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

Names and origin

Protein names

Recommended name:
    3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
Alternative name(s):
    3-beta-HSD II
Including the following 2 domains:
    1- Recommended name:
            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- Recommended name:
            Steroid Delta-isomerase
              EC=5.3.3.1
        Alternative name(s):
            Delta-5-3-ketosteroid isomerase

Gene names

Name:	HSD3B2
Synonyms:	HSDB3B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Adrenal glands, testes and ovaries.
Involvement in disease	Defects in HSD3B2 are the cause of adrenal hyperplasia type 2 (AH2) [MIM:201810]. AH2 is 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. Ref.10 Ref.11 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 Mild HSD3B2 deficiency in hyperandrogenic females is associated with characteristic traits of polycystic ovary syndrome, such as insulin resistance and luteinizing hormon 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 process	Steroidogenesis
Cellular component	Endoplasmic reticulum Membrane Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital adrenal hyperplasia Disease mutation
Domain	Transmembrane
Ligand	NAD
Molecular function	Isomerase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Ref.2 Non-traceable author statement. Source: UniProtKB microsome Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial intermembrane space Inferred from sequence or structural similarity. Source: UniProtKB smooth endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	3-beta-hydroxy-delta5-steroid dehydrogenase activity Ref.2 Inferred from direct assay. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro steroid delta-isomerase activity Ref.2 Inferred from direct assay. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 372	371	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2		PRO_0000087775
Regions
	Transmembrane	287 – 307	21	Potential
Sites
	Active site	154	1	Proton acceptor By similarity
	Binding site	158	1	NAD By similarity
Natural variations
	Alternative sequence	103 – 222	120	GTQLL…STVNP → ELQNKIKLTVLEGDILDEPF LKRACQDVSVVIHTACIIDV FGVTHRQSIMNVNVKGRVAW GGDKARWGNEDQKEGQEGKR SLSIEHLLCSGPSDFADHYQ LGELKAAIFSFIDEKTRTEQ in isoform 2.		VSP_037399
	Alternative sequence	223 – 372	150	Missing in isoform 2.		VSP_037400
	Natural variant	10	1	A → E in AH2; activity abolished. Ref.23		VAR_010517
	Natural variant	10	1	A → V in AH2; nonsalt-wasting form. Ref.23		VAR_010518
	Natural variant	15	1	G → D in AH2; activity abolished. Ref.16		VAR_010519
	Natural variant	74	1	D → N: dbSNP rs4986954.		VAR_048099
	Natural variant	82	1	A → T in AH2. Ref.14		VAR_010520
	Natural variant	94	1	E → Q: dbSNP rs6211.		VAR_014818
	Natural variant	100	1	N → S in AH2; nonsalt-wasting form. Ref.19		VAR_010521
	Natural variant	108	1	L → W in AH2; activity abolished. Ref.11		VAR_010522
	Natural variant	129	1	G → R in AH2; nonsalt-wasting form. Ref.13 Ref.22		VAR_010523
	Natural variant	142	1	E → K in AH2; activity abolished. Ref.10 Ref.24		VAR_000006
	Natural variant	155	1	P → L in AH2; nonsalt-wasting form.		VAR_010524
	Natural variant	167	1	A → V in AH2; late onset; almost normal activity.		VAR_010525
	Natural variant	173	1	L → R in AH2; nonsalt-wasting form. Ref.15		VAR_010526
	Natural variant	186	1	P → L in AH2; activity abolished. Ref.11		VAR_010527
	Natural variant	205	1	L → P in AH2. Ref.17		VAR_000007
	Natural variant	213	1	S → G in AH2; late onset; partial loss of activity.		VAR_010528
	Natural variant	216	1	K → E in AH2; late onset; partial loss of activity.		VAR_010529
	Natural variant	222	1	P → H in AH2; nonsalt-wasting form; activity abolished. Ref.22 Ref.24		VAR_010530
	Natural variant	222	1	P → Q in AH2; activity abolished. Ref.22 Ref.24		VAR_010531
	Natural variant	222	1	P → T in AH2. Ref.22 Ref.24		VAR_015411
	Natural variant	231 – 238	8	Missing in AH2; activity abolished.		VAR_010532
	Natural variant	236	1	L → S in AH2; mild; 100% of activity. dbSNP rs35887327. Ref.20		VAR_010533
	Natural variant	245	1	A → P in AH2; loss of 88% of activity. Ref.10		VAR_000008
	Natural variant	253	1	Y → N in AH2; activity abolished. Ref.10		VAR_000009
	Natural variant	254	1	Y → D in AH2; activity abolished. Ref.12		VAR_000010
	Natural variant	259	1	T → M in AH2; activity abolished. Ref.18 Ref.22		VAR_010534
	Natural variant	259	1	T → R in AH2; activity abolished. Ref.18 Ref.22		VAR_000011
	Natural variant	294	1	G → V in AH2; nonsalt-wasting form; activity abolished.		VAR_010535
Experimental info
	Sequence conflict	52 – 53	2	RT → KI in AAD14329. Ref.7
	Sequence conflict	92 – 94	3	HRE → RRQ in AAD14329. Ref.7
	Sequence conflict	232	1	H → L in BAD96717. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8E0D933488988451	FASTA	372	42,052
	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
	Isoform 2. Checksum: 48A60A9900F0C500	FASTA	222	24,987
	10 20 30 40 50 60 MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG 70 80 90 100 110 120 DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKELQNKIKL TVLEGDILDE 130 140 150 160 170 180 PFLKRACQDV SVVIHTACII DVFGVTHRQS IMNVNVKGRV AWGGDKARWG NEDQKEGQEG 190 200 210 220 KRSLSIEHLL CSGPSDFADH YQLGELKAAI FSFIDEKTRT EQ

References

	« Hide 'large scale' referencesShow '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: 1741954] [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: 1944309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal gland.
[3]	The German cDNA consortium Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases 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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"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: 7588414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-102.
[8]	"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: 1363812] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205.
[9]	"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: 14764797] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN INSULIN-RESISTANT POLYCYSTIC OVARY SYNDROME.
[10]	"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: 8316254] [Abstract] Cited for: VARIANTS AH2 LYS-142; PRO-245 AND ASN-253.
[11]	"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: 7833923] [Abstract] Cited for: VARIANTS AH2 TRP-108 AND LEU-186.
[12]	"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: 8126127] [Abstract] Cited for: VARIANT AH2 ASP-254.
[13]	"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: 7962268] [Abstract] Cited for: VARIANT AH2 ARG-129.
[14]	"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: 8185809] [Abstract] Cited for: VARIANT AH2 THR-82.
[15]	"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: 8060486] [Abstract] Cited for: VARIANT AH2 ARG-173.
[16]	"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: 7893703] [Abstract] Cited for: VARIANT AH2 ASP-15.
[17]	"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: 7633426] [Abstract] Cited for: VARIANT AH2 PRO-205.
[18]	"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: 7633460] [Abstract] Cited for: VARIANT AH2 ARG-259.
[19]	"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: 7608265] [Abstract] Cited for: VARIANT AH2 SER-100.
[20]	"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: 9719627] [Abstract] Cited for: VARIANT AH2 SER-236.
[21]	"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: 10599696] [Abstract] Cited for: VARIANTS AH2.
[22]	"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: 10651755] [Abstract] Cited for: VARIANTS AH2 ARG-129; GLN-222 AND MET-259.
[23]	"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: 10843183] [Abstract] Cited for: VARIANT AH2 GLU-10.
[24]	"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: 12050213] [Abstract] Cited for: VARIANTS AH2 LYS-142 AND THR-222.
+	Additional computationally mapped references.

Web resources

GeneDis

Congenital adrenal hyperplasia website

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC038419 mRNA. Translation: AAH38419.1. S80140 Genomic DNA. Translation: AAD14329.1. S60309 Genomic DNA. Translation: AAC60599.1. S60310 Genomic DNA. Translation: AAC60600.1. Frameshift.
IPI	IPI00218494.
PIR	DEHUH2. A39488.
RefSeq	NP_000189.1.
UniGene	Hs.654399
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P26439.
Genome annotation databases
Ensembl	ENSG00000203859. Homo sapiens. [Contig view]
GeneID	3284.
KEGG	hsa:3284.
UCSC	uc001ehs.1. human.
Organism-specific databases
GeneCards	GC01P119669.
H-InvDB	HIX0023638.
HGNC	HGNC:5218. HSD3B2.
MIM	201810. gene+phenotype.
Orphanet	418. Congenital adrenal hyperplasia. 1331. Prostate cancer, familial. 3185. Stein-Leventhal syndrome.
PharmGKB	PA29487.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P26439.
HOVERGEN	P26439.
OMA	P26439. LATCAIR.
Enzyme and pathway databases
BRENDA	1.1.1.145. 247. 5.3.3.1. 247.
Reactome	REACT_15314. Hormone biosynthesis. REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	P26439.
Bgee	P26439.
CleanEx	HS_HSD3B2.
GermOnline	ENSG00000203859. Homo sapiens.
Family and domain databases
InterPro	IPR002225. 3Beta_OHSteriod_DH/Estase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01073. 3Beta_HSD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00157. NADH. DB01108. Trilostane.
NextBio	13035.
SOURCE	Search...

Entry information

Entry name

3BHS2_HUMAN

Accession

Primary (citable) accession number: P26439
Secondary accession number(s): Q16010 , Q53GD4, Q6AI10, Q6LDB9, Q99890, Q9UD08

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)