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P14061 (DHB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

17-beta-estradiol + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 328327Estradiol 17-beta-dehydrogenase 1
PRO_0000054567

Regions

Nucleotide binding10 – 3829NADP

Sites

Active site1561Proton acceptor
Binding site661NADP
Binding site1431Substrate
Binding site1601NADP

Natural variations

Natural variant2381A → V. Ref.25
VAR_006951
Natural variant3131G → 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

Mutagenesis1501L → V: Alters substrate specificity. Ref.21
Sequence conflict31R → E AA sequence Ref.11

Secondary structure

............................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14061 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 5B5C8909F9120832

FASTA32834,950
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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], 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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS11428.1.
PIRDEHUE7. A36081.
RefSeqNP_000404.2. NM_000413.2.
UniGeneHs.654385.
Hs.655222.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A27X-ray1.90A2-290[»]
1BHSX-ray2.20A2-328[»]
1DHTX-ray2.24A2-328[»]
1EQUX-ray3.00A/B2-328[»]
1FDSX-ray1.70A2-328[»]
1FDTX-ray2.20A2-328[»]
1FDUX-ray2.70A/B/C/D2-328[»]
1FDVX-ray3.10A/B/C/D2-328[»]
1FDWX-ray2.70A2-328[»]
1I5RX-ray1.60A2-328[»]
1IOLX-ray2.30A2-328[»]
1JTVX-ray1.54A2-328[»]
1QYVX-ray1.81A2-328[»]
1QYWX-ray1.63A2-328[»]
1QYXX-ray1.89A2-328[»]
3DEYX-ray1.70X2-328[»]
3DHEX-ray2.30A2-328[»]
3HB4X-ray2.21X2-328[»]
3HB5X-ray2.00X2-328[»]
3KLMX-ray1.70X2-328[»]
3KLPX-ray2.50X2-328[»]
3KM0X-ray2.30A/B2-328[»]
DisProtDP00023.
ProteinModelPortalP14061.
SMRP14061. Positions 2-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109525. 1 interaction.
STRING9606.ENSP00000225929.

Chemistry

BindingDBP14061.
ChEMBLCHEMBL3181.
DrugBankDB00157. NADH.

Polymorphism databases

DMDM313104233.

Proteomic databases

PaxDbP14061.
PRIDEP14061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000585807; ENSP00000466799; ENSG00000108786.
GeneID3292.
KEGGhsa:3292.
UCSCuc002hzw.3. human.

Organism-specific databases

CTD3292.
GeneCardsGC17P040701.
H-InvDBHIX0202506.
HGNCHGNC:5210. HSD17B1.
HPAHPA021032.
MIM109684. gene.
neXtProtNX_P14061.
PharmGKBPA29478.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG014077.
InParanoidP14061.
KOK00044.
OrthoDBEOG76T9RW.
PhylomeDBP14061.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15493. Steroid hormones.
SABIO-RKP14061.
UniPathwayUPA00769.

Gene expression databases

ArrayExpressP14061.
BgeeP14061.
CleanExHS_HSD17B1.
GenevestigatorP14061.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011348. 17beta_DH.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFPIRSF000095. 17beta-HSD. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14061.
GeneWikiHSD17B1.
GenomeRNAi3292.
NextBio13059.
PROP14061.
SOURCESearch...

Entry information

Entry nameDHB1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM