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Protein

Estradiol 17-beta-dehydrogenase 11

Gene

HSD17B11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell lymphoma.

Catalytic activityi

17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721SubstrateBy similarity
Active sitei185 – 1851Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 6425NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • estradiol 17-beta-dehydrogenase activity Source: Reactome
  • steroid dehydrogenase activity Source: HGNC

GO - Biological processi

  • androgen catabolic process Source: HGNC
  • estrogen biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-HSA-193144. Estrogen biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Estradiol 17-beta-dehydrogenase 11 (EC:1.1.1.62)
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 11
Short name:
17-beta-HSD 11
Short name:
17bHSD11
Short name:
17betaHSD11
17-beta-hydroxysteroid dehydrogenase XI
Short name:
17-beta-HSD XI
Short name:
17betaHSDXI
Cutaneous T-cell lymphoma-associated antigen HD-CL-03
Short name:
CTCL-associated antigen HD-CL-03
Dehydrogenase/reductase SDR family member 8
Retinal short-chain dehydrogenase/reductase 2
Short name:
retSDR2
Short chain dehydrogenase/reductase family 16C member 2
Gene namesi
Name:HSD17B11
Synonyms:DHRS8, PAN1B, SDR16C2
ORF Names:PSEC0029, UNQ207/PRO233
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:22960. HSD17B11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • extracellular region Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: HPA
  • lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391655.

Polymorphism and mutation databases

BioMutaiHSD17B11.
DMDMi296439374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 300281Estradiol 17-beta-dehydrogenase 11PRO_0000031970Add
BLAST

Proteomic databases

EPDiQ8NBQ5.
MaxQBiQ8NBQ5.
PaxDbiQ8NBQ5.
PRIDEiQ8NBQ5.

PTM databases

iPTMnetiQ8NBQ5.
PhosphoSiteiQ8NBQ5.

Expressioni

Tissue specificityi

Present at high level in steroidogenic cells such as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa cells of the dominant follicle and corpus luteum. In lung, it is detected in the ciliated epithelium and in acini of adult trachea, in bronchioles, but not in alveoli. In the eye, it is detected in the nonpigmented epithelium of the ciliary body and, at lower level, in the inner nuclear layer of the retina (at protein level). Widely expressed. Highly expressed in retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart.4 Publications

Gene expression databases

BgeeiQ8NBQ5.
CleanExiHS_HSD17B11.
ExpressionAtlasiQ8NBQ5. baseline and differential.
GenevisibleiQ8NBQ5. HS.

Organism-specific databases

HPAiHPA021608.

Interactioni

Protein-protein interaction databases

BioGridi119349. 5 interactions.
IntActiQ8NBQ5. 1 interaction.
STRINGi9606.ENSP00000351035.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 425Combined sources
Turni43 – 453Combined sources
Helixi47 – 5812Combined sources
Beta strandi62 – 687Combined sources
Helixi70 – 8213Combined sources
Beta strandi87 – 915Combined sources
Helixi97 – 11014Combined sources
Beta strandi115 – 1195Combined sources
Helixi130 – 1323Combined sources
Helixi133 – 14412Combined sources
Helixi146 – 16116Combined sources
Beta strandi165 – 1706Combined sources
Helixi179 – 20527Combined sources
Beta strandi211 – 2188Combined sources
Helixi220 – 2234Combined sources
Helixi230 – 2334Combined sources
Helixi239 – 25113Combined sources
Beta strandi255 – 2595Combined sources
Helixi265 – 2706Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YB1X-ray1.95A/B28-275[»]
ProteinModelPortaliQ8NBQ5.
SMRiQ8NBQ5. Positions 30-273.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NBQ5.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1201. Eukaryota.
COG1028. LUCA.
HOVERGENiHBG051352.
InParanoidiQ8NBQ5.
OrthoDBiEOG7Z3F50.
PhylomeDBiQ8NBQ5.
TreeFamiTF312837.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NBQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLDILLL LPLLIVCSLE SFVKLFIPKR RKSVTGEIVL ITGAGHGIGR
60 70 80 90 100
LTAYEFAKLK SKLVLWDINK HGLEETAAKC KGLGAKVHTF VVDCSNREDI
110 120 130 140 150
YSSAKKVKAE IGDVSILVNN AGVVYTSDLF ATQDPQIEKT FEVNVLAHFW
160 170 180 190 200
TTKAFLPAMT KNNHGHIVTV ASAAGHVSVP FLLAYCSSKF AAVGFHKTLT
210 220 230 240 250
DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPTLEPE EVVNRLMHGI
260 270 280 290 300
LTEQKMIFIP SSIAFLTTLE RILPERFLAV LKQKISVKFD AVIGYKMKAQ
Length:300
Mass (Da):32,936
Last modified:May 18, 2010 - v3
Checksum:i51DE633A205EBE86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231V → E in AAH08650 (PubMed:15489334).Curated
Sequence conflicti38 – 381I → T in BAC11560 (PubMed:16303743).Curated
Sequence conflicti106 – 1061K → N in AAH08650 (PubMed:15489334).Curated
Sequence conflicti107 – 1071V → C in AAH08650 (PubMed:15489334).Curated
Sequence conflicti228 – 2281N → K in AAH08650 (PubMed:15489334).Curated
Sequence conflicti229 – 2291P → M in AAH08650 (PubMed:15489334).Curated
Sequence conflicti263 – 2631I → N in AAH08650 (PubMed:15489334).Curated
Sequence conflicti264 – 2641A → C in AAH08650 (PubMed:15489334).Curated
Sequence conflicti265 – 2651F → I in AAH08650 (PubMed:15489334).Curated
Sequence conflicti283 – 2831Q → R in AAF06939 (PubMed:10800688).Curated
Sequence conflicti283 – 2831Q → R in AAM44459 (PubMed:14996095).Curated
Sequence conflicti283 – 2831Q → R in AAQ88917 (PubMed:12975309).Curated
Sequence conflicti283 – 2831Q → R in BAC11560 (PubMed:16303743).Curated
Sequence conflicti283 – 2831Q → R in AAH08650 (PubMed:15489334).Curated
Sequence conflicti283 – 2831Q → R in AAH14327 (PubMed:15489334).Curated
Sequence conflicti283 – 2831Q → R in AAH16367 (PubMed:15489334).Curated
Sequence conflicti283 – 2831Q → R in AAH21673 (PubMed:15489334).Curated
Sequence conflicti283 – 2831Q → R in AAH36001 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126780 mRNA. Translation: AAF06939.1.
AF273056 mRNA. Translation: AAM44459.1.
AY358553 mRNA. Translation: AAQ88917.1.
AK075348 mRNA. Translation: BAC11560.1.
AC108516 Genomic DNA. No translation available.
BC008650 mRNA. Translation: AAH08650.1.
BC014327 mRNA. Translation: AAH14327.1.
BC016367 mRNA. Translation: AAH16367.1.
BC021673 mRNA. Translation: AAH21673.1.
BC036001 mRNA. Translation: AAH36001.1.
CCDSiCCDS3619.1.
RefSeqiNP_057329.3. NM_016245.4.
UniGeneiHs.594923.

Genome annotation databases

EnsembliENST00000358290; ENSP00000351035; ENSG00000198189.
GeneIDi51170.
KEGGihsa:51170.
UCSCiuc003hqp.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126780 mRNA. Translation: AAF06939.1.
AF273056 mRNA. Translation: AAM44459.1.
AY358553 mRNA. Translation: AAQ88917.1.
AK075348 mRNA. Translation: BAC11560.1.
AC108516 Genomic DNA. No translation available.
BC008650 mRNA. Translation: AAH08650.1.
BC014327 mRNA. Translation: AAH14327.1.
BC016367 mRNA. Translation: AAH16367.1.
BC021673 mRNA. Translation: AAH21673.1.
BC036001 mRNA. Translation: AAH36001.1.
CCDSiCCDS3619.1.
RefSeqiNP_057329.3. NM_016245.4.
UniGeneiHs.594923.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YB1X-ray1.95A/B28-275[»]
ProteinModelPortaliQ8NBQ5.
SMRiQ8NBQ5. Positions 30-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119349. 5 interactions.
IntActiQ8NBQ5. 1 interaction.
STRINGi9606.ENSP00000351035.

PTM databases

iPTMnetiQ8NBQ5.
PhosphoSiteiQ8NBQ5.

Polymorphism and mutation databases

BioMutaiHSD17B11.
DMDMi296439374.

Proteomic databases

EPDiQ8NBQ5.
MaxQBiQ8NBQ5.
PaxDbiQ8NBQ5.
PRIDEiQ8NBQ5.

Protocols and materials databases

DNASUi51170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358290; ENSP00000351035; ENSG00000198189.
GeneIDi51170.
KEGGihsa:51170.
UCSCiuc003hqp.3. human.

Organism-specific databases

CTDi51170.
GeneCardsiHSD17B11.
H-InvDBHIX0004358.
HGNCiHGNC:22960. HSD17B11.
HPAiHPA021608.
MIMi612831. gene.
neXtProtiNX_Q8NBQ5.
PharmGKBiPA162391655.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1201. Eukaryota.
COG1028. LUCA.
HOVERGENiHBG051352.
InParanoidiQ8NBQ5.
OrthoDBiEOG7Z3F50.
PhylomeDBiQ8NBQ5.
TreeFamiTF312837.

Enzyme and pathway databases

ReactomeiR-HSA-193144. Estrogen biosynthesis.

Miscellaneous databases

ChiTaRSiHSD17B11. human.
EvolutionaryTraceiQ8NBQ5.
GeneWikiiHSD17B11.
GenomeRNAii51170.
PROiQ8NBQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NBQ5.
CleanExiHS_HSD17B11.
ExpressionAtlasiQ8NBQ5. baseline and differential.
GenevisibleiQ8NBQ5. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Short-chain dehydrogenases/reductases in retina."
    Haeseleer F., Palczewski K.
    Methods Enzymol. 316:372-383(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Retina.
  2. "SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
    Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
    Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow, Colon, Kidney, Liver and Urinary bladder.
  7. "Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase."
    Li K.X.Z., Smith R.E., Krozowski Z.S.
    Endocr. Res. 24:663-667(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Cited for: TISSUE SPECIFICITY.
  9. "17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells."
    Chai Z., Brereton P., Suzuki T., Sasano H., Obeyesekere V., Escher G., Saffery R., Fuller P., Enriquez C., Krozowski Z.
    Endocrinology 144:2084-2091(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY IN VITRO, TISSUE SPECIFICITY.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type XI."
    Lukacik P., Bunkoczi G., Kavanagh K., Ng S., Von delft F., Bray J., Edwards A., Arrowsmith C., Sundstrom M., Oppermann U.
    Submitted (DEC-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-275.

Entry informationi

Entry nameiDHB11_HUMAN
AccessioniPrimary (citable) accession number: Q8NBQ5
Secondary accession number(s): Q96HF6, Q9UKU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 128 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.