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Protein

3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1

Gene

HSD3B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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:isteroid 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551Proton acceptorBy similarity
Binding sitei159 – 1591NADBy similarity

GO - Molecular functioni

  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity Source: UniProtKB
  • steroid delta-isomerase activity Source: UniProtKB

GO - Biological processi

  • androgen biosynthetic process Source: UniProtKB
  • estrogen biosynthetic process Source: UniProtKB
  • glucocorticoid biosynthetic process Source: Reactome
  • mineralocorticoid biosynthetic process Source: Reactome
  • small molecule metabolic process Source: Reactome
  • steroid biosynthetic process Source: UniProtKB
  • steroid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Biological processi

Steroidogenesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS08829-MONOMER.
BRENDAi1.1.1.145. 2681.
5.3.3.1. 2681.
ReactomeiREACT_11036. Glucocorticoid biosynthesis.
REACT_11047. Mineralocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
SABIO-RKP14060.
UniPathwayiUPA00062.

Names & Taxonomyi

Protein namesi
Recommended 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:
3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC:1.1.1.145)
Alternative name(s):
3-beta-hydroxy-5-ene steroid dehydrogenase
Progesterone reductase
Steroid Delta-isomerase (EC:5.3.3.1)
Alternative name(s):
Delta-5-3-ketosteroid isomerase
Gene namesi
Name:HSD3B1
Synonyms:3BH, HSDB3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5217. HSD3B1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29486.

Chemistry

DrugBankiDB01108. Trilostane.

Polymorphism and mutation databases

BioMutaiHSD3B1.
DMDMi112767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 3733723 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1PRO_0000087774Add
BLAST

Proteomic databases

PaxDbiP14060.
PRIDEiP14060.

PTM databases

PhosphoSiteiP14060.

Expressioni

Tissue specificityi

Placenta and skin. Predominantly expressed in mammary gland tissue.

Gene expression databases

BgeeiP14060.
CleanExiHS_HSD3B1.
ExpressionAtlasiP14060. baseline and differential.
GenevisibleiP14060. HS.

Organism-specific databases

HPAiHPA043261.
HPA043264.
HPA044028.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000358421.

Structurei

3D structure databases

ProteinModelPortaliP14060.
SMRiP14060. Positions 3-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-beta-HSD family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
HOVERGENiHBG000014.
KOiK00070.
OMAiMEYSEMY.
PhylomeDBiP14060.
TreeFamiTF343138.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14060-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGWSCLVTG AGGFLGQRII RLLVKEKELK EIRVLDKAFG PELREEFSKL
60 70 80 90 100
QNKTKLTVLE GDILDEPFLK RACQDVSVII HTACIIDVFG VTHRESIMNV
110 120 130 140 150
NVKGTQLLLE ACVQASVPVF IYTSSIEVAG PNSYKEIIQN GHEEEPLENT
160 170 180 190 200
WPAPYPHSKK LAEKAVLAAN GWNLKNGGTL YTCALRPMYI YGEGSRFLSA
210 220 230 240 250
SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL QDPKKAPSIR
260 270 280 290 300
GQFYYISDDT PHQSYDNLNY TLSKEFGLRL DSRWSFPLSL MYWIGFLLEI
310 320 330 340 350
VSFLLRPIYT YRPPFNRHIV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK
360 370
QKTVEWVGSL VDRHKETLKS KTQ
Length:373
Mass (Da):42,252
Last modified:January 23, 2007 - v2
Checksum:i2C76616E7EA7433A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541T → I.
Corresponds to variant rs3088283 [ dbSNP | Ensembl ].
VAR_048096
Natural varianti71 – 711R → I.
Corresponds to variant rs4986952 [ dbSNP | Ensembl ].
VAR_048097
Natural varianti79 – 791I → V.1 Publication
Corresponds to variant rs6201 [ dbSNP | Ensembl ].
VAR_014174
Natural varianti90 – 901G → S.
Corresponds to variant rs6684974 [ dbSNP | Ensembl ].
VAR_048098
Natural varianti286 – 2861F → L.1 Publication
Corresponds to variant rs6205 [ dbSNP | Ensembl ].
VAR_014175
Natural varianti367 – 3671T → N.2 Publications
Corresponds to variant rs1047303 [ dbSNP | Ensembl ].
VAR_000005

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS903.1.
PIRiA36551. DEHUHS.
RefSeqiNP_000853.1. NM_000862.2.
UniGeneiHs.364941.

Genome annotation databases

EnsembliENST00000369413; ENSP00000358421; ENSG00000203857.
ENST00000528909; ENSP00000432268; ENSG00000203857.
GeneIDi3283.
KEGGihsa:3283.
UCSCiuc001ehv.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS903.1.
PIRiA36551. DEHUHS.
RefSeqiNP_000853.1. NM_000862.2.
UniGeneiHs.364941.

3D structure databases

ProteinModelPortaliP14060.
SMRiP14060. Positions 3-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000358421.

Chemistry

BindingDBiP14060.
ChEMBLiCHEMBL1958.
DrugBankiDB01108. Trilostane.

PTM databases

PhosphoSiteiP14060.

Polymorphism and mutation databases

BioMutaiHSD3B1.
DMDMi112767.

Proteomic databases

PaxDbiP14060.
PRIDEiP14060.

Protocols and materials databases

DNASUi3283.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369413; ENSP00000358421; ENSG00000203857.
ENST00000528909; ENSP00000432268; ENSG00000203857.
GeneIDi3283.
KEGGihsa:3283.
UCSCiuc001ehv.1. human.

Organism-specific databases

CTDi3283.
GeneCardsiGC01P120049.
H-InvDBHIX0028579.
HGNCiHGNC:5217. HSD3B1.
HPAiHPA043261.
HPA043264.
HPA044028.
MIMi109715. gene.
neXtProtiNX_P14060.
PharmGKBiPA29486.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
HOVERGENiHBG000014.
KOiK00070.
OMAiMEYSEMY.
PhylomeDBiP14060.
TreeFamiTF343138.

Enzyme and pathway databases

UniPathwayiUPA00062.
BioCyciMetaCyc:HS08829-MONOMER.
BRENDAi1.1.1.145. 2681.
5.3.3.1. 2681.
ReactomeiREACT_11036. Glucocorticoid biosynthesis.
REACT_11047. Mineralocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
SABIO-RKP14060.

Miscellaneous databases

GeneWikiiHSD3B1.
GenomeRNAii3283.
NextBioi13031.
PROiP14060.
SOURCEiSearch...

Gene expression databases

BgeeiP14060.
CleanExiHS_HSD3B1.
ExpressionAtlasiP14060. baseline and differential.
GenevisibleiP14060. HS.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: VARIANTS VAL-79 AND LEU-286.

Entry informationi

Entry namei3BHS1_HUMAN
AccessioniPrimary (citable) accession number: P14060
Secondary accession number(s): A8K691, Q14545, Q8IV65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.