Reviewed, UniProtKB/Swiss-Prot P37059 (DHB2_HUMAN)

Names and origin

Protein names

Recommended name:
    Estradiol 17-beta-dehydrogenase 2
    EC=1.1.1.62
Alternative name(s):
    Testosterone 17-beta-dehydrogenase
    EC=1.1.1.63
    Microsomal 17-beta-hydroxysteroid dehydrogenase
    17-beta-HSD 2
    20 alpha-hydroxysteroid dehydrogenase
      Short name=20-alpha-HSD
    E2DH

Gene names

Name:	HSD17B2
Synonyms:	EDH17B2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Testosterone + NAD+ = androst-4-ene-3,17-dione + NADH.
Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
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

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to retinoic acid Inferred from direct assay. Source: UniProtKB steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.1 Traceable author statement. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	20-alpha-hydroxysteroid dehydrogenase activity Traceable author statement. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro estradiol 17-beta-dehydrogenase activity Inferred from direct assay. Source: UniProtKB testosterone 17-beta-dehydrogenase activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Estradiol 17-beta-dehydrogenase 2		PRO_0000054570
Regions
	Transmembrane	4 – 24	21	Signal-anchor for type II membrane protein Potential
	Nucleotide binding	82 – 111	30	NAD By similarity
Sites
	Active site	232	1	By similarity
	Binding site	219	1	Substrate By similarity
Amino acid modifications
	Modified residue	273	1	Phosphoserine Ref.7
Natural variations
	Natural variant	121	1	A → T: dbSNP rs8191136. Ref.3		VAR_018852

Sequences

	Sequence		Length	Mass (Da)
	P37059-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: EDE5606EA041042B	FASTA	387	42,785
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity." Wu L., Einstein M., Geissler W.M., Chan H.K., Elliston K.O., Andersson S. J. Biol. Chem. 268:12964-12969(1993) [PubMed: 8099587] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Prostate.
[2]	"The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species." Labrie Y., Durocher F., Lachance Y., Turgeon C., Simard J., Labrie C., Labrie F. DNA Cell Biol. 14:849-862(1995) [PubMed: 7546291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	NIEHS SNPs program Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-121.
[4]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, MASS SPECTROMETRY. Tissue: Epithelium.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	L11708 mRNA. Translation: AAA03562.1. L40802 , L40796, L40797, L40798, L40801 Genomic DNA. Translation: AAC41917.1. AY325910 Genomic DNA. Translation: AAP78485.1. AK313109 mRNA. Translation: BAG35931.1. CH471114 Genomic DNA. Translation: EAW95519.1. BC009581 mRNA. Translation: AAH09581.1. BC059170 mRNA. Translation: AAH59170.1.
IPI	IPI00019872.
PIR	A47287.
RefSeq	NP_002144.1.
UniGene	Hs.162795
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P37059.
Proteomic databases
PeptideAtlas	P37059.
PRIDE	P37059.
Genome annotation databases
Ensembl	ENST00000199936; ENSP00000199936; ENSG00000086696; Homo sapiens. [Genome view]
GeneID	3294.
KEGG	hsa:3294.
UCSC	uc002fgv.1. human.
Organism-specific databases
CTD	3294.
GeneCards	GC16P080626.
H-InvDB	HIX0013279.
HGNC	HGNC:5211. HSD17B2.
MIM	109685. gene.
PharmGKB	PA29479.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P37059.
HOVERGEN	P37059.
OMA	QEDYGQD.
Enzyme and pathway databases
BRENDA	1.1.1.62. 247. 1.1.1.63. 247.
Gene expression databases
ArrayExpress	P37059.
Bgee	P37059.
CleanEx	HS_HSD17B2.
Genevestigator	P37059.
GermOnline	ENSG00000086696. Homo sapiens.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00157. NADH.
NextBio	13067.
SOURCE	Search...

Entry information

Entry name

DHB2_HUMAN

Accession

Primary (citable) accession number: P37059
Secondary accession number(s): B2R7T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.