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P14060

- 3BHS1_HUMAN

UniProt

P14060 - 3BHS1_HUMAN

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Protein

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

Gene
HSD3B1, 3BH, HSDB3A
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei155 – 1551Proton acceptor By similarity
Binding sitei159 – 1591NAD By similarity

GO - Molecular functioni

  1. 3-beta-hydroxy-delta5-steroid dehydrogenase activity Source: UniProtKB
  2. steroid delta-isomerase activity Source: UniProtKB

GO - Biological processi

  1. androgen biosynthetic process Source: UniProtKB
  2. estrogen biosynthetic process Source: UniProtKB
  3. glucocorticoid biosynthetic process Source: Reactome
  4. mineralocorticoid biosynthetic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. steroid biosynthetic process Source: UniProtKB
  7. 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.
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:5217. HSD3B1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei288 – 30821Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrial intermembrane space Source: UniProtKB
  5. smooth endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29486.

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

ArrayExpressiP14060.
BgeeiP14060.
CleanExiHS_HSD3B1.
GenevestigatoriP14060.

Organism-specific databases

HPAiHPA043261.
HPA043264.
HPA044028.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000358421.

Structurei

3D structure databases

ProteinModelPortaliP14060.
SMRiP14060. Positions 7-159.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-beta-HSD family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0451.
HOGENOMiHOG000167989.
HOVERGENiHBG000014.
InParanoidiP14060.
KOiK00070.
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

MTGWSCLVTG AGGFLGQRII RLLVKEKELK EIRVLDKAFG PELREEFSKL    50
QNKTKLTVLE GDILDEPFLK RACQDVSVII HTACIIDVFG VTHRESIMNV 100
NVKGTQLLLE ACVQASVPVF IYTSSIEVAG PNSYKEIIQN GHEEEPLENT 150
WPAPYPHSKK LAEKAVLAAN GWNLKNGGTL YTCALRPMYI YGEGSRFLSA 200
SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL QDPKKAPSIR 250
GQFYYISDDT PHQSYDNLNY TLSKEFGLRL DSRWSFPLSL MYWIGFLLEI 300
VSFLLRPIYT YRPPFNRHIV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK 350
QKTVEWVGSL VDRHKETLKS KTQ 373
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.

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi112767.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS903.1.
PIRi A36551. DEHUHS.
RefSeqi NP_000853.1. NM_000862.2.
UniGenei Hs.364941.

3D structure databases

ProteinModelPortali P14060.
SMRi P14060. Positions 7-159.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000358421.

Chemistry

BindingDBi P14060.
ChEMBLi CHEMBL1958.
DrugBanki DB00157. NADH.
DB01108. Trilostane.

PTM databases

PhosphoSitei P14060.

Polymorphism databases

DMDMi 112767.

Proteomic databases

PaxDbi P14060.
PRIDEi P14060.

Protocols and materials databases

DNASUi 3283.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369413 ; ENSP00000358421 ; ENSG00000203857 .
ENST00000528909 ; ENSP00000432268 ; ENSG00000203857 .
GeneIDi 3283.
KEGGi hsa:3283.
UCSCi uc001ehv.1. human.

Organism-specific databases

CTDi 3283.
GeneCardsi GC01P120049.
H-InvDB HIX0028579.
HGNCi HGNC:5217. HSD3B1.
HPAi HPA043261.
HPA043264.
HPA044028.
MIMi 109715. gene.
neXtProti NX_P14060.
PharmGKBi PA29486.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0451.
HOGENOMi HOG000167989.
HOVERGENi HBG000014.
InParanoidi P14060.
KOi K00070.
PhylomeDBi P14060.
TreeFami TF343138.

Enzyme and pathway databases

UniPathwayi UPA00062 .
BioCyci MetaCyc:HS08829-MONOMER.
BRENDAi 1.1.1.145. 2681.
Reactomei REACT_11036. Glucocorticoid biosynthesis.
REACT_11047. Mineralocorticoid biosynthesis.
REACT_11059. Androgen biosynthesis.
SABIO-RK P14060.

Miscellaneous databases

GeneWikii HSD3B1.
GenomeRNAii 3283.
NextBioi 13031.
PROi P14060.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14060.
Bgeei P14060.
CleanExi HS_HSD3B1.
Genevestigatori P14060.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01073. 3Beta_HSD. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 154 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

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