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UniProtKB - Q99714 (HCD2_HUMAN)

Entry version 216 (02 Dec 2020)
Sequence version 3 (23 Jan 2007)
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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

HSD17B10

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

Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:20077426, PubMed:18996107, PubMed:19706438, PubMed:25925575, PubMed:26950678, PubMed:28888424). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PubMed:9553139, PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PubMed:20077426, PubMed:18996107, PubMed:19706438). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PubMed:10600649, PubMed:12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PubMed:19706438, PubMed:28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PubMed:26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426).10 Publications
In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:24549042, PubMed:25925575, PubMed:26950678, PubMed:28888424). Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N1-methylguanine and N1-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit (PubMed:23042678, PubMed:25925575, PubMed:28888424). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">Function</a> 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

The phospholipase C-like activity toward cardiolipin is inhibited by amyloid-beta peptide.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

Kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). Kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).1 Publication
  1. KM=25.7 µM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)1 Publication
  2. KM=85.2 µM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  3. KM=41 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  4. KM=5 µM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  5. KM=219 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  6. KM=36.4 µM for chenodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  7. KM=1.7 µM for dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  8. KM=30.6 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)1 Publication
  9. KM=42.3 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)1 Publication
  10. KM=69 µM for DL-3-hydroxybutyryl-CoA1 Publication
  11. KM=7.7 µM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone1 Publication
  12. KM=30 µM for 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone1 Publication
  13. KM=140 µM for tetramyristoyl cardiolipin1 Publication
  14. KM=148 µM for tetralinoleoyl cardiolipin1 Publication
  15. KM=40 µM for oxidized tetralinoleoyl cardiolipin1 Publication
  16. KM=7.1 µM for (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA1 Publication
  1. Vmax=14.8 µmol/min/mg enzyme toward (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA1 Publication
  2. Vmax=150 µmol/min/mg enzyme 3alpha-hydroxy-5alpha-pregnan-20-one/allopregnanolone1 Publication

pH dependencei

Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees Celsius, and 7.0 for the reductase reaction at 25 degrees Celsius.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-isoleucine degradation

This protein is involved in the pathway L-isoleucine degradation, which is part of Amino-acid degradation.1 Publication
View all proteins of this organism that are known to be involved in the pathway L-isoleucine degradation and in Amino-acid degradation.

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Pathwayi: Steroid metabolism

This protein is involved in Steroid metabolism.2 Publications
View all proteins of this organism that are known to be involved in Steroid metabolism.

Pathwayi: bile acid biosynthesis

This protein is involved in the pathway bile 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 bile acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei155Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei168Proton acceptor1 Publication1
Binding sitei172NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi12 – 41NAD1 PublicationAdd BLAST30

<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 metabolism, Lipid metabolism, Steroid metabolism, tRNA processing
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS01071-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.178, 2681
1.1.1.35, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q99714

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-6785470, tRNA processing in the mitochondrion
R-HSA-6787450, tRNA modification in the mitochondrion
R-HSA-70895, Branched-chain amino acid catabolism
R-HSA-8868766, rRNA processing in the mitochondrion

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q99714

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

More...UniPathwayi		UPA00221
UPA00364
UPA00659

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000787

<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%5Fand%5Ftaxonomy%5Fsection">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:
3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.355 Publications)
Alternative name(s):
17-beta-estradiol 17-dehydrogenase (EC:1.1.1.622 Publications)
2-methyl-3-hydroxybutyryl-CoA dehydrogenase1 Publication
Short name:
MHBD1 Publication
3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)) (EC:1.1.1.2391 Publication)
3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.1783 Publications)
3-hydroxyacyl-CoA dehydrogenase type II
3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC:1.1.1.531 Publication)
7-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.1591 Publication)
Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
Mitochondrial ribonuclease P protein 2
Short name:
Mitochondrial RNase P protein 2
Short chain dehydrogenase/reductase family 5C member 1
Short-chain type dehydrogenase/reductase XH98G2
Type II HADH
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HSD17B10
Synonyms:ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 X

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000072506.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:4800, HSD17B10

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		300256, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q99714

<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

Mitochondrion, Mitochondrion nucleoid

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

HDS10 mitochondrial disease (HSD10MD)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked multisystemic disorder with highly variable severity. Age at onset ranges from the neonatal period to early childhood. Features include progressive neurodegeneration, psychomotor retardation, loss of mental and motor skills, seizures, cardiomyopathy, and visual and hearing impairment. Some patients manifest lactic acidosis and metabolic acidosis.
Related information in OMIM
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_08004912V → L in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing. 1 Publication1
Natural variantiVAR_07886365V → A in HSD10MD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs104886492EnsemblClinVar.1
Natural variantiVAR_07886486D → G in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD+ binding; complete loss of phospholipase C-like activity toward cardiolipin. 2 PublicationsCorresponds to variant dbSNP:rs587777651EnsemblClinVar.1
Natural variantiVAR_015987122L → V in HSD10MD. 1 PublicationCorresponds to variant dbSNP:rs28935476EnsemblClinVar.1
Natural variantiVAR_015988130R → C in HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization; complete loss of phospholipase C-like activity toward cardiolipin. 8 PublicationsCorresponds to variant dbSNP:rs28935475EnsemblClinVar.1
Natural variantiVAR_078865165Q → H in HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD+; complete loss of phospholipase C-like activity toward cardiolipin. 3 Publications1
Natural variantiVAR_080050176V → M in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing. 1 Publication1
Natural variantiVAR_080051210P → S in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization. 2 Publications1
Natural variantiVAR_078866212K → E in HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase activity; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing. 1 PublicationCorresponds to variant dbSNP:rs886041974Ensembl.1
Natural variantiVAR_080052226R → Q in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 2 PublicationsCorresponds to variant dbSNP:rs1556894502Ensembl.1
Natural variantiVAR_032093247N → S in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 3 PublicationsCorresponds to variant dbSNP:rs122461163Ensembl.1
Natural variantiVAR_078867249E → Q in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity. 1 PublicationCorresponds to variant dbSNP:rs62626305Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi20S → F: Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. 2 Publications1
Mutagenesisi172K → A: Abolishes dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. Does not affect homotetramerization. 2 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation, Neurodegeneration

Organism-specific databases

DisGeNET

More...DisGeNETi		3028

MalaCards human disease database

More...MalaCardsi		HSD17B10
MIMi300438, phenotype

Open Targets

More...OpenTargetsi		ENSG00000072506

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		85295, HSD10 disease, atypical type
391428, HSD10 disease, infantile type
391457, HSD10 disease, neonatal type

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA162391638

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q99714, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4159

Drug and drug target database

More...DrugBanki		DB02820, 1-Azepan-1-Yl-2-Phenyl-2-(4-Thioxo-1,4-Dihydro-Pyrazolo[3,4-D]Pyrimidin-5-Yl)Ethanone Adduct
DB00157, NADH
DB09568, Omega-3-carboxylic acids

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HSD17B10

Domain mapping of disease mutations (DMDM)

More...DMDMi		2492759

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000548102 – 2613-hydroxyacyl-CoA dehydrogenase type-2Add BLAST260

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 residuei2N-acetylalanineCombined sources1
Modified residuei53N6-acetyllysine; alternateBy similarity1
Modified residuei53N6-succinyllysine; alternateBy similarity1
Modified residuei69N6-acetyllysineBy similarity1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei212N6-acetyllysine; alternateBy similarity1
Modified residuei212N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-522
CPTAC-523

Encyclopedia of Proteome Dynamics

More...EPDi		Q99714

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q99714

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q99714

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q99714

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

More...PaxDbi		Q99714

PeptideAtlas

More...PeptideAtlasi		Q99714

PRoteomics IDEntifications database

More...PRIDEi		Q99714

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		78427 [Q99714-1]
78428 [Q99714-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q99714-1 [Q99714-1]
Q99714-2 [Q99714-2]

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00017726
Q99714

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		Q99714

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q99714

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q99714

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

More...PhosphoSitePlusi		Q99714

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q99714

<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

Ubiquitously expressed in normal tissues but is overexpressed in neurons affected in AD.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000072506, Expressed in right lobe of liver and 127 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q99714, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q99714, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000072506, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (PubMed:15342248, PubMed:20077426, PubMed:25925575).

Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3 (PubMed:18984158, PubMed:25925575, PubMed:26950678, PubMed:28888424).

Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex (PubMed:23042678, PubMed:29040705).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109278, 420 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q99714

Protein interaction database and analysis system

More...IntActi		Q99714, 199 interactors

Molecular INTeraction database

More...MINTi		Q99714

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000168216

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q99714

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q99714, 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		Q99714

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		Q99714

<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		KOG1199, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155170

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_010194_42_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q99714

Identification of Orthologs from Complete Genome Data

More...OMAi		ANIRCVK

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q99714

TreeFam database of animal gene trees

More...TreeFami		TF354307

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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00106, adh_short, 1 hit

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%5Flength">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 2 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q99714-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ 
        60         70         80         90        100
AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT 
       110        120        130        140        150
YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI 
       160        170        180        190        200
INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL 
       210        220        230        240        250
FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV 
       260 
IRLDGAIRMQ P
Length:261
Mass (Da):26,923
Last modified:January 23, 2007 - v3
<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:i9E74F242E3E6FEF1
GO
Isoform 2 (identifier: Q99714-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-199: Missing.

Show »
Length:252
Mass (Da):25,984
Checksum:iF36BB71070CE872D
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5H928Q5H928_HUMAN
3-hydroxyacyl-CoA dehydrogenase typ...
HSD17B10 RP3-339A18.2-004
169Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08004912V → L in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing. 1 Publication1
Natural variantiVAR_07886365V → A in HSD10MD; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs104886492EnsemblClinVar.1
Natural variantiVAR_07886486D → G in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD+ binding; complete loss of phospholipase C-like activity toward cardiolipin. 2 PublicationsCorresponds to variant dbSNP:rs587777651EnsemblClinVar.1
Natural variantiVAR_015987122L → V in HSD10MD. 1 PublicationCorresponds to variant dbSNP:rs28935476EnsemblClinVar.1
Natural variantiVAR_015988130R → C in HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization; complete loss of phospholipase C-like activity toward cardiolipin. 8 PublicationsCorresponds to variant dbSNP:rs28935475EnsemblClinVar.1
Natural variantiVAR_078865165Q → H in HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD+; complete loss of phospholipase C-like activity toward cardiolipin. 3 Publications1
Natural variantiVAR_080050176V → M in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing. 1 Publication1
Natural variantiVAR_080051210P → S in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization. 2 Publications1
Natural variantiVAR_078866212K → E in HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase activity; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing. 1 PublicationCorresponds to variant dbSNP:rs886041974Ensembl.1
Natural variantiVAR_080052226R → Q in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 2 PublicationsCorresponds to variant dbSNP:rs1556894502Ensembl.1
Natural variantiVAR_032093247N → S in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization. 3 PublicationsCorresponds to variant dbSNP:rs122461163Ensembl.1
Natural variantiVAR_078867249E → Q in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity. 1 PublicationCorresponds to variant dbSNP:rs62626305Ensembl.1

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_007830191 – 199Missing in isoform 2. 1 Publication9

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
U96132 mRNA Translation: AAC51812.1
U73514 mRNA Translation: AAB68958.1
AF069134 mRNA Translation: AAC39900.1
AF035555 mRNA Translation: AAC15902.1
AF037438 Genomic DNA Translation: AAC16419.1
CR456723 mRNA Translation: CAG33004.1
Z97054 Genomic DNA Translation: CAI42652.1
Z97054 Genomic DNA Translation: CAI42653.1
CH471154 Genomic DNA Translation: EAW93157.1
CH471154 Genomic DNA Translation: EAW93158.1
BC000372 mRNA Translation: AAH00372.1
BC008708 mRNA Translation: AAH08708.1
AY092415 mRNA Translation: AAM18189.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS14354.1 [Q99714-1]
CCDS35300.1 [Q99714-2]

NCBI Reference Sequences

More...RefSeqi		NP_001032900.1, NM_001037811.2 [Q99714-2]
NP_004484.1, NM_004493.2 [Q99714-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000168216; ENSP00000168216; ENSG00000072506 [Q99714-1]
ENST00000375304; ENSP00000364453; ENSG00000072506 [Q99714-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3028

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3028

UCSC genome browser

More...UCSCi		uc004dsl.2, human [Q99714-1]

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
U96132 mRNA Translation: AAC51812.1
U73514 mRNA Translation: AAB68958.1
AF069134 mRNA Translation: AAC39900.1
AF035555 mRNA Translation: AAC15902.1
AF037438 Genomic DNA Translation: AAC16419.1
CR456723 mRNA Translation: CAG33004.1
Z97054 Genomic DNA Translation: CAI42652.1
Z97054 Genomic DNA Translation: CAI42653.1
CH471154 Genomic DNA Translation: EAW93157.1
CH471154 Genomic DNA Translation: EAW93158.1
BC000372 mRNA Translation: AAH00372.1
BC008708 mRNA Translation: AAH08708.1
AY092415 mRNA Translation: AAM18189.1
CCDSiCCDS14354.1 [Q99714-1]
CCDS35300.1 [Q99714-2]
RefSeqiNP_001032900.1, NM_001037811.2 [Q99714-2]
NP_004484.1, NM_004493.2 [Q99714-1]

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
1F67model-A1-261[»]
1SO8X-ray2.30A1-261[»]
1U7TX-ray2.00A/B/C/D1-261[»]
2O23X-ray1.20A/B1-261[»]
SMRiQ99714
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109278, 420 interactors
CORUMiQ99714
IntActiQ99714, 199 interactors
MINTiQ99714
STRINGi9606.ENSP00000168216

Chemistry databases

BindingDBiQ99714
ChEMBLiCHEMBL4159
DrugBankiDB02820, 1-Azepan-1-Yl-2-Phenyl-2-(4-Thioxo-1,4-Dihydro-Pyrazolo[3,4-D]Pyrimidin-5-Yl)Ethanone Adduct
DB00157, NADH
DB09568, Omega-3-carboxylic acids
SwissLipidsiSLP:000000787

PTM databases

iPTMnetiQ99714
MetOSiteiQ99714
PhosphoSitePlusiQ99714
SwissPalmiQ99714

Polymorphism and mutation databases

BioMutaiHSD17B10
DMDMi2492759

2D gel databases

REPRODUCTION-2DPAGEiIPI00017726
Q99714
UCD-2DPAGEiQ99714

Proteomic databases

CPTACiCPTAC-522
CPTAC-523
EPDiQ99714
jPOSTiQ99714
MassIVEiQ99714
MaxQBiQ99714
PaxDbiQ99714
PeptideAtlasiQ99714
PRIDEiQ99714
ProteomicsDBi78427 [Q99714-1]
78428 [Q99714-2]
TopDownProteomicsiQ99714-1 [Q99714-1]
Q99714-2 [Q99714-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		357, 527 antibodies

The DNASU plasmid repository

More...DNASUi		3028

Genome annotation databases

EnsembliENST00000168216; ENSP00000168216; ENSG00000072506 [Q99714-1]
ENST00000375304; ENSP00000364453; ENSG00000072506 [Q99714-2]
GeneIDi3028
KEGGihsa:3028
UCSCiuc004dsl.2, human [Q99714-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3028
DisGeNETi3028
EuPathDBiHostDB:ENSG00000072506.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		HSD17B10
HGNCiHGNC:4800, HSD17B10
HPAiENSG00000072506, Low tissue specificity
MalaCardsiHSD17B10
MIMi300256, gene
300438, phenotype
neXtProtiNX_Q99714
OpenTargetsiENSG00000072506
Orphaneti85295, HSD10 disease, atypical type
391428, HSD10 disease, infantile type
391457, HSD10 disease, neonatal type
PharmGKBiPA162391638

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1199, Eukaryota
GeneTreeiENSGT00940000155170
HOGENOMiCLU_010194_42_0_1
InParanoidiQ99714
OMAiANIRCVK
PhylomeDBiQ99714
TreeFamiTF354307

Enzyme and pathway databases

UniPathwayiUPA00221
UPA00364
UPA00659
BioCyciMetaCyc:HS01071-MONOMER
BRENDAi1.1.1.178, 2681
1.1.1.35, 2681
PathwayCommonsiQ99714
ReactomeiR-HSA-6785470, tRNA processing in the mitochondrion
R-HSA-6787450, tRNA modification in the mitochondrion
R-HSA-70895, Branched-chain amino acid catabolism
R-HSA-8868766, rRNA processing in the mitochondrion
SABIO-RKiQ99714

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3028, 101 hits in 482 CRISPR screens

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

More...ChiTaRSi		HSD17B10, human
EvolutionaryTraceiQ99714

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HSD17B10

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

More...GenomeRNAii		3028
PharosiQ99714, Tbio

Protein Ontology

More...PROi		PR:Q99714
RNActiQ99714, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000072506, Expressed in right lobe of liver and 127 other tissues
ExpressionAtlasiQ99714, baseline and differential
GenevisibleiQ99714, 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...

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 nameiHCD2_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: Q99714
Secondary accession number(s): Q5H927
, Q6IBS9, Q8TCV9, Q96HD5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: December 2, 2020
This is version 216 of the entry and version 3 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 polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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
  6. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations