UniProtKB - P26439 (3BHS2_HUMAN)
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- BLAST>sp|P26439|3BHS2_HUMAN 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 OS=Homo sapiens OX=9606 GN=HSD3B2 PE=1 SV=2 MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEG DILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFI YTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLY TCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALR DPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVV SFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLV DRHKETLKSKTQ
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Protein
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
Gene
HSD3B2
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta5-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.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
A 3-beta-hydroxy-Delta5-steroid + NAD+ = a 3-oxo-Delta5-steroid + NADH.
A 3-oxo-Delta5-steroid = a 3-oxo-Delta4-steroid.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: steroid biosynthesis
This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 154 | Proton acceptorBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 158 | NADBy similarity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 3-beta-hydroxy-delta5-steroid dehydrogenase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cholesterol dehydrogenase activity Source: UniProtKB-EC
- steroid delta-isomerase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- androgen biosynthetic process Source: Reactome
- glucocorticoid biosynthetic process Source: Reactome
- mineralocorticoid biosynthetic process Source: Reactome
- steroid biosynthetic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Isomerase, Multifunctional enzyme, Oxidoreductase |
| Biological process | Steroidogenesis |
| Ligand | NAD |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS10943-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.145 2681 5.3.3.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-193048 Androgen biosynthesis R-HSA-193993 Mineralocorticoid biosynthesis R-HSA-194002 Glucocorticoid biosynthesis |
SIGNOR Signaling Network Open Resource More...SIGNORi | P26439 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00062 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001296 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2Alternative 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: |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:HSD3B2 Synonyms:HSDB3B |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000203859.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5218 HSD3B2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 613890 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P26439 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
Mitochondrion
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- endoplasmic reticulum membrane Source: Reactome
- smooth endoplasmic reticulum membrane Source: UniProtKB
Mitochondrion
- mitochondrial inner membrane Source: UniProtKB
- mitochondrial intermembrane space Source: UniProtKB
- mitochondrial membrane Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
Other locations
- integral component of membrane Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 287 – 307 | HelicalSequence analysisAdd BLAST | 21 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, Mitochondrion<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Adrenal hyperplasia 2 (AH2)17 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.11"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. - Ref.12"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. - Ref.13"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. - Ref.14"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. - Ref.15"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. - Ref.16"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. - Ref.17"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. - Ref.18"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. - Ref.19"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. - Ref.20"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. - Ref.21"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. - Ref.22"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. - Ref.23"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. - Ref.24"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. - Ref.25"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. - Ref.26"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. - Ref.27"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.
Ref.11
"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]
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.
Ref.12
"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]
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.
Ref.13
"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]
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.
Ref.14
"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]
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.
Ref.15
"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]
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.
Ref.16
"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]
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.
Ref.17
"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]
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.
Ref.18
"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]
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.
Ref.19
"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]
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.
Ref.20
"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]
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.
Ref.21
"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]
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.
Ref.22
"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]
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.
Ref.23
"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]
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.
Ref.24
"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]
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.
Ref.25
"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]
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.
Ref.26
"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]
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.
Ref.27
"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]
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.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:201810| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010517 | 10 | A → E in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010518 | 10 | A → V in AH2; nonsalt-wasting form. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010519 | 15 | G → D in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070028 | 82 | A → P in AH2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010520 | 82 | A → T in AH2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010521 | 100 | N → S in AH2; nonsalt-wasting form. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010522 | 108 | L → W in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010523 | 129 | G → R in AH2; nonsalt-wasting form. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000006 | 142 | E → K in AH2; activity abolished. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010524 | 155 | P → L in AH2; nonsalt-wasting form. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010525 | 167 | A → V in AH2; late onset; almost normal activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010526 | 173 | L → R in AH2; nonsalt-wasting form. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010527 | 186 | P → L in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000007 | 205 | L → P in AH2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010528 | 213 | S → G in AH2; late onset; partial loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010529 | 216 | K → E in AH2; late onset; partial loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010530 | 222 | P → H in AH2; nonsalt-wasting form; activity abolished. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010531 | 222 | P → Q in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015411 | 222 | P → T in AH2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010532 | 231 – 238 | Missing in AH2; activity abolished. | 8 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010533 | 236 | L → S in AH2; mild; 100% of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000008 | 245 | A → P in AH2; loss of 88% of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000009 | 253 | Y → N in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000010 | 254 | Y → D in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010534 | 259 | T → M in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000011 | 259 | T → R in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010535 | 294 | G → V in AH2; nonsalt-wasting form; activity abolished. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065665 | 341 | P → L in AH2; strongly reduced activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mild HSD3B2 deficiency in hyperandrogenic females is associated with characteristic traits of polycystic ovary syndrome, such as insulin resistance and luteinizing hormone hypersecretion.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Congenital adrenal hyperplasia, Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 3284 |
MalaCards human disease database More...MalaCardsi | HSD3B2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 201810 phenotype |
Open Targets More...OpenTargetsi | ENSG00000203859 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 90791 Congenital adrenal hyperplasia due to 3-beta-hydroxysteroid dehydrogenase deficiency 3185 Polycystic ovary syndrome |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29487 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3670 |
Drug and drug target database More...DrugBanki | DB01285 Corticotropin DB00603 Medroxyprogesterone acetate DB00157 NADH DB01108 Trilostane |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSD3B2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112770 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000087775 | 1 – 372 | 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2Add BLAST | 372 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P26439 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P26439 |
PeptideAtlas More...PeptideAtlasi | P26439 |
PRoteomics IDEntifications database More...PRIDEi | P26439 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54346 54347 [P26439-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P26439 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P26439 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed in adrenal gland, testis and ovary.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000203859 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSD3B2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P26439 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P26439 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA043261 HPA043264 HPA044028 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109517, 22 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P26439 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358424 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P26439 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P26439 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the 3-beta-HSD family.Curated
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1430 Eukaryota COG0451 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074557 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000014 |
KEGG Orthology (KO) More...KOi | K00070 |
Identification of Orthologs from Complete Genome Data More...OMAi | YSYQPPF |
Database of Orthologous Groups More...OrthoDBi | EOG091G09QZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P26439 |
TreeFam database of animal gene trees More...TreeFami | TF343138 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002225 3Beta_OHSteriod_DH/Estase IPR036291 NAD(P)-bd_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01073 3Beta_HSD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735 SSF51735, 2 hits |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P26439-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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.
10 20 30 40 50
MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ
60 70 80 90 100
NRTKLTVLEG DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN
110 120 130 140 150
VKGTQLLLEA CVQASVPVFI YTSSIEVAGP NSYKEIIQNG HEEEPLENTW
160 170 180 190 200
PTPYPYSKKL AEKAVLAANG WNLKNGDTLY TCALRPTYIY GEGGPFLSAS
210 220 230 240 250
INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR DPKKAPSVRG
260 270 280 290 300
QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV
310 320 330 340 350
SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ
360 370
KTVEWVGSLV DRHKETLKSK TQ
Length:372
Mass (Da):42,052
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8E0D933488988451
Isoform 2 (identifier: P26439-2) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
103-222: GTQLLLEACV...SVGKFSTVNP → ELQNKIKLTV...FIDEKTRTEQ
223-372: Missing.
10 20 30 40 50
MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ
60 70 80 90 100
NRTKLTVLEG DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN
110 120 130 140 150
VKELQNKIKL TVLEGDILDE PFLKRACQDV SVVIHTACII DVFGVTHRQS
160 170 180 190 200
IMNVNVKGRV AWGGDKARWG NEDQKEGQEG KRSLSIEHLL CSGPSDFADH
210 220
YQLGELKAAI FSFIDEKTRT EQ
Length:222
Mass (Da):24,987
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i48A60A9900F0C500
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence AAC60600 differs from that shown. Reason: Frameshift at position 186. The frameshift is caused by a single nucleotide insertion which is found in AH2.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 52 – 53 | RT → KI in AAD14329 (PubMed:7588414).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 92 – 94 | HRE → RRQ in AAD14329 (PubMed:7588414).Curated | 3 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 232 | H → L in BAD96717 (Ref. 4) Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010517 | 10 | A → E in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010518 | 10 | A → V in AH2; nonsalt-wasting form. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010519 | 15 | G → D in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_048099 | 74 | D → N. Corresponds to variant dbSNP:rs4986954Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_070028 | 82 | A → P in AH2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010520 | 82 | A → T in AH2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014818 | 94 | E → Q1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010521 | 100 | N → S in AH2; nonsalt-wasting form. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010522 | 108 | L → W in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010523 | 129 | G → R in AH2; nonsalt-wasting form. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000006 | 142 | E → K in AH2; activity abolished. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010524 | 155 | P → L in AH2; nonsalt-wasting form. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010525 | 167 | A → V in AH2; late onset; almost normal activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010526 | 173 | L → R in AH2; nonsalt-wasting form. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010527 | 186 | P → L in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000007 | 205 | L → P in AH2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010528 | 213 | S → G in AH2; late onset; partial loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010529 | 216 | K → E in AH2; late onset; partial loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010530 | 222 | P → H in AH2; nonsalt-wasting form; activity abolished. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010531 | 222 | P → Q in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015411 | 222 | P → T in AH2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010532 | 231 – 238 | Missing in AH2; activity abolished. | 8 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010533 | 236 | L → S in AH2; mild; 100% of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000008 | 245 | A → P in AH2; loss of 88% of activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000009 | 253 | Y → N in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000010 | 254 | Y → D in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010534 | 259 | T → M in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000011 | 259 | T → R in AH2; activity abolished. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010535 | 294 | G → V in AH2; nonsalt-wasting form; activity abolished. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065665 | 341 | P → L in AH2; strongly reduced activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_037399 | 103 – 222 | GTQLL…STVNP → ELQNKIKLTVLEGDILDEPF LKRACQDVSVVIHTACIIDV FGVTHRQSIMNVNVKGRVAW GGDKARWGNEDQKEGQEGKR SLSIEHLLCSGPSDFADHYQ LGELKAAIFSFIDEKTRTEQ in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 120 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_037400 | 223 – 372 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 150 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M77144 Genomic DNA Translation: AAA36014.1 M67466 mRNA Translation: AAA36016.1 CR627415 mRNA Translation: CAH10504.1 AK222997 mRNA Translation: BAD96717.1 AL359553 Genomic DNA No translation available. 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. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS902.1 [P26439-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A39488 DEHUH2 |
NCBI Reference Sequences More...RefSeqi | NP_000189.1, NM_000198.3 [P26439-1] NP_001159592.1, NM_001166120.1 [P26439-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.654399 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369416; ENSP00000358424; ENSG00000203859 [P26439-1] ENST00000543831; ENSP00000445122; ENSG00000203859 [P26439-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3284 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3284 |
UCSC genome browser More...UCSCi | uc001eht.4 human [P26439-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M77144 Genomic DNA Translation: AAA36014.1 M67466 mRNA Translation: AAA36016.1 CR627415 mRNA Translation: CAH10504.1 AK222997 mRNA Translation: BAD96717.1 AL359553 Genomic DNA No translation available. 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. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS902.1 [P26439-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A39488 DEHUH2 |
NCBI Reference Sequences More...RefSeqi | NP_000189.1, NM_000198.3 [P26439-1] NP_001159592.1, NM_001166120.1 [P26439-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.654399 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P26439 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109517, 22 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P26439 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358424 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P26439 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3670 |
Drug and drug target database More...DrugBanki | DB01285 Corticotropin DB00603 Medroxyprogesterone acetate DB00157 NADH DB01108 Trilostane |
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001296 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P26439 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P26439 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSD3B2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112770 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P26439 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P26439 |
PeptideAtlas More...PeptideAtlasi | P26439 |
PRoteomics IDEntifications database More...PRIDEi | P26439 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54346 54347 [P26439-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 3284 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369416; ENSP00000358424; ENSG00000203859 [P26439-1] ENST00000543831; ENSP00000445122; ENSG00000203859 [P26439-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3284 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3284 |
UCSC genome browser More...UCSCi | uc001eht.4 human [P26439-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3284 |
DisGeNET More...DisGeNETi | 3284 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000203859.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HSD3B2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5218 HSD3B2 |
Human Protein Atlas More...HPAi | HPA043261 HPA043264 HPA044028 |
MalaCards human disease database More...MalaCardsi | HSD3B2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 201810 phenotype 613890 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P26439 |
Open Targets More...OpenTargetsi | ENSG00000203859 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 90791 Congenital adrenal hyperplasia due to 3-beta-hydroxysteroid dehydrogenase deficiency 3185 Polycystic ovary syndrome |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29487 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1430 Eukaryota COG0451 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074557 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000014 |
KEGG Orthology (KO) More...KOi | K00070 |
Identification of Orthologs from Complete Genome Data More...OMAi | YSYQPPF |
Database of Orthologous Groups More...OrthoDBi | EOG091G09QZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P26439 |
TreeFam database of animal gene trees More...TreeFami | TF343138 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00062 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS10943-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.145 2681 5.3.3.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-193048 Androgen biosynthesis R-HSA-193993 Mineralocorticoid biosynthesis R-HSA-194002 Glucocorticoid biosynthesis |
SIGNOR Signaling Network Open Resource More...SIGNORi | P26439 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | HSD3B2 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | HSD3B2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3284 |
Protein Ontology More...PROi | PR:P26439 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000203859 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSD3B2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P26439 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P26439 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002225 3Beta_OHSteriod_DH/Estase IPR036291 NAD(P)-bd_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF01073 3Beta_HSD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735 SSF51735, 2 hits |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | 3BHS2_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P26439Primary (citable) accession number: P26439 Secondary accession number(s): A2RRA5 , Q16010, Q53GD4, Q6AI10, Q6LDB9, Q99890, Q9UD08 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | June 20, 2018 | |
| This is version 191 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
