Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dehydrogenase/reductase SDR family member 11

Gene

DHRS11

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

Functioni

Catalyzes the conversion of the 17-keto group of estrone, 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta-hydroxyl metabolites and the conversion of the 3-keto group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites. Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May also reduce endogenous and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic ketones.1 Publication

Catalytic activityi

A 3-beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH.1 Publication
17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.1 Publication

Enzyme regulationi

Inhibited by flavonoids including apigenin, luteolin, genistein, kaempferol and quercetin and also by carbenoxolone, zearalenone, glycyrrhetinic, curcumin and flufenamic acid.1 Publication

Kineticsi

  1. KM=1.1 µM for NADPH1 Publication
  2. KM=0.7 µM for estrone (at 37 degrees Celsius)1 Publication
  3. KM=1.3 µM for 5-alpha-androstan-3-alpha-ol-17-one (at 37 degrees Celsius)1 Publication
  4. KM=2.2 µM for 5-alpha-androstan-3-beta-ol-17-one (at 37 degrees Celsius)1 Publication
  5. KM=11 µM for dehydroepiandrosterone (DHEA) (at 37 degrees Celsius)1 Publication
  6. KM=12 µM for DHEA sulfate (at 37 degrees Celsius)1 Publication
  7. KM=19 µM for 4-androsten-3-alpha-ol-17-one (at 37 degrees Celsius)1 Publication
  8. KM=0.7 µM for 5-beta-pregnan-20-beta-ol-3-one (at 37 degrees Celsius)1 Publication
  9. KM=1.1 µM for dehydrolithocholic acid (at 37 degrees Celsius)1 Publication
  10. KM=5.2 µM for 5-beta-cholanic acid-3,7-dione (at 37 degrees Celsius)1 Publication
  11. KM=5.1 µM for 20-alpha-hydroxyprogesterone (at 37 degrees Celsius)1 Publication
  12. KM=44 µM for taurodehydrocholic acid (at 37 degrees Celsius)1 Publication
  13. KM=29 µM for dehydrocholic acid (at 37 degrees Celsius)1 Publication
  14. KM=102 µM for 5-beta-dihydrotestosterone (DHT) (at 37 degrees Celsius)1 Publication
  15. KM=5.2 µM for 5-beta-androstane-3,17-dione (at 37 degrees Celsius)1 Publication
  16. KM=4.6 µM for 4-androstene-3,17-dione (at 37 degrees Celsius)1 Publication
  17. KM=12 µM for 5-alpha-androstane-3,17-dione (at 37 degrees Celsius)1 Publication
  18. KM=2.1 µM for 5-beta-pregnane-21-ol-3,20-dione (at 37 degrees Celsius)1 Publication
  19. KM=3.4 µM for progesterone (at 37 degrees Celsius)1 Publication
  20. KM=15 µM for 5-beta-pregnane-3,20-dione (at 37 degrees Celsius)1 Publication
  21. KM=16 µM for 17-beta-estradiol (at 37 degrees Celsius)1 Publication
  22. KM=30 µM for testosterone (at 37 degrees Celsius)1 Publication
  23. KM=23 µM for 4-androstene-3-alpha,17-beta-diol (at 37 degrees Celsius)1 Publication
  24. KM=11 µM for 5-androstene-3-alpha,17-beta-diol (at 37 degrees Celsius)1 Publication
  25. KM=26 µM for 5-alpha-dihydrotestosterone (DHT) (at 37 degrees Celsius)1 Publication
  26. KM=9.2 µM for 5-alpha-androstane-3-alpha,17-beta-diol (at 37 degrees Celsius)1 Publication
  27. KM=1.1 µM for 5-alpha-androstane-3-beta,17-beta-diol (at 37 degrees Celsius)1 Publication
  28. KM=36 µM for 5-beta-androstan-3-beta-ol-17-one (at 37 degrees Celsius)1 Publication
  29. KM=12 µM for 5-beta-androstane-3-beta,17-beta-diol (at 37 degrees Celsius)1 Publication
  30. KM=22 µM for 3-beta-hydroxyprogesterone (at 37 degrees Celsius)1 Publication
  31. KM=36 µM for 5-beta-pregnan-3-beta-ol-20-one (at 37 degrees Celsius)1 Publication
  32. KM=14 µM for 5-beta-pregnane-3-beta,20-beta-diol (at 37 degrees Celsius)1 Publication
  33. KM=4.7 µM for 5-beta-pregnane-3-beta,21-diol-20-one (at 37 degrees Celsius)1 Publication
  34. KM=0.4 µM for isolithocholic acid (at 37 degrees Celsius)1 Publication
  35. KM=60 µM for 1-phenyl-1,2-propanedione (at 37 degrees Celsius)1 Publication
  36. KM=620 µM for 2,3-hexanedione (at 37 degrees Celsius)1 Publication
  37. KM=201 µM for 2,3-heptanedione (at 37 degrees Celsius)1 Publication
  38. KM=420 µM for 3,4-hexanedione (at 37 degrees Celsius)1 Publication
  39. KM=178 µM for alpha-tetralone (at 37 degrees Celsius)1 Publication
  40. KM=740 µM for loxoprofen (at 37 degrees Celsius)1 Publication
  1. Vmax=43 nmol/min/mg enzyme with estrone as substrate (at 37 degrees Celsius)1 Publication
  2. Vmax=42 nmol/min/mg enzyme with 5-alpha-androstan-3-alpha-ol-17-one as substrate (at 37 degrees Celsius)1 Publication
  3. Vmax=49 nmol/min/mg enzyme with 5-alpha-androstan-3-beta-ol-17-one as substrate (at 37 degrees Celsius)1 Publication
  4. Vmax=118 nmol/min/mg enzyme with dehydroepiandrosterone (DHEA) as substrate (at 37 degrees Celsius)1 Publication
  5. Vmax=60 nmol/min/mg enzyme with DHEA sulfate as substrate (at 37 degrees Celsius)1 Publication
  6. Vmax=43 nmol/min/mg enzyme with 4-androsten-3-alpha-ol-17-one as substrate (at 37 degrees Celsius)1 Publication
  7. Vmax=44 nmol/min/mg enzyme with 5-beta-pregnan-20-beta-ol-3-one as substrate (at 37 degrees Celsius)1 Publication
  8. Vmax=44 nmol/min/mg enzyme with dehydrolithocholic acid as substrate (at 37 degrees Celsius)1 Publication
  9. Vmax=85 nmol/min/mg enzyme with 5-beta-cholanic acid-3,7-dione as substrate (at 37 degrees Celsius)1 Publication
  10. Vmax=40 nmol/min/mg enzyme with 20-alpha-hydroxyprogesterone as substrate (at 37 degrees Celsius)1 Publication
  11. Vmax=200 nmol/min/mg enzyme with taurodehydrocholic acid as substrate (at 37 degrees Celsius)1 Publication
  12. Vmax=119 nmol/min/mg enzyme with dehydrocholic acid as substrate (at 37 degrees Celsius)1 Publication
  13. Vmax=389 nmol/min/mg enzyme with 5-beta-dihydrotestosterone (DTH) as substrate (at 37 degrees Celsius)1 Publication
  14. Vmax=62 nmol/min/mg enzyme with 5-beta-androstane-3,17-dione as substrate (at 37 degrees Celsius)1 Publication
  15. Vmax=52 nmol/min/mg enzyme with 4-androstene-3,17-dione as substrate (at 37 degrees Celsius)1 Publication
  16. Vmax=57 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as substrate (at 37 degrees Celsius)1 Publication
  17. Vmax=49 nmol/min/mg enzyme with 5-beta-pregnane-21-ol-3,20-dione as substrate (at 37 degrees Celsius)1 Publication
  18. Vmax=36 nmol/min/mg enzyme with progesterone as substrate (at 37 degrees Celsius)1 Publication
  19. Vmax=123 nmol/min/mg enzyme with 5-beta-pregnane-3,20-dione as substrate (at 37 degrees Celsius)1 Publication
  20. Vmax=246 nmol/min/mg enzyme with 17-beta-estradiol as substrate (at 37 degrees Celsius)1 Publication
  21. Vmax=238 nmol/min/mg enzyme with testosterone as substrate (at 37 degrees Celsius)1 Publication
  22. Vmax=33 nmol/min/mg enzyme with 4-androstene-3-alpha,17-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  23. Vmax=366 nmol/min/mg enzyme with 5-androstene-3-alpha,17-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  24. Vmax=117 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone (DHT) as substrate (at 37 degrees Celsius)1 Publication
  25. Vmax=40 nmol/min/mg enzyme with 5-alpha-androstane-3-alpha,17-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  26. Vmax=96 nmol/min/mg enzyme with 5-alpha-androstane-3-beta,17-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  27. Vmax=137 nmol/min/mg enzyme with 5-beta-androstan-3-beta-ol-17-one as substrate (at 37 degrees Celsius)1 Publication
  28. Vmax=511 nmol/min/mg enzyme with 5-beta-androstane-3-beta,17-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  29. Vmax=364 nmol/min/mg enzyme with 3-beta-hydroxyprogesterone as substrate (at 37 degrees Celsius)1 Publication
  30. Vmax=268 nmol/min/mg enzyme with 5-beta-pregnan-3-beta-ol-20-one as substrate (at 37 degrees Celsius)1 Publication
  31. Vmax=220 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,20-beta-diol as substrate (at 37 degrees Celsius)1 Publication
  32. Vmax=96 nmol/min/mg enzyme with 5-beta-pregnane-3-beta,21-diol-20-one as substrate (at 37 degrees Celsius)1 Publication
  33. Vmax=28 nmol/min/mg enzyme with isolithocholic acid as substrate (at 37 degrees Celsius)1 Publication
  34. Vmax=69 nmol/min/mg enzyme with 1-phenyl-1,2-propanedione as substrate (at 37 degrees Celsius)1 Publication
  35. Vmax=331 nmol/min/mg enzyme with 2,3-hexanedione as substrate (at 37 degrees Celsius)1 Publication
  36. Vmax=86 nmol/min/mg enzyme with 2,3-heptanedione as substrate (at 37 degrees Celsius)1 Publication
  37. Vmax=166 nmol/min/mg enzyme with 3,4-hexanedione as substrate (at 37 degrees Celsius)1 Publication
  38. Vmax=67 nmol/min/mg enzyme with alpha-tetralone as substrate (at 37 degrees Celsius)1 Publication
  39. Vmax=51 nmol/min/mg enzyme with loxoprofen as substrate (at 37 degrees Celsius)1 Publication

Pathwayi: estrogen biosynthesis

This protein is involved in the pathway estrogen biosynthesis, which is part of Steroid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway estrogen biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49NADPCombined sources1
Binding sitei97NADP; via carbonyl oxygenCombined sources1
Binding sitei151SubstrateCombined sources1
Active sitei166Proton acceptorPROSITE-ProRule annotation1
Binding sitei166NADPCombined sources1
Binding sitei166SubstrateCombined sources1
Binding sitei170NADPCombined sources1
Binding sitei208NADPCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 23NADPCombined sources6
Nucleotide bindingi43 – 44NADPCombined sources2
Nucleotide bindingi70 – 71NADPCombined sources2
Nucleotide bindingi201 – 204NADPCombined sources4

GO - Molecular functioni

  • 17-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: UniProtKB
  • 17-beta-ketosteroid reductase activity Source: UniProtKB
  • 3-keto sterol reductase activity Source: UniProtKB
  • estradiol 17-beta-dehydrogenase activity Source: UniProtKB
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • estrogen biosynthetic process Source: UniProtKB-UniPathway
  • steroid biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processLipid metabolism, Steroid metabolism
LigandNADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00769.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrogenase/reductase SDR family member 11
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase1 Publication
3-beta-hydroxysteroid 3-dehydrogenase1 Publication (EC:1.1.1.2701 Publication)
Estradiol 17-beta-dehydrogenase1 Publication (EC:1.1.1.621 Publication)
Short-chain dehydrogenase/reductase family 24C member 11 Publication
Gene namesi
Name:DHRS11
Synonyms:SDR24C11 Publication
ORF Names:UNQ836/PRO1774
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000278535.4.
HGNCiHGNC:28639. DHRS11.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000278535.
PharmGKBiPA164718841.

Chemistry databases

DrugBankiDB03461. 2'-Monophosphoadenosine 5'-Diphosphoribose.

Polymorphism and mutation databases

BioMutaiDHRS11.
DMDMi74749397.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000004549031 – 260Dehydrogenase/reductase SDR family member 11Add BLAST230

Proteomic databases

EPDiQ6UWP2.
MaxQBiQ6UWP2.
PaxDbiQ6UWP2.
PeptideAtlasiQ6UWP2.
PRIDEiQ6UWP2.

PTM databases

iPTMnetiQ6UWP2.
PhosphoSitePlusiQ6UWP2.

Expressioni

Tissue specificityi

Isoform 1: Ubiquitously expressed, with highest levels in testis, small intestine, colon, kidney, brain and heart. Isoform 3: Expressed in brain, heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000278535.
ExpressionAtlasiQ6UWP2. baseline and differential.
GenevisibleiQ6UWP2. HS.

Organism-specific databases

HPAiHPA041226.
HPA048236.
HPA053623.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi122572. 5 interactors.
IntActiQ6UWP2. 1 interactor.
STRINGi9606.ENSP00000251312.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Beta strandi13 – 18Combined sources6
Helixi22 – 33Combined sources12
Beta strandi37 – 43Combined sources7
Helixi45 – 57Combined sources13
Beta strandi61 – 68Combined sources8
Helixi74 – 88Combined sources15
Beta strandi92 – 96Combined sources5
Turni106 – 108Combined sources3
Helixi111 – 121Combined sources11
Helixi123 – 138Combined sources16
Beta strandi145 – 149Combined sources5
Helixi152 – 154Combined sources3
Helixi161 – 163Combined sources3
Helixi164 – 186Combined sources23
Beta strandi192 – 199Combined sources8
Helixi205 – 209Combined sources5
Turni210 – 212Combined sources3
Helixi214 – 221Combined sources8
Helixi229 – 241Combined sources13
Beta strandi246 – 255Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XG5X-ray1.53A/B/C/D1-256[»]
ProteinModelPortaliQ6UWP2.
SMRiQ6UWP2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6UWP2.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IUBV. Eukaryota.
COG4221. LUCA.
GeneTreeiENSGT00840000129887.
HOVERGENiHBG105262.
InParanoidiQ6UWP2.
OMAiNAGITTH.
OrthoDBiEOG091G0J8P.
PhylomeDBiQ6UWP2.
TreeFamiTF324174.

Family and domain databases

InterProiView protein in InterPro
IPR036291. NAD(P)-bd_dom_sf.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
PfamiView protein in Pfam
PF00106. adh_short. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00061. ADH_SHORT. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6UWP2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARPGMERWR DRLALVTGAS GGIGAAVARA LVQQGLKVVG CARTVGNIEE
60 70 80 90 100
LAAECKSAGY PGTLIPYRCD LSNEEDILSM FSAIRSQHSG VDICINNAGL
110 120 130 140 150
ARPDTLLSGS TSGWKDMFNV NVLALSICTR EAYQSMKERN VDDGHIININ
160 170 180 190 200
SMSGHRVLPL SVTHFYSATK YAVTALTEGL RQELREAQTH IRATCISPGV
210 220 230 240 250
VETQFAFKLH DKDPEKAAAT YEQMKCLKPE DVAEAVIYVL STPAHIQIGD
260
IQMRPTEQVT
Length:260
Mass (Da):28,308
Last modified:July 5, 2004 - v1
Checksum:i88DFF656874F19F4
GO
Isoform 2 (identifier: Q6UWP2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Show »
Length:181
Mass (Da):20,022
Checksum:i5BFCBE5727835A38
GO
Isoform 3 (identifier: Q6UWP2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     196-226: Missing.

Show »
Length:229
Mass (Da):24,843
Checksum:i66E1E75A130F4103
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti81F → S in BAB15390 (PubMed:14702039).Curated1
Sequence conflicti81F → S in CAG33637 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0169871 – 79Missing in isoform 2. 2 PublicationsAdd BLAST79
Alternative sequenceiVSP_059104196 – 226Missing in isoform 3. CuratedAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LC110386 mRNA. Translation: BAU36404.1.
AY358712 mRNA. Translation: AAQ89074.1.
AK026196 mRNA. Translation: BAB15390.1.
AK315735 mRNA. Translation: BAG38090.1.
CR457356 mRNA. Translation: CAG33637.1.
CH471199 Genomic DNA. Translation: EAW57568.1.
BC002731 mRNA. Translation: AAH02731.2.
CCDSiCCDS11315.2. [Q6UWP2-1]
RefSeqiNP_077284.2. NM_024308.3. [Q6UWP2-1]
XP_005257715.1. XM_005257658.2.
UniGeneiHs.462859.

Genome annotation databases

EnsembliENST00000611337; ENSP00000477603; ENSG00000278535. [Q6UWP2-2]
ENST00000618403; ENSP00000482704; ENSG00000278535. [Q6UWP2-1]
ENST00000621143; ENSP00000483747; ENSG00000275397. [Q6UWP2-1]
ENST00000631686; ENSP00000488610; ENSG00000275397. [Q6UWP2-2]
GeneIDi79154.
KEGGihsa:79154.
UCSCiuc002hnd.4. human. [Q6UWP2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDHR11_HUMAN
AccessioniPrimary (citable) accession number: Q6UWP2
Secondary accession number(s): A0A0U5BLD0
, B2RDZ3, Q9BUC7, Q9H674
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: October 25, 2017
This is version 128 of the entry and version 1 of the sequence. See 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 17
    Human chromosome 17: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families