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P26439 (3BHS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
Alternative name(s):
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II
Short name=3-beta-HSD II
3-beta-HSD adrenal and gonadal type

Including the following 2 domains:

  1. 3-beta-hydroxy-Delta(5)-steroid dehydrogenase
    EC=1.1.1.145
    Alternative name(s):
    3-beta-hydroxy-5-ene steroid dehydrogenase
    Progesterone reductase
  2. Steroid Delta-isomerase
    EC=5.3.3.1
    Alternative name(s):
    Delta-5-3-ketosteroid isomerase
Gene names
Name:HSD3B2
Synonyms:HSDB3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.

Catalytic activity

A 3-beta-hydroxy-Delta(5)-steroid + NAD+ = a 3-oxo-Delta(5)-steroid + NADH.

A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.

Tissue specificity

Expressed in adrenal gland, testis and ovary.

Involvement in disease

Adrenal hyperplasia 2 (AH2) [MIM:201810]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH)and 'cryptic' (asymptomatic). In AH2, virilization is much less marked or does not occur. AH2 is frequently lethal in early life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Mild HSD3B2 deficiency in hyperandrogenic females is associated with characteristic traits of polycystic ovary syndrome, such as insulin resistance and luteinizing hormone hypersecretion.

Sequence similarities

Belongs to the 3-beta-HSD family.

Sequence caution

The sequence AAC60600.1 differs from that shown. Reason: Frameshift at position 186. The frameshift is caused by a single nucleotide insertion which is found in AH2.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital adrenal hyperplasia
Disease mutation
   DomainTransmembrane
Transmembrane helix
   LigandNAD
   Molecular functionIsomerase
Oxidoreductase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen biosynthetic process

Traceable author statement. Source: Reactome

glucocorticoid biosynthetic process

Traceable author statement. Source: Reactome

mineralocorticoid biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

steroid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Non-traceable author statement Ref.2. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial intermembrane space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial membrane

Non-traceable author statement Ref.2. Source: UniProtKB

smooth endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function3-beta-hydroxy-delta5-steroid dehydrogenase activity

Inferred from direct assay Ref.2. Source: UniProtKB

steroid delta-isomerase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26439-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P26439-2)

The sequence of this isoform differs from the canonical sequence as follows:
     103-222: GTQLLLEACV...SVGKFSTVNP → ELQNKIKLTV...FIDEKTRTEQ
     223-372: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3723723 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
PRO_0000087775

Regions

Transmembrane287 – 30721Helical; Potential

Sites

Active site1541Proton acceptor By similarity
Binding site1581NAD By similarity

Natural variations

Alternative sequence103 – 222120GTQLL…STVNP → ELQNKIKLTVLEGDILDEPF LKRACQDVSVVIHTACIIDV FGVTHRQSIMNVNVKGRVAW GGDKARWGNEDQKEGQEGKR SLSIEHLLCSGPSDFADHYQ LGELKAAIFSFIDEKTRTEQ in isoform 2.
VSP_037399
Alternative sequence223 – 372150Missing in isoform 2.
VSP_037400
Natural variant101A → E in AH2; activity abolished. Ref.23 Ref.25
Corresponds to variant rs28934880 [ dbSNP | Ensembl ].
VAR_010517
Natural variant101A → V in AH2; nonsalt-wasting form. Ref.23
VAR_010518
Natural variant151G → D in AH2; activity abolished. Ref.18 Ref.23
VAR_010519
Natural variant741D → N.
Corresponds to variant rs4986954 [ dbSNP | Ensembl ].
VAR_048099
Natural variant821A → P in AH2. Ref.28
VAR_070028
Natural variant821A → T in AH2. Ref.16 Ref.23
VAR_010520
Natural variant941E → Q. Ref.3
Corresponds to variant rs6211 [ dbSNP | Ensembl ].
VAR_014818
Natural variant1001N → S in AH2; nonsalt-wasting form. Ref.21 Ref.23
VAR_010521
Natural variant1081L → W in AH2; activity abolished. Ref.13 Ref.23
VAR_010522
Natural variant1291G → R in AH2; nonsalt-wasting form. Ref.15 Ref.23 Ref.24
VAR_010523
Natural variant1421E → K in AH2; activity abolished. Ref.12 Ref.23 Ref.26
VAR_000006
Natural variant1551P → L in AH2; nonsalt-wasting form. Ref.23
VAR_010524
Natural variant1671A → V in AH2; late onset; almost normal activity. Ref.23
Corresponds to variant rs35486059 [ dbSNP | Ensembl ].
VAR_010525
Natural variant1731L → R in AH2; nonsalt-wasting form. Ref.17 Ref.23
VAR_010526
Natural variant1861P → L in AH2; activity abolished. Ref.13 Ref.23
VAR_010527
Natural variant2051L → P in AH2. Ref.19 Ref.23
VAR_000007
Natural variant2131S → G in AH2; late onset; partial loss of activity. Ref.23
VAR_010528
Natural variant2161K → E in AH2; late onset; partial loss of activity. Ref.23
VAR_010529
Natural variant2221P → H in AH2; nonsalt-wasting form; activity abolished. Ref.23
VAR_010530
Natural variant2221P → Q in AH2; activity abolished. Ref.23 Ref.24
VAR_010531
Natural variant2221P → T in AH2. Ref.26
VAR_015411
Natural variant231 – 2388Missing in AH2; activity abolished.
VAR_010532
Natural variant2361L → S in AH2; mild; 100% of activity. Ref.22 Ref.23
Corresponds to variant rs35887327 [ dbSNP | Ensembl ].
VAR_010533
Natural variant2451A → P in AH2; loss of 88% of activity. Ref.12 Ref.23
VAR_000008
Natural variant2531Y → N in AH2; activity abolished. Ref.12 Ref.23
VAR_000009
Natural variant2541Y → D in AH2; activity abolished. Ref.14 Ref.23
VAR_000010
Natural variant2591T → M in AH2; activity abolished. Ref.23 Ref.24
VAR_010534
Natural variant2591T → R in AH2; activity abolished. Ref.20 Ref.23
VAR_000011
Natural variant2941G → V in AH2; nonsalt-wasting form; activity abolished. Ref.23
VAR_010535
Natural variant3411P → L in AH2; strongly reduced activity. Ref.27
VAR_065665

Experimental info

Sequence conflict52 – 532RT → KI in AAD14329. Ref.8
Sequence conflict92 – 943HRE → RRQ in AAD14329. Ref.8
Sequence conflict2321H → L in BAD96717. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8E0D933488988451

FASTA37242,052
        10         20         30         40         50         60 
MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG 

        70         80         90        100        110        120 
DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI 

       130        140        150        160        170        180 
YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PTPYPYSKKL AEKAVLAANG WNLKNGDTLY 

       190        200        210        220        230        240 
TCALRPTYIY GEGGPFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR 

       250        260        270        280        290        300 
DPKKAPSVRG QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV 

       310        320        330        340        350        360 
SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV 

       370 
DRHKETLKSK TQ 

« Hide

Isoform 2 [UniParc].

Checksum: 48A60A9900F0C500
Show »

FASTA22224,987

References

« Hide 'large scale' references
[1]"Structure of the human type II 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal and gonadal specificity."
Lachance Y., Luu-The V., Verreault H., Dumont M., Rheaume E., Leblanc G., Labrie F.
DNA Cell Biol. 10:701-711(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and expression of a new complementary DNA encoding the almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase in human adrenals and gonads."
Rheaume E., Lachance Y., Zhao H.-F., Breton N., Dumont M., de Launoit Y., Trudel C., Luu-The V., Simard J., Labrie F.
Mol. Endocrinol. 5:1147-1157(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-94.
Tissue: Adrenal gland.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
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] (ISOFORM 1).
Tissue: Brain.
[8]"Variation in the expression of human 3 beta-hydroxysteroid dehydrogenase."
Russell A.J., McCartin S., Corcao G., Burridge S.M., McBride M.W., McNicol A.M., Hawes C.S., Mason J.I., Sutcliffe R.G.
Endocr. Res. 21:485-494(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-102.
[9]"Congenital adrenal hyperplasia due to point mutations in the type II 3 beta-hydroxysteroid dehydrogenase gene."
Rheaume E., Simard J., Morel Y., Mebarki F., Zachmann M., Forest M.G., New M.I., Labrie F.
Nat. Genet. 1:239-245(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205.
[10]"The hormonal phenotype of nonclassic 3 beta-hydroxysteroid dehydrogenase (HSD3B) deficiency in hyperandrogenic females is associated with insulin-resistant polycystic ovary syndrome and is not a variant of inherited HSD3B2 deficiency."
Carbunaru G., Prasad P., Scoccia B., Shea P., Hopwood N., Ziai F., Chang Y.T., Myers S.E., Mason J.I., Pang S.
J. Clin. Endocrinol. Metab. 89:783-794(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN INSULIN-RESISTANT POLYCYSTIC OVARY SYNDROME.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Molecular basis of congenital adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase deficiency."
Simard J., Rheaume E., Sanchez R., Laflamme N., de Launoit Y., Luu-The V., van Seters A.P., Gordon R.D., Bettendorf M., Heinrich U., Moshang T., New M.I., Labrie F.
Mol. Endocrinol. 7:716-728(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH2 LYS-142; PRO-245 AND ASN-253.
[13]"Functional characterization of the novel L108W and P186L mutations detected in the type II 3 beta-hydroxysteroid dehydrogenase gene of a male pseudohermaphrodite with congenital adrenal hyperplasia."
Sanchez R., Mebarki F., Rheaume E., Laflamme N., Forest M.G., Bey-Omar F., David M., Morel Y., Labrie F., Simard J.
Hum. Mol. Genet. 3:1639-1645(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH2 TRP-108 AND LEU-186.
[14]"Detection and functional characterization of the novel missense mutation Y254D in type II 3 beta-hydroxysteroid dehydrogenase (3 beta HSD) gene of a female patient with nonsalt-losing 3 beta HSD deficiency."
Sanchez R., Rheaume E., Laflamme N., Rosenfield R.L., Labrie F., Simard J.
J. Clin. Endocrinol. Metab. 78:561-567(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 ASP-254.
[15]"Molecular basis of congenital adrenal hyperplasia in two siblings with classical nonsalt-losing 3 beta-hydroxysteroid dehydrogenase deficiency."
Rheaume E., Sanchez R., Simard J., Chang Y.T., Wang J., Pang S., Labrie F.
J. Clin. Endocrinol. Metab. 79:1012-1018(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 ARG-129.
[16]"Mutation in 3 beta-hydroxysteroid dehydrogenase type II associated with pseudohermaphroditism in males and premature pubarche or cryptic expression in females."
Mendonca B.B., Russell A.J., Vasconcelos-Leite M., Arnhold I.J., Bloise W., Wajchenberg B.L., Nicolau W., Sutcliffe R.G., Wallace A.M.
J. Mol. Endocrinol. 12:119-122(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 THR-82.
[17]"Mutation in the human gene for 3 beta-hydroxysteroid dehydrogenase type II leading to male pseudohermaphroditism without salt loss."
Russell A.J., Wallace A.M., Forest M.G., Donaldson M.D., Edwards C.R., Sutcliffe R.G.
J. Mol. Endocrinol. 12:225-237(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 ARG-173.
[18]"Identification and characterization of the G15D mutation found in a male patient with 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) deficiency: alteration of the putative NAD-binding domain of type II 3 beta-HSD."
Rheaume E., Sanchez R., Mebarki F., Gagnon E., Carel J.-C., Chaussain J.-L., Morel Y., Labrie F., Simard J.
Biochemistry 34:2893-2900(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 ASP-15.
[19]"A novel missense mutation in the type II 3 beta-hydroxysteroid dehydrogenase gene in a family with classical salt-wasting congenital adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase deficiency."
Katsumata N., Tanae A., Yasunaga T., Horikawa R., Tanaka T., Hibi I.
Hum. Mol. Genet. 4:745-746(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 PRO-205.
[20]"Molecular analysis of type II 3 beta-hydroxysteroid dehydrogenase gene in Japanese patients with classical 3 beta-hydroxysteroid dehydrogenase deficiency."
Tajima T., Fujieda K., Nakae J., Shinohara N., Yoshimoto M., Baba T., Kinoshita E., Igarashi Y., Oomura T.
Hum. Mol. Genet. 4:969-971(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 ARG-259.
[21]"Nonsalt-losing male pseudohermaphroditism due to the novel homozygous N100S mutation in the type II 3 beta-hydroxysteroid dehydrogenase gene."
Mebarki F., Sanchez R., Rheaume E., Laflamme N., Simard J., Forest M.G., Bey-Omar F., David M., Labrie F., Morel Y.
J. Clin. Endocrinol. Metab. 80:2127-2134(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 SER-100.
[22]"Variants of the type II 3beta-hydroxysteroid dehydrogenase gene in children with premature pubic hair and hyperandrogenic adolescents."
Nayak S., Lee P.A., Witchel S.F.
Mol. Genet. Metab. 64:184-192(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 SER-236.
[23]"New insight into the molecular basis of 3beta-hydroxysteroid dehydrogenase deficiency: identification of eight mutations in the HSD3B2 gene in eleven patients from seven new families and comparison of the functional properties of twenty-five mutant enzymes."
Moisan A.M., Ricketts M.L., Tardy V., Desrochers M., Mebarki F., Chaussain J.-L., Cabrol S., Raux-Demay M.C., Forest M.G., Sippell W.G., Peter M., Morel Y., Simard J.
J. Clin. Endocrinol. Metab. 84:4410-4425(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH2 GLU-10; VAL-10; ASP-15; THR-82; SER-100; TRP-108; ARG-129; LYS-142; LEU-155; VAL-167; ARG-173; LEU-186; PRO-205; GLY-213; GLU-216; GLN-222; HIS-222; SER-236; PRO-245; ASN-253; ASP-254; ARG-259; MET-259 AND VAL-294.
[24]"Mutations in the type II 3beta-hydroxysteroid dehydrogenase (HSD3B2) gene can cause premature pubarche in girls."
Marui S., Castro M., Latronico A.C., Elias L.L., Arnhold I.J., Moreira A.C., Mendonca B.B.
Clin. Endocrinol. (Oxf.) 52:67-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH2 ARG-129; GLN-222 AND MET-259.
[25]"A novel A10E homozygous mutation in the HSD3B2 gene causing severe salt-wasting 3beta-hydroxysteroid dehydrogenase deficiency in 46,XX and 46,XY French-Canadians: evaluation of gonadal function after puberty."
Alos N., Moisan A.M., Ward L., Desrochers M., Legault L., Leboeuf G., van Vliet G., Simard J.
J. Clin. Endocrinol. Metab. 85:1968-1974(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 GLU-10.
[26]"A novel nonstop mutation in the stop codon and a novel missense mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD deficiency congenital adrenal hyperplasia."
Pang S., Wang W., Rich B., David R., Chang Y.T., Carbunaru G., Myers S.E., Howie A.F., Smillie K.J., Mason J.I.
J. Clin. Endocrinol. Metab. 87:2556-2563(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH2 LYS-142 AND THR-222.
[27]"Carboxyl-terminal mutations in 3beta-hydroxysteroid dehydrogenase type II cause severe salt-wasting congenital adrenal hyperplasia."
Welzel M., Wustemann N., Simic-Schleicher G., Dorr H.G., Schulze E., Shaikh G., Clayton P., Grotzinger J., Holterhus P.M., Riepe F.G.
J. Clin. Endocrinol. Metab. 93:1418-1425(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 LEU-341, CHARACTERIZATION OF VARIANT AH2 LEU-341.
[28]"In silico structural, functional and pathogenicity evaluation of a novel mutation: an overview of HSD3B2 gene mutations."
Rabbani B., Mahdieh N., Haghi Ashtiani M.T., Setoodeh A., Rabbani A.
Gene 503:215-221(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH2 PRO-82.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77144 Genomic DNA. Translation: AAA36014.1.
M67466 mRNA. Translation: AAA36016.1.
CR627415 mRNA. Translation: CAH10504.1.
AK222997 mRNA. Translation: BAD96717.1.
AL359553 Genomic DNA. Translation: CAC19799.1.
CH471122 Genomic DNA. Translation: EAW56700.1.
BC038419 mRNA. Translation: AAH38419.1.
BC131488 mRNA. Translation: AAI31489.1.
S80140 Genomic DNA. Translation: AAD14329.1.
S60309 Genomic DNA. Translation: AAC60599.1.
S60310 Genomic DNA. Translation: AAC60600.1. Frameshift.
PIRDEHUH2. A39488.
RefSeqNP_000189.1. NM_000198.3.
NP_001159592.1. NM_001166120.1.
UniGeneHs.654399.

3D structure databases

ProteinModelPortalP26439.
SMRP26439. Positions 4-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109517. 1 interaction.
STRING9606.ENSP00000358424.

Chemistry

BindingDBP26439.
ChEMBLCHEMBL3670.
DrugBankDB00157. NADH.
DB01108. Trilostane.

PTM databases

PhosphoSiteP26439.

Polymorphism databases

DMDM112770.

Proteomic databases

PaxDbP26439.
PRIDEP26439.

Protocols and materials databases

DNASU3284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369416; ENSP00000358424; ENSG00000203859. [P26439-1]
ENST00000543831; ENSP00000445122; ENSG00000203859. [P26439-1]
GeneID3284.
KEGGhsa:3284.
UCSCuc001ehs.3. human. [P26439-1]
uc001ehu.3. human. [P26439-2]

Organism-specific databases

CTD3284.
GeneCardsGC01P119957.
HGNCHGNC:5218. HSD3B2.
MIM201810. phenotype.
613890. gene.
neXtProtNX_P26439.
Orphanet90791. Congenital adrenal hyperplasia due to 3-beta-hydroxysteroid dehydrogenase deficiency.
1331. Familial prostate cancer.
3185. Polycystic ovarian syndrome.
PharmGKBPA29487.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0451.
HOVERGENHBG000014.
InParanoidP26439.
KOK00070.
OMATTEWLAS.
PhylomeDBP26439.
TreeFamTF343138.

Enzyme and pathway databases

BioCycMetaCyc:HS10943-MONOMER.
BRENDA1.1.1.145. 2681.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
UniPathwayUPA00062.

Gene expression databases

ArrayExpressP26439.
BgeeP26439.
CleanExHS_HSD3B2.
GenevestigatorP26439.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHSD3B2.
GenomeRNAi3284.
NextBio13035.
PROP26439.
SOURCESearch...

Entry information

Entry name3BHS2_HUMAN
AccessionPrimary (citable) accession number: P26439
Secondary accession number(s): A2RRA5 expand/collapse secondary AC list , Q16010, Q53GD4, Q6AI10, Q6LDB9, Q99890, Q9UD08
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM