Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14060 (3BHS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

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

Names and origin

Protein namesRecommended name:
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
Alternative name(s):
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
Short name=3-beta-HSD I
Trophoblast antigen FDO161G

Including the following 2 domains:

  1. 3-beta-hydroxy-Delta(5)-steroid dehydrogenase
    EC=1.1.1.145
    Alternative name(s):
    3-beta-hydroxy-5-ene steroid dehydrogenase
    Progesterone reductase
  2. Steroid Delta-isomerase
    EC=5.3.3.1
    Alternative name(s):
    Delta-5-3-ketosteroid isomerase
Gene names
Name:HSD3B1
Synonyms:3BH, HSDB3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. Efficiently catalyzes the transformation of pregnenolone to progesterone, 17-alpha-hydroxypregnenolone to 17-alpha-hydroxyprogesterone, DHEA to 4-androstenedione, dihydrotestosterone to 5-alpha-androstane-3 beta,17 beta-diol, dehydroepiandrosterone to androstenedione and 5-alpha-androstan-3 beta,17 beta-diol to 5-alpha-dihydrotestosterone. Ref.2 Ref.6

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

Placenta and skin. Predominantly expressed in mammary gland tissue.

Sequence similarities

Belongs to the 3-beta-HSD family.

Sequence caution

The sequence AAA36001.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandNAD
   Molecular functionIsomerase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen biosynthetic process

Traceable author statement PubMed 1944309. Source: UniProtKB

estrogen biosynthetic process

Traceable author statement PubMed 1944309. Source: UniProtKB

glucocorticoid biosynthetic process

Traceable author statement. Source: Reactome

mineralocorticoid biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid biosynthetic process

Inferred from sequence or structural similarity PubMed 1944309. Source: UniProtKB

steroid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from direct assay PubMed 8274411. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay PubMed 8274411. Source: UniProtKB

smooth endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function3-beta-hydroxy-delta5-steroid dehydrogenase activity

Inferred from sequence or structural similarity PubMed 1944309. Source: UniProtKB

steroid delta-isomerase activity

Inferred from sequence or structural similarity PubMed 1944309. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 3733723 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
PRO_0000087774

Regions

Transmembrane288 – 30821Helical; Potential

Sites

Active site1551Proton acceptor By similarity
Binding site1591NAD By similarity

Natural variations

Natural variant541T → I.
Corresponds to variant rs3088283 [ dbSNP | Ensembl ].
VAR_048096
Natural variant711R → I.
Corresponds to variant rs4986952 [ dbSNP | Ensembl ].
VAR_048097
Natural variant791I → V. Ref.9
Corresponds to variant rs6201 [ dbSNP | Ensembl ].
VAR_014174
Natural variant901G → S.
Corresponds to variant rs6684974 [ dbSNP | Ensembl ].
VAR_048098
Natural variant2861F → L. Ref.9
Corresponds to variant rs6205 [ dbSNP | Ensembl ].
VAR_014175
Natural variant3671T → N. Ref.4 Ref.8
Corresponds to variant rs1047303 [ dbSNP | Ensembl ].
VAR_000005

Sequences

Sequence LengthMass (Da)Tools
P14060 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2C76616E7EA7433A

FASTA37342,252
        10         20         30         40         50         60 
MTGWSCLVTG AGGFLGQRII RLLVKEKELK EIRVLDKAFG PELREEFSKL QNKTKLTVLE 

        70         80         90        100        110        120 
GDILDEPFLK RACQDVSVII HTACIIDVFG VTHRESIMNV NVKGTQLLLE ACVQASVPVF 

       130        140        150        160        170        180 
IYTSSIEVAG PNSYKEIIQN GHEEEPLENT WPAPYPHSKK LAEKAVLAAN GWNLKNGGTL 

       190        200        210        220        230        240 
YTCALRPMYI YGEGSRFLSA SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL 

       250        260        270        280        290        300 
QDPKKAPSIR GQFYYISDDT PHQSYDNLNY TLSKEFGLRL DSRWSFPLSL MYWIGFLLEI 

       310        320        330        340        350        360 
VSFLLRPIYT YRPPFNRHIV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK QKTVEWVGSL 

       370 
VDRHKETLKS KTQ 

« Hide

References

« Hide 'large scale' references
[1]"Full length cDNA structure and deduced amino acid sequence of human 3 beta-hydroxy-5-ene steroid dehydrogenase."
Luu-The V., Lachance Y., Labrie F., Leblanc G., Thomas J.L., Strickler R.C., Labrie C.
Mol. Endocrinol. 3:1310-1312(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-30.
[2]"Human 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids."
Lorence M.C., Murry B.A., Trant J.M., Mason J.I.
Endocrinology 126:2493-2498(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Placenta.
[3]"Structural analysis of the gene encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase."
Lorence M.C., Corbin C.J., Kamimura N., Mahendroo M.S., Mason J.I.
Mol. Endocrinol. 4:1850-1855(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase gene and its expression in mammalian cells."
Lachance Y., Luu-The V., Labrie C., Simard J., Dumont M., Launoit Y.D., Guerin S., Leblanc G., Labrie F.
J. Biol. Chem. 265:20469-20475(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-367.
[5]"Molecular cloning and expression of human trophoblast antigen FDO161G and its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase."
Nickson D.A., McBride M.W., Zeinali S., Hawes C.S., Petropoulos A., Mueller U.W., Sutcliffe R.G.
J. Reprod. Fertil. 93:149-156(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[6]"Characterization, expression, and immunohistochemical localization of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human skin."
Dumont M., Van L.T., Dupont E., Pelletier G., Labrie F.
J. Invest. Dermatol. 99:415-421(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-367.
Tissue: Skin.
[9]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-79 AND LEU-286.
[10]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27137 mRNA. Translation: AAA36015.1.
M28392, M28162, M28391 Genomic DNA. Translation: AAA36001.1. Sequence problems.
X53321 mRNA. Translation: CAA37408.1.
M35493 mRNA. Translation: AAA51538.1.
M63397, M63395, M63396 Genomic DNA. Translation: AAA51662.1.
M38180 Genomic DNA. Translation: AAA51831.1.
X55997 mRNA. Translation: CAA39469.1.
S45679 mRNA. Translation: AAB23543.1.
AK291556 mRNA. Translation: BAF84245.1.
BC031999 mRNA. Translation: AAH31999.1.
PIRDEHUHS. A36551.
RefSeqNP_000853.1. NM_000862.2.
UniGeneHs.364941.

3D structure databases

ProteinModelPortalP14060.
SMRP14060. Positions 5-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000358421.

Chemistry

BindingDBP14060.
ChEMBLCHEMBL1958.
DrugBankDB00157. NADH.
DB01108. Trilostane.

PTM databases

PhosphoSiteP14060.

Polymorphism databases

DMDM112767.

Proteomic databases

PaxDbP14060.
PRIDEP14060.

Protocols and materials databases

DNASU3283.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369413; ENSP00000358421; ENSG00000203857.
ENST00000528909; ENSP00000432268; ENSG00000203857.
GeneID3283.
KEGGhsa:3283.
UCSCuc001ehv.1. human.

Organism-specific databases

CTD3283.
GeneCardsGC01P120049.
H-InvDBHIX0028579.
HGNCHGNC:5217. HSD3B1.
HPAHPA043261.
HPA043264.
HPA044028.
MIM109715. gene.
neXtProtNX_P14060.
PharmGKBPA29486.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0451.
HOGENOMHOG000167989.
HOVERGENHBG000014.
InParanoidP14060.
KOK00070.
PhylomeDBP14060.
TreeFamTF343138.

Enzyme and pathway databases

BioCycMetaCyc:HS08829-MONOMER.
BRENDA1.1.1.145. 2681.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
SABIO-RKP14060.
UniPathwayUPA00062.

Gene expression databases

ArrayExpressP14060.
BgeeP14060.
CleanExHS_HSD3B1.
GenevestigatorP14060.

Family and domain databases

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

Other

GeneWikiHSD3B1.
GenomeRNAi3283.
NextBio13031.
PROP14060.
SOURCESearch...

Entry information

Entry name3BHS1_HUMAN
AccessionPrimary (citable) accession number: P14060
Secondary accession number(s): A8K691, Q14545, Q8IV65
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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