P14061 (DHB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Estradiol 17-beta-dehydrogenase 1
EC=1.1.1.62

Alternative name(s):
17-beta-hydroxysteroid dehydrogenase type 1
Short name=17-beta-HSD 1
20 alpha-hydroxysteroid dehydrogenase
Short name=20-alpha-HSD
E2DH
Placental 17-beta-hydroxysteroid dehydrogenase

Gene names

Name:	HSD17B1
Synonyms:	E17KSR, EDH17B1, EDH17B2, EDHB17

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH.
Catalytic activity	Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.
Pathway	Steroid biosynthesis; estrogen biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	estrogen biosynthetic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	estradiol 17-beta-dehydrogenase activity Traceable author statement. Source: Reactome nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 328

327

Estradiol 17-beta-dehydrogenase 1

PRO_0000054567

Regions

Nucleotide binding

10 – 38

29

NADP

Sites

Active site

156

1

Proton acceptor

Binding site

66

1

NADP

Binding site

143

1

Substrate

Binding site

160

1

NADP

Natural variations

Natural variant

238

1

A → V. Ref.25

VAR_006951

Natural variant

313

1

G → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.25
Corresponds to variant rs605059 [ dbSNP | Ensembl ].

VAR_006952

Experimental info

Mutagenesis

150

1

L → V: Alters substrate specificity. Ref.21

Sequence conflict

3

1

R → E AA sequence Ref.11

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

14 – 24

11

Beta strand

31 – 39

9

Helix

40 – 42

3

Helix

44 – 52

9

Beta strand

59 – 64

6

Helix

70 – 78

9

Beta strand

86 – 90

5

Helix

100 – 102

3

Helix

105 – 115

11

Helix

117 – 133

17

Beta strand

136 – 143

8

Helix

144 – 146

3

Helix

154 – 174

21

Helix

175 – 177

3

Beta strand

179 – 186

8

Beta strand

189 – 192

4

Turn

193 – 196

4

Helix

201 – 207

7

Helix

210 – 230

21

Helix

234 – 246

13

Beta strand

252 – 256

5

Helix

261 – 265

5

Turn

266 – 268

3

Helix

274 – 285

12

Sequences

	Sequence		Length	Mass (Da)
	P14061 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 5B5C8909F9120832	FASTA	328	34,950
	10 20 30 40 50 60 MARTVVLITG CSSGIGLHLA VRLASDPSQS FKVYATLRDL KTQGRLWEAA RALACPPGSL 70 80 90 100 110 120 ETLQLDVRDS KSVAAARERV TEGRVDVLVC NAGLGLLGPL EALGEDAVAS VLDVNVVGTV 130 140 150 160 170 180 RMLQAFLPDM KRRGSGRVLV TGSVGGLMGL PFNDVYCASK FALEGLCESL AVLLLPFGVH 190 200 210 220 230 240 LSLIECGPVH TAFMEKVLGS PEEVLDRTDI HTFHRFYQYL AHSKQVFREA AQNPEEVAEV 250 260 270 280 290 300 FLTALRAPKP TLRYFTTERF LPLLRMRLDD PSGSNYVTAM HREVFGDVPA KAEAGAEAGG 310 320 GAGPGAEDEA GRGAVGDPEL GDPPAAPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA." Peltoketo H., Isomaa V., Maeentausta O., Vihko R. FEBS Lett. 239:73-77(1988) [PubMed: 2846351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313. Tissue: Placenta.
[2]	"Characterization of cDNAs for human estradiol 17 beta-dehydrogenase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5'-termini in human placenta." Luu-The V., Labrie C., Zhao H.F., Couet J., Lachance Y., Simard J., Leblanc G., Labrie F. Mol. Endocrinol. 3:1301-1309(1989) [PubMed: 2779584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313. Tissue: Placenta.
[3]	"Structure of two in tandem human 17 beta-hydroxysteroid dehydrogenase genes." Luu-The V., Labrie C., Simard J., Lachance Y., Zhao H.F., Couet J., Leblanc G., Labrie F. Mol. Endocrinol. 4:268-275(1990) [PubMed: 2330005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
[4]	"Purification, cloning, complementary DNA structure, and predicted amino acid sequence of human estradiol 17 beta-dehydrogenase." Luu-The V., Labrie C., Zhao H.F., Couet J., Lachance Y., Simard J., Cote J., Leblanc G., Lagace L., Berube D., Gagne R., Labrie F. Ann. N. Y. Acad. Sci. 595:40-52(1990) [PubMed: 2197970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313.
[5]	"Genomic organization and DNA sequences of human 17 beta-hydroxysteroid dehydrogenase genes and flanking regions. Localization of multiple Alu sequences and putative cis-acting elements." Peltoketo H.E., Isomma V., Vihko R. Eur. J. Biochem. 209:459-466(1992) [PubMed: 1327779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
[6]	Shen Y., Gibbs R.A. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-313. Tissue: Placenta.
[8]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-313.
[10]	"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], VARIANT SER-313. Tissue: Brain.
[11]	"Amino acid composition and subunit structure. Human placental 17 - estradiol dehydrogenase." Burns D.J.W., Engel L.L., Bethune J.L. Biochemistry 11:2699-2703(1972) [PubMed: 5045524] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6.
[12]	"Human placental 17 -oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteine." Nicholas J.C., Harris J.I. FEBS Lett. 29:173-176(1973) [PubMed: 4719204] [Abstract] Cited for: PROTEIN SEQUENCE OF 52-68.
[13]	"Human placental estradiol 17 beta-dehydrogenase: sequence of a histidine-bearing peptide in the catalytic region." Murdock G.L., Chin C.-C., Warren J.C. Biochemistry 25:641-646(1986) [PubMed: 3456799] [Abstract] Cited for: PROTEIN SEQUENCE OF 205-224.
[14]	"Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione." Murdock G.L., Chin C.C., Offord R.E., Bradshaw R.A., Warren J.C. J. Biol. Chem. 258:11460-11464(1983) [PubMed: 6578212] [Abstract] Cited for: PROTEIN SEQUENCE OF 220-224.
[15]	"Human placental 17 beta-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti." Baker M.E. Mol. Endocrinol. 3:881-884(1989) [PubMed: 2547159] [Abstract] Cited for: SIMILARITY TO SHORT CHAIN DEHYDROGENASES.
[16]	"Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20-A resolution." Ghosh D., Pletnev V.Z., Zhu D.W., Wawrzak Z., Duax W.L., Pangborn W., Labrie F., Lin S.-X. Structure 3:503-513(1995) [PubMed: 7663947] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[17]	"Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol." Azzi A., Rehse P.H., Zhu D.W., Campbell R.L., Labrie F., Lin S.X. Nat. Struct. Biol. 3:665-668(1996) [PubMed: 8756321] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[18]	"The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors." Breton R., Housset D., Mazza C., Fontecilla-Camps J.-C. Structure 4:905-915(1996) [PubMed: 8805577] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP.
[19]	"Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase." Mazza C., Breton R., Housset D., Fontecilla-Camps J.-C. J. Biol. Chem. 273:8145-8152(1998) [PubMed: 9525918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[20]	"Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+." Sawicki M.W., Erman M., Puranen T., Vihko P., Ghosh D. Proc. Natl. Acad. Sci. U.S.A. 96:840-845(1999) [PubMed: 9927655] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[21]	"Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain." Han Q., Campbell R.L., Gangloff A., Huang Y.-W., Lin S.-X. J. Biol. Chem. 275:1105-1111(2000) [PubMed: 10625652] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 39-328, MUTAGENESIS OF LEU-150.
[22]	"A concerted, rational design of type 1 17beta-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity." Qiu W., Campbell R.L., Gangloff A., Dupuis P., Boivin R.P., Tremblay M.R., Poirier D., Lin S.X. FASEB J. 16:1829-1831(2002) [PubMed: 12223444] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[23]	"Pseudo-symmetry of C19 steroids, alternative binding orientations, and multispecificity in human estrogenic 17beta-hydroxysteroid dehydrogenase." Gangloff A., Shi R., Nahoum V., Lin S.X. FASEB J. 17:274-276(2003) [PubMed: 12490543] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
[24]	"Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation." Shi R., Lin S.X. J. Biol. Chem. 279:16778-16785(2004) [PubMed: 14966133] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS).
[25]	"Detection of polymorphisms in the estradiol 17 beta-hydroxysteroid dehydrogenase II gene at the EDH17B2 locus on 17q11-q21." Normand T., Narod S., Labrie F., Simard J. Hum. Mol. Genet. 2:479-483(1993) [PubMed: 8389226] [Abstract] Cited for: VARIANTS VAL-238 AND SER-313.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13440 mRNA. Translation: CAA31792.1.
M36263 mRNA. Translation: AAA35600.1.
M27138 Genomic DNA. Translation: AAB16941.1.
M84472 Genomic DNA. Translation: AAB16942.1.
U34879 Genomic DNA. Translation: AAD05019.1.
AK127832 mRNA. Translation: BAG54583.1.
AC067852 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60836.1.
BC104752 mRNA. Translation: AAI04753.1.
BC111935 mRNA. Translation: AAI11936.1.

IPI

IPI00218721.

PIR

DEHUE7. A36081.

RefSeq

NP_000404.2. NM_000413.2.

UniGene

Hs.654385.
Hs.655222.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A27	X-ray	1.90	A	2-289	[»]
1BHS	X-ray	2.20	A	2-328	[»]
1DHT	X-ray	2.24	A	2-328	[»]
1EQU	X-ray	3.00	A/B	2-328	[»]
1FDS	X-ray	1.70	A	2-328	[»]
1FDT	X-ray	2.20	A	2-328	[»]
1FDU	X-ray	2.70	A/B/C/D	2-328	[»]
1FDV	X-ray	3.10	A/B/C/D	2-328	[»]
1FDW	X-ray	2.70	A	2-328	[»]
1I5R	X-ray	1.60	A	2-328	[»]
1IOL	X-ray	2.30	A	2-328	[»]
1JTV	X-ray	1.54	A	2-328	[»]
1QYV	X-ray	1.81	A	2-328	[»]
1QYW	X-ray	1.63	A	2-328	[»]
1QYX	X-ray	1.89	A	2-328	[»]
3DEY	X-ray	1.70	X	2-328	[»]
3DHE	X-ray	2.30	A	2-328	[»]
3HB4	X-ray	2.21	X	2-328	[»]
3HB5	X-ray	2.00	X	2-328	[»]
3KLM	X-ray	1.70	X	2-328	[»]
3KLP	X-ray	2.50	X	2-328	[»]
3KM0	X-ray	2.30	A/B	2-328	[»]

ProteinModelPortal

P14061.

SMR

P14061. Positions 2-286.

DisProt

DP00023.

ModBase

Search...

Protein-protein interaction databases

STRING

P14061.

Polymorphism databases

DMDM

118554.

Proteomic databases

PRIDE

P14061.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225929; ENSP00000225929; ENSG00000108786.

GeneID

3292.

KEGG

hsa:3292.

UCSC

uc002hzw.1. human.

Organism-specific databases

CTD

3292.

GeneCards

GC17P040701.

H-InvDB

HIX0202506.

HGNC

HGNC:5210. HSD17B1.

HPA

HPA021032.

MIM

109684. gene.

neXtProt

NX_P14061.

PharmGKB

PA29478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13283.

GeneTree

ENSGT00600000084310.

HOGENOM

HBG750976.

HOVERGEN

HBG014077.

InParanoid

P14061.

OMA

HTAFYEK.

OrthoDB

EOG45MN61.

PhylomeDB

P14061.

Enzyme and pathway databases

Reactome

REACT_15493. Steroid hormones.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P14061.

Bgee

P14061.

CleanEx

HS_HSD17B1.

Genevestigator

P14061.

GermOnline

ENSG00000108786. Homo sapiens.

Family and domain databases

InterPro

IPR011348. 17beta_DH.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K00044.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PIRSF

PIRSF000095. 17beta-HSD. 1 hit.

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00157. NADH.

NextBio

13059.

SOURCE

Search...

Entry information

Entry name

DHB1_HUMAN

Accession

Primary (citable) accession number: P14061
Secondary accession number(s): B3KXS1, Q2M2L8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 30, 2010
Last modified:	January 25, 2012
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.