 A -> V (in AME; reduces enzyme activity).
{ECO:0000269|PubMed:10523339}.
/FTId=VAR_015640.
VARIANT 244 244 D -> N (in AME; associated with R-250).
{ECO:0000269|PubMed:9661590}.
/FTId=VAR_015641.
VARIANT 250 251 LL -> PS (in AME; abolishes enzyme
activity).
/FTId=VAR_015643.
VARIANT 250 250 L -> R (in AME; associated with N-244).
{ECO:0000269|PubMed:9661590}.
/FTId=VAR_015642.
VARIANT 279 279 R -> C (in AME; decreases enzyme activity
by 33%; dbSNP:rs28934594).
{ECO:0000269|PubMed:9683587}.
/FTId=VAR_015644.
VARIANT 328 328 A -> V (in AME; abolishes enzyme
activity). {ECO:0000269|PubMed:10489390,
ECO:0000269|PubMed:10523339}.
/FTId=VAR_015645.
VARIANT 337 338 RY -> H (in AME; abolishes enzyme
activity). {ECO:0000269|PubMed:7593417,
ECO:0000269|PubMed:7670488,
ECO:0000269|PubMed:9398712,
ECO:0000269|PubMed:9661590}.
/FTId=VAR_015647.
VARIANT 337 337 R -> C (in AME; decreased half-life from
21 to 4 hours compared to wild-type,
probably due to degradation via the
proteasomal pathway; dbSNP:rs121917781).
{ECO:0000269|PubMed:17314322,
ECO:0000269|PubMed:7608290,
ECO:0000269|PubMed:9661590}.
/FTId=VAR_066515.
VARIANT 338 338 Y -> 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; dbSNP:rs387907117).
{ECO:0000269|PubMed:17314322}.
/FTId=VAR_015646.
MUTAGEN 115 115 E->K,Q: Abolishes cofactor specificity.
{ECO:0000269|PubMed:11238516}.
MUTAGEN 335 335 R->A,Q: Reduced enzyme activity.
{ECO:0000269|PubMed:17314322}.
MUTAGEN 335 335 R->K: No effect on enzyme activity.
{ECO:0000269|PubMed:17314322}.
MUTAGEN 336 336 R->A,Q: Almost complete loss of enzyme
activity. {ECO:0000269|PubMed:17314322}.
MUTAGEN 336 336 R->K: Reduced enzyme activity.
{ECO:0000269|PubMed:17314322}.
MUTAGEN 337 337 R->A,Q: Almost complete loss of enzyme
activity. {ECO:0000269|PubMed:17314322}.
MUTAGEN 337 337 R->K: Reduced enzyme activity.
{ECO:0000269|PubMed:17314322}.
MUTAGEN 338 338 Y->F,A: Complete loss of enzyme activity.
{ECO:0000269|PubMed:17314322}.
MUTAGEN 339 339 Y->A,F,H: Reduced enzyme activity.
{ECO:0000269|PubMed:17314322}.
CONFLICT 148 148 V -> F (in Ref. 2; AAB48544).
{ECO:0000305}.
CONFLICT 148 148 V -> L (in Ref. 1; AAA91969).
{ECO:0000305}.
CONFLICT 350 350 I -> T (in Ref. 7; AAH64536).
{ECO:0000305}.
CONFLICT 392 392 D -> G (in Ref. 7; AAH36780).
{ECO:0000305}.
SEQUENCE 405 AA; 44127 MW; 4AB269E269982D24 CRC64;
MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR LLPPPAALAV
LAAAGWIALS RLARPQRLPV ATRAVLITGC DSGFGKETAK KLDSMGFTVL ATVLELNSPG
AIELRTCCSP RLRLLQMDLT KPGDISRVLE FTKAHTTSTG LWGLVNNAGH NEVVADAELS
PVATFRSCME VNFFGALELT KGLLPLLRSS RGRIVTVGSP AGDMPYPCLG AYGTSKAAVA
LLMDTFSCEL LPWGVKVSII QPGCFKTESV RNVGQWEKRK QLLLANLPQE LLQAYGKDYI
EHLHGQFLHS LRLAMSDLTP VVDAITDALL AARPRRRYYP GQGLGLMYFI HYYLPEGLRR
RFLQAFFISH CLPRALQPGQ PGTTPPQDAA QDPNLSPGPS PAVAR


Related products :

Catalog number Product name Quantity
EIAAB11152 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Homo sapiens,HSD11B2,HSD11K,Human,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11148 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Rat,Rattus norvegicus
EIAAB11149 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Oryctolagus cuniculus,Rabbit
EIAAB11151 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,Mouse,Mus musculus,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11150 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Bos taurus,Bovine,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
15-288-22852 Corticosteroid 11-beta-dehydrogenase isozyme 2 - EC 1.1.1.-; 11-DH2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-HSD2; NAD-dependent 11-beta-hydroxysteroid dehydrogenase Polyclonal 0.05 mg
15-288-22852 Corticosteroid 11-beta-dehydrogenase isozyme 2 - EC 1.1.1.-; 11-DH2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-HSD2; NAD-dependent 11-beta-hydroxysteroid dehydrogenase Polyclonal 0.1 mg
EIAAB11106 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,EDH17B3,Homo sapiens,HSD17B3,Human,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11108 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Rat,Rattus norvegicus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11107 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Mouse,Mus musculus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11146 11-beta-HSD3,11-beta-hydroxysteroid dehydrogenase type 3,11-DH3,Homo sapiens,HSD11B1L,HSD3,Human,Hydroxysteroid 11-beta-dehydrogenase 1-like protein,SCDR10,Short-chain dehydrogenase_reductase 10
EIAAB11102 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Dehydrogenase_reductase SDR family member 10,DHRS10,Homo sapiens,HSD17B14,Human,Retinal short-chain d
EIAAB11101 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Bos taurus,Bovine,Dehydrogenase_reductase SDR family member 10,DHRS10,HSD17B14,Retinal short-chain de
EIAAB11092 17-beta-HSD 1,17-beta-hydroxysteroid dehydrogenase type 1,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E17KSR,E2DH,EDH17B1,EDH17B2,EDHB17,Estradiol 17-beta-dehydrogenase 1,Homo sapiens,HSD17B1,H
EIAAB11095 17-beta-HSD 11,17-beta-HSD XI,17betaHSD11,17betaHSDXI,17-beta-hydroxysteroid dehydrogenase 11,17-beta-hydroxysteroid dehydrogenase XI,17bHSD11,Dehydrogenase_reductase SDR family member 8,Dhrs8,Estradi
EIAAB11096 17-beta-HSD 11,17-beta-HSD XI,17betaHSD11,17betaHSDXI,17-beta-hydroxysteroid dehydrogenase 11,17-beta-hydroxysteroid dehydrogenase XI,17bHSD11,Dehydrogenase_reductase SDR family member 8,Dhrs8,Estradi
EIAAB11105 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E2DH,EDH17B2,Estradiol 17-beta-dehydrogenase 2,Homo sapiens,HSD17B2,Human,Microsomal 17-bet
EIAAB11104 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Mouse,Mus musculus,Testosterone 17-beta-dehydrogenase
EIAAB11103 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase
EIAAB11117 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,Hsd17b8,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase 8
U2268Rb CLIA 11-beta-HSD1,11-beta-hydroxysteroid dehydrogenase 1,11-DH,Corticosteroid 11-beta-dehydrogenase isozyme 1,HSD11B1,Oryctolagus cuniculus,Rabbit 96T
E2268r ELISA 11-beta-HSD1,11-beta-hydroxysteroid dehydrogenase 1,11-DH,Corticosteroid 11-beta-dehydrogenase isozyme 1,Hsd11,Hsd11b1,Rat,Rattus norvegicus 96T
U2268r CLIA 11-beta-HSD1,11-beta-hydroxysteroid dehydrogenase 1,11-DH,Corticosteroid 11-beta-dehydrogenase isozyme 1,Hsd11,Hsd11b1,Rat,Rattus norvegicus 96T
E2268Rb ELISA kit 11-beta-HSD1,11-beta-hydroxysteroid dehydrogenase 1,11-DH,Corticosteroid 11-beta-dehydrogenase isozyme 1,HSD11B1,Oryctolagus cuniculus,Rabbit 96T
E2268Rb ELISA 11-beta-HSD1,11-beta-hydroxysteroid dehydrogenase 1,11-DH,Corticosteroid 11-beta-dehydrogenase isozyme 1,HSD11B1,Oryctolagus cuniculus,Rabbit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur