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UniProtKB/Swiss-Prot entry P37059

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHB2_HUMAN
Primary accession number P37059
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 2
Synonyms EC 1.1.1.62
Testosterone 17-beta-dehydrogenase
EC 1.1.1.63
Microsomal 17-beta-hydroxysteroid dehydrogenase
17-beta-HSD 2
20 alpha-hydroxysteroid dehydrogenase
20-alpha-HSD
E2DH
Gene name
Name: HSD17B2
Synonyms: EDH17B2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Prostate;
PubMed=8099587 [NCBI, ExPASy, EBI, Israel, Japan]
Wu L., Einstein M., Geissler W.M., Chan H.K., Elliston K.O., Andersson S.;
"Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity.";
J. Biol. Chem. 268:12964-12969(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7546291 [NCBI, ExPASy, EBI, Israel, Japan]
Labrie Y., Durocher F., Lachance Y., Turgeon C., Simard J., Labrie C., Labrie F.;
"The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species.";
DNA Cell Biol. 14:849-862(1995).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-121.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
Comments
  • FUNCTION: Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH.
  • CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.
  • CATALYTIC ACTIVITY: Testosterone + NAD+ = androst-4-ene-3,17-dione + NADH.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=0.21 µM for estradiol;
    KM=0.39 µM for testosterone;
    KM=0.31 µM for dihydrotestosterone;
    KM=0.71 µM for 20-alpha-dihydroprogesterone;
    KM=0.78 µM for estrone;
    KM=2.63 µM for androstenedione;
    Vmax=38 nmol/min/mg enzyme with estradiol as substrate;
    Vmax=45 nmol/min/mg enzyme with testosterone as substrate;
    Vmax=38 nmol/min/mg enzyme with dihydrotestosterone as substrate;
    Vmax=5.6 nmol/min/mg enzyme with 20-alpha-dihydroprogesterone as substrate;
    Vmax=6.6 nmol/min/mg enzyme with estrone as substrate;
    Vmax=11.5 nmol/min/mg enzyme with androstenedione as substrate;
  • SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein (Potential).
  • SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L11708; AAA03562.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40802; AAC41917.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40796; AAC41917.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40797; AAC41917.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40798; AAC41917.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40801; AAC41917.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY325910; AAP78485.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009581; AAH09581.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059170; AAH59170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A47287; A47287.
RefSeq NP_002144.1; -.
UniGene Hs.162795
3D structure databases
ModBase P37059.
PTM databases
PhosphoSite P37059; -.
Polymorphism databases
NIEHS-SNPs HSD17B2.
Organism-specific databases
H-InvDB HIX0013279; -.
HGNC HGNC:5211; HSD17B2.
GenAtlas HSD17B2.
MIM 109685; gene. [NCBI / EBI]
PharmGKB PA29479; -.
GeneCards P37059.
Gene expression databases
ArrayExpress P37059; -.
CleanEx HS_HSD17B2; -.
GermOnline ENSG00000086696; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (traceable author statement from ProtInc).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0047006; Molecular function: 20-alpha-hydroxysteroid dehydrogenase activity (traceable author statement from UniProtKB).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0050327; Molecular function: testosterone 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0032526; Biological process: response to retinoic acid (inferred from direct assay from UniProtKB).
GO:0006694; Biological process: steroid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
ProtoNet P37059.
Proteomic databases
PeptideAtlas P37059; -.
Genome annotation databases
Ensembl ENSG00000086696; Homo sapiens. [Contig view]
GeneID 3294; -.
KEGG hsa:3294; -.
Phylogenomic databases
HOGENOM P37059; -.
HOVERGEN P37059; -.
Other
DrugBank DB00157; NADH.
NextBio 13067; -.
SOURCE HSD17B2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Lipid synthesis; Membrane; NAD; Oxidoreductase; Phosphoprotein; Polymorphism; Signal-anchor; Steroid biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   387  387     Estradiol 17-beta-dehydrogenase 2. PRO_0000054570
TRANSMEM   4    24  21     Signal-anchor for type II membrane protein (Potential). 
NP_BIND   82   111  30     NAD (By similarity). 
ACT_SITE   232   232        By similarity. 
BINDING   219   219        Substrate (By similarity). 
MOD_RES   273   273        Phosphoserine. 
VARIANT   121   121  1     A -> T (in dbSNP:rs8191136 [NCBI]). VAR_018852 
Sequence information
Length: 387 AA [This is the length of the unprocessed precursor] Molecular weight: 42785 Da [This is the MW of the unprocessed precursor] CRC64: EDE5606EA041042B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTFFSDTAW ICLAVPTVLC GTVFCKYKKS SGQLWSWMVC LAGLCAVCLL ILSPFWGLIL 

        70         80         90        100        110        120 
FSVSCFLMYT YLSGQELLPV DQKAVLVTGG DCGLGHALCK YLDELGFTVF AGVLNENGPG 

       130        140        150        160        170        180 
AEELRRTCSP RLSVLQMDIT KPVQIKDAYS KVAAMLQDRG LWAVINNAGV LGFPTDGELL 

       190        200        210        220        230        240 
LMTDYKQCMA VNFFGTVEVT KTFLPLLRKS KGRLVNVSSM GGGAPMERLA SYGSSKAAVT 

       250        260        270        280        290        300 
MFSSVMRLEL SKWGIKVASI QPGGFLTNIA GTSDKWEKLE KDILDHLPAE VQEDYGQDYI 

       310        320        330        340        350        360 
LAQRNFLLLI NSLASKDFSP VLRDIQHAIL AKSPFAYYTP GKGAYLWICL AHYLPIGIYD 

       370        380 
YFAKRHFGQD KPMPRALRMP NYKKKAT
P37059 in FASTA format

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