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Entry version 137 (08 May 2019)
Sequence version 1 (05 Jul 2004)
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Protein

Dehydrogenase/reductase SDR family member 11

Gene

DHRS11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei49NADPCombined sources1
Binding sitei97NADP; via carbonyl oxygenCombined sources1
Binding sitei151SubstrateCombined sources1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei166Proton acceptorPROSITE-ProRule annotation1
Binding sitei166NADPCombined sources1
Binding sitei166SubstrateCombined sources1
Binding sitei170NADPCombined sources1
Binding sitei208NADPCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 23NADPCombined sources6
Nucleotide bindingi43 – 44NADPCombined sources2
Nucleotide bindingi70 – 71NADPCombined sources2
Nucleotide bindingi201 – 204NADPCombined sources4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00769

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DHRS11
Synonyms:SDR24C11 Publication
ORF Names:UNQ836/PRO1774
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:28639 DHRS11

Online Mendelian Inheritance in Man (OMIM)

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MIMi
616159 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q6UWP2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...
DisGeNETi
79154

Open Targets

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OpenTargetsi
ENSG00000278535

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA164718841

Chemistry databases

Drug and drug target database

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DrugBanki
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DHRS11

Domain mapping of disease mutations (DMDM)

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DMDMi
74749397

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 30Sequence analysisAdd BLAST30
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004549031 – 260Dehydrogenase/reductase SDR family member 11Add BLAST230

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q6UWP2

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q6UWP2

MaxQB - The MaxQuant DataBase

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MaxQBi
Q6UWP2

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q6UWP2

PeptideAtlas

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PeptideAtlasi
Q6UWP2

PRoteomics IDEntifications database

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PRIDEi
Q6UWP2

ProteomicsDB human proteome resource

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ProteomicsDBi
67507
67508 [Q6UWP2-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q6UWP2

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q6UWP2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000278535 Expressed in 192 organ(s), highest expression level in jejunal mucosa

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q6UWP2 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q6UWP2 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA041226
HPA048236
HPA053623

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
122572, 5 interactors

Protein interaction database and analysis system

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IntActi
Q6UWP2, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000482704

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XG5X-ray1.53A/B/C/D1-256[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q6UWP2

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q6UWP2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IUBV Eukaryota
COG4221 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00840000129887

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6UWP2

KEGG Orthology (KO)

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KOi
K22970

Identification of Orthologs from Complete Genome Data

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OMAi
PNHVAYV

Database of Orthologous Groups

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OrthoDBi
1190834at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q6UWP2

TreeFam database of animal gene trees

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TreeFami
TF324174

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

Pfam protein domain database

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Pfami
View protein in Pfam
PF00106 adh_short, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00081 GDHRDH
PR00080 SDRFAMILY

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00061 ADH_SHORT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WZN3A0A087WZN3_HUMAN
Dehydrogenase/reductase SDR family ...
DHRS11
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X0R1A0A087X0R1_HUMAN
Dehydrogenase/reductase SDR family ...
DHRS11
109Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WYV4A0A087WYV4_HUMAN
Dehydrogenase/reductase SDR family ...
DHRS11
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti81F → S in BAB15390 (PubMed:14702039).Curated1
Sequence conflicti81F → S in CAG33637 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11315.2 [Q6UWP2-1]

NCBI Reference Sequences

More...
RefSeqi
NP_077284.2, NM_024308.3 [Q6UWP2-1]
XP_005257715.1, XM_005257658.2 [Q6UWP2-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000611337; ENSP00000477603; ENSG00000278535 [Q6UWP2-2]
ENST00000618403; ENSP00000482704; ENSG00000278535 [Q6UWP2-1]
ENST00000621143; ENSP00000483747; ENSG00000275397 [Q6UWP2-1]
ENST00000631686; ENSP00000488610; ENSG00000275397 [Q6UWP2-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
79154

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:79154

UCSC genome browser

More...
UCSCi
uc002hnd.4 human [Q6UWP2-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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 [Q6UWP2-3]

3D structure databases

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

Protein-protein interaction databases

BioGridi122572, 5 interactors
IntActiQ6UWP2, 1 interactor
STRINGi9606.ENSP00000482704

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose

PTM databases

iPTMnetiQ6UWP2
PhosphoSitePlusiQ6UWP2

Polymorphism and mutation databases

BioMutaiDHRS11
DMDMi74749397

Proteomic databases

EPDiQ6UWP2
jPOSTiQ6UWP2
MaxQBiQ6UWP2
PaxDbiQ6UWP2
PeptideAtlasiQ6UWP2
PRIDEiQ6UWP2
ProteomicsDBi67507
67508 [Q6UWP2-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
79154
DisGeNETi79154

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DHRS11
HGNCiHGNC:28639 DHRS11
HPAiHPA041226
HPA048236
HPA053623
MIMi616159 gene
neXtProtiNX_Q6UWP2
OpenTargetsiENSG00000278535
PharmGKBiPA164718841

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IUBV Eukaryota
COG4221 LUCA
GeneTreeiENSGT00840000129887
InParanoidiQ6UWP2
KOiK22970
OMAiPNHVAYV
OrthoDBi1190834at2759
PhylomeDBiQ6UWP2
TreeFamiTF324174

Enzyme and pathway databases

UniPathwayi
UPA00769

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DHRS11 human
EvolutionaryTraceiQ6UWP2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
79154

Protein Ontology

More...
PROi
PR:Q6UWP2

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000278535 Expressed in 192 organ(s), highest expression level in jejunal mucosa
ExpressionAtlasiQ6UWP2 baseline and differential
GenevisibleiQ6UWP2 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHR11_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6UWP2
Secondary accession number(s): A0A0U5BLD0
, B2RDZ3, Q9BUC7, Q9H674
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: May 8, 2019
This is version 137 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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