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UniProtKB - Q92506 (DHB8_HUMAN)

Entry version 201 (29 Sep 2021)
Sequence version 2 (24 Jan 2001)
Previous versions | rss
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Protein

(3R)-3-hydroxyacyl-CoA dehydrogenase

Gene

HSD17B8

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

Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex that acts as a scaffold protein required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference; this enzymatic activity is not needed for the KAR function (PubMed:19571038, PubMed:25203508, PubMed:30508570).

Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD+ (PubMed:19571038).

Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (Probable) (PubMed:30508570).

NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol (17beta-estradiol or E2). Has very low activity towards testosterone and dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one). Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active 17beta-estradiol (PubMed:17978863).

1 Publication1 Publication3 Publications

Miscellaneous

The fatty acyl-CoA dehydrogenase activity is several thousand times higher than the estradiol and testosterone 17beta-hydroxysteroid dehydrogenase conversion.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 <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.

Pathwayi: fatty acid biosynthesis

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

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei156SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei169Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi15 – 23NADCombined sources2 Publications9
Nucleotide bindingi42 – 43NADCombined sources2 Publications2
Nucleotide bindingi74 – 76NADCombined sources2 Publications3
Nucleotide bindingi169 – 173NADCombined sources2 Publications5
Nucleotide bindingi202 – 204NADCombined sources1 Publication3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS03575-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.100, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q92506

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-75105, Fatty acyl-CoA biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q92506

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

More...UniPathwayi		UPA00094
UPA00660
UPA00769

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001271

<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:
(3R)-3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.n122 Publications)
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 82 Publications
Short name:
17-beta-HSD 8
Short name:
HSD17B81 Publication
3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit1 Publication
Short name:
KAR alpha subunit1 Publication
3-oxoacyl-[acyl-carrier-protein] reductase
Estradiol 17-beta-dehydrogenase 8 (EC:1.1.1.621 Publication)
Protein Ke6
Short name:
Ke62 Publications
Short chain dehydrogenase/reductase family 30C member 1
Testosterone 17-beta-dehydrogenase 8 (EC:1.1.1.2391 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:HSD17B8
Synonyms:FABGL, HKE6, RING2, SDR30C1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 6

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3554, HSD17B8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601417, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q92506

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000204228

<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

Keywords - Cellular componenti

Mitochondrion

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi42D → A: Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant. 1 Publication1
Mutagenesisi148R → E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant. 1 Publication1
Mutagenesisi169Y → A: Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant. 1 Publication1
Mutagenesisi173K → A: Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant. 1 Publication1
Mutagenesisi189R → E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7923

Open Targets

More...OpenTargetsi		ENSG00000204228

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29484

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q92506, Tbio

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00157, NADH
DB03461, Nicotinamide adenine dinucleotide phosphate

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HSD17B8

Domain mapping of disease mutations (DMDM)

More...DMDMi		12643402

<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 describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000545981 – 261(3R)-3-hydroxyacyl-CoA dehydrogenaseAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei60PhosphoserineBy similarity1
Modified residuei160N6-succinyllysineBy similarity1
Modified residuei173N6-succinyllysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q92506

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q92506

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q92506

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q92506

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

More...PaxDbi		Q92506

PeptideAtlas

More...PeptideAtlasi		Q92506

PRoteomics IDEntifications database

More...PRIDEi		Q92506

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		75276

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q92506

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q92506, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q92506

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

More...PhosphoSitePlusi		Q92506

<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

Widely expressed, particularly abundant in prostate, placenta and kidney (PubMed:17978863). Expressed at protein level in various tissues like brain, cerebellum, heart, lung, kidney, ovary, testis, adrenals and prostate (PubMed:30508570).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by estradiol.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000204228, Expressed in right lobe of liver and 227 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q92506, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q92506, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000204228, Tissue enhanced (pancreas)

<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

Heterotetramer with CBR4; contains two molecules of HSD17B8 and CBR4.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		113653, 24 interactors

Protein interaction database and analysis system

More...IntActi		Q92506, 16 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000363794

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q92506, protein

<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

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q92506

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q92506

<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

Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1200, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160668

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_010194_1_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q92506

Identification of Orthologs from Complete Genome Data

More...OMAi		QLLMRMS

Database of Orthologous Groups

More...OrthoDBi		1226147at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q92506

TreeFam database of animal gene trees

More...TreeFami		TF313099

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00081, GDHRDH
PR00080, SDRFAMILY

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735, SSF51735, 1 hit

PROSITE; a protein domain and family database

More...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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q92506-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASQLQNRLR SALALVTGAG SGIGRAVSVR LAGEGATVAA CDLDRAAAQE 
        60         70         80         90        100
TVRLLGGPGS KEGPPRGNHA AFQADVSEAR AARCLLEQVQ ACFSRPPSVV 
       110        120        130        140        150
VSCAGITQDE FLLHMSEDDW DKVIAVNLKG TFLVTQAAAQ ALVSNGCRGS 
       160        170        180        190        200
IINISSIVGK VGNVGQTNYA ASKAGVIGLT QTAARELGRH GIRCNSVLPG 
       210        220        230        240        250
FIATPMTQKV PQKVVDKITE MIPMGHLGDP EDVADVVAFL ASEDSGYITG 
       260 
TSVEVTGGLF M
Length:261
Mass (Da):26,974
Last modified:January 24, 2001 - v2
<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:i8B8B2D7131714D71
GO

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 conflicti117E → R in BAA11529 (PubMed:8812499).Curated1
Sequence conflicti193R → P in BAA11529 (PubMed:8812499).Curated1
Sequence conflicti208Q → K in BAA11529 (PubMed:8812499).Curated1
Sequence conflicti212Q → K in BAA11529 (PubMed:8812499).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_035844158V → L in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_052316190H → R. Corresponds to variant dbSNP:rs34491699Ensembl.1

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
BT007239 mRNA Translation: AAP35903.1
AL031228 Genomic DNA Translation: CAC38444.1
AL662824 Genomic DNA No translation available.
AL713971 Genomic DNA No translation available.
AL645940 Genomic DNA No translation available.
AL844527 Genomic DNA No translation available.
CR759786 Genomic DNA No translation available.
CR759733 Genomic DNA No translation available.
CR847841 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03682.1
BC008185 mRNA Translation: AAH08185.1
D82061 mRNA Translation: BAA11529.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4769.1

NCBI Reference Sequences

More...RefSeqi		NP_055049.1, NM_014234.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000230236; ENSP00000230236; ENSG00000112474
ENST00000374662; ENSP00000363794; ENSG00000204228
ENST00000414463; ENSP00000387753; ENSG00000228357
ENST00000422433; ENSP00000406488; ENSG00000232357
ENST00000427295; ENSP00000403538; ENSG00000228712
ENST00000454191; ENSP00000413950; ENSG00000225312

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7923

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7923

UCSC genome browser

More...UCSCi		uc003odi.3, human

<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
BT007239 mRNA Translation: AAP35903.1
AL031228 Genomic DNA Translation: CAC38444.1
AL662824 Genomic DNA No translation available.
AL713971 Genomic DNA No translation available.
AL645940 Genomic DNA No translation available.
AL844527 Genomic DNA No translation available.
CR759786 Genomic DNA No translation available.
CR759733 Genomic DNA No translation available.
CR847841 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03682.1
BC008185 mRNA Translation: AAH08185.1
D82061 mRNA Translation: BAA11529.1
CCDSiCCDS4769.1
RefSeqiNP_055049.1, NM_014234.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PD6X-ray2.00A/B/C/D6-261[»]
4CQLX-ray2.85A/D/E/H/I/L/M/P1-261[»]
4CQMX-ray2.34A/D/E/H/I/L/M/P1-261[»]
SMRiQ92506
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113653, 24 interactors
IntActiQ92506, 16 interactors
STRINGi9606.ENSP00000363794

Chemistry databases

DrugBankiDB00157, NADH
DB03461, Nicotinamide adenine dinucleotide phosphate
SwissLipidsiSLP:000001271

PTM databases

GlyGeniQ92506, 1 site, 1 O-linked glycan (1 site)
iPTMnetiQ92506
PhosphoSitePlusiQ92506

Genetic variation databases

BioMutaiHSD17B8
DMDMi12643402

Proteomic databases

EPDiQ92506
jPOSTiQ92506
MassIVEiQ92506
MaxQBiQ92506
PaxDbiQ92506
PeptideAtlasiQ92506
PRIDEiQ92506
ProteomicsDBi75276
TopDownProteomicsiQ92506

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		28972, 222 antibodies

The DNASU plasmid repository

More...DNASUi		7923

Genome annotation databases

EnsembliENST00000230236; ENSP00000230236; ENSG00000112474
ENST00000374662; ENSP00000363794; ENSG00000204228
ENST00000414463; ENSP00000387753; ENSG00000228357
ENST00000422433; ENSP00000406488; ENSG00000232357
ENST00000427295; ENSP00000403538; ENSG00000228712
ENST00000454191; ENSP00000413950; ENSG00000225312
GeneIDi7923
KEGGihsa:7923
UCSCiuc003odi.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7923
DisGeNETi7923

GeneCards: human genes, protein and diseases

More...GeneCardsi		HSD17B8
HGNCiHGNC:3554, HSD17B8
HPAiENSG00000204228, Tissue enhanced (pancreas)
MIMi601417, gene
neXtProtiNX_Q92506
OpenTargetsiENSG00000204228
PharmGKBiPA29484
VEuPathDBiHostDB:ENSG00000204228

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1200, Eukaryota
GeneTreeiENSGT00940000160668
HOGENOMiCLU_010194_1_3_1
InParanoidiQ92506
OMAiQLLMRMS
OrthoDBi1226147at2759
PhylomeDBiQ92506
TreeFamiTF313099

Enzyme and pathway databases

UniPathwayiUPA00094
UPA00660
UPA00769
BioCyciMetaCyc:HS03575-MONOMER
BRENDAi1.1.1.100, 2681
PathwayCommonsiQ92506
ReactomeiR-HSA-75105, Fatty acyl-CoA biosynthesis
SABIO-RKiQ92506

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		7923, 6 hits in 1018 CRISPR screens

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

More...ChiTaRSi		HSD17B8, human
EvolutionaryTraceiQ92506

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HSD17B8

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

More...GenomeRNAii		7923
PharosiQ92506, Tbio

Protein Ontology

More...PROi		PR:Q92506
RNActiQ92506, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000204228, Expressed in right lobe of liver and 227 other tissues
ExpressionAtlasiQ92506, baseline and differential
GenevisibleiQ92506, HS

Family and domain databases

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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiDHB8_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: Q92506
Secondary accession number(s): A6NLX7, Q5STP7, Q9UIQ1
<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: May 30, 2000
Last sequence update: January 24, 2001
Last modified: September 29, 2021
This is version 201 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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