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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 that catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone (PubMed:9553139, PubMed:23042678, PubMed:12917011, PubMed:18996107, PubMed:25925575, PubMed:28888424). Catalyzes the third step in the beta-oxidation of fatty acids (PubMed:9553139, PubMed:12917011, PubMed:18996107, PubMed:25925575, PubMed:28888424). Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids (PubMed:12917011). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids (PubMed:12917011). 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).9 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 HSD17B10/MRPP2, 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).7 Publications

<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 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 for DL-3-hydroxybutyryl-CoA1 Publication
  11. KM=7.7 µM for for 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

    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 sitei155Substrate1 Publication1
    <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 sitei168Proton acceptor1 Publication1
    Binding sitei172NAD1 Publication1

    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 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

    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 processtRNA 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

    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

    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_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:
    3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.355 Publications)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.512 Publications)
    Short name:
    17-beta-HSD 10
    2-methyl-3-hydroxybutyryl-CoA dehydrogenase1 Publication
    Short name:
    MHBD1 Publication
    3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.1781 Publication)
    3-hydroxyacyl-CoA dehydrogenase type II
    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_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:HSD17B10
    Synonyms:ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
    <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 X

    Organism-specific databases

    Eukaryotic Pathogen 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; Source: COMPARTMENTS

    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

    <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)12 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.
    See also OMIM:300438
    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. 1 PublicationCorresponds 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. 7 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+. 2 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; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing. 1 PublicationCorresponds to variant dbSNP:rs886041974EnsemblClinVar.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 Publications1
    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
    Mental retardation, X-linked 17 (MRX17)1 Publication
    The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.
    Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
    See also OMIM:300705

    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>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
    300705 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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4159

    Drug and drug target database

    More...
    DrugBanki
    DB00157 NADH

    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_processing_section">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.<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

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    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 human proteome resource

    More...
    ProteomicsDBi
    78427
    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

    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 104 organ(s), highest expression level in right lobe of liver

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_HSD17B10

    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
    HPA001432

    <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 (PubMed:15342248, PubMed:20077426, PubMed:25925575). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31 (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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    109278, 383 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q99714

    Protein interaction database and analysis system

    More...
    IntActi
    Q99714, 182 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

    <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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q99714

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

    More...
    SMRi
    Q99714

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1199 Eukaryota
    ENOG410XNNW LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155170

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG002145

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q99714

    KEGG Orthology (KO)

    More...
    KOi
    K08683

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LMGLVNC

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0G9O

    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_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 (2+)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 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.<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 '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
    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.

    Note: No experimental confirmation available.
    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. 1 PublicationCorresponds 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. 7 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+. 2 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; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing. 1 PublicationCorresponds to variant dbSNP:rs886041974EnsemblClinVar.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 Publications1
    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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.171280

    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, Chromosomal rearrangement

    <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]
    UniGeneiHs.171280

    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[»]
    ProteinModelPortaliQ99714
    SMRiQ99714
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109278, 383 interactors
    CORUMiQ99714
    IntActiQ99714, 182 interactors
    MINTiQ99714
    STRINGi9606.ENSP00000168216

    Chemistry databases

    BindingDBiQ99714
    ChEMBLiCHEMBL4159
    DrugBankiDB00157 NADH
    SwissLipidsiSLP:000000787

    PTM databases

    iPTMnetiQ99714
    PhosphoSitePlusiQ99714
    SwissPalmiQ99714

    Polymorphism and mutation databases

    BioMutaiHSD17B10
    DMDMi2492759

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00017726
    Q99714
    UCD-2DPAGEiQ99714

    Proteomic databases

    EPDiQ99714
    MaxQBiQ99714
    PaxDbiQ99714
    PeptideAtlasiQ99714
    PRIDEiQ99714
    ProteomicsDBi78427
    78428 [Q99714-2]
    TopDownProteomicsiQ99714-1 [Q99714-1]
    Q99714-2 [Q99714-2]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    3028
    Structural Biology KnowledgebaseSearch...

    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
    HPAiHPA001432
    MalaCardsiHSD17B10
    MIMi300256 gene
    300438 phenotype
    300705 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
    ENOG410XNNW LUCA
    GeneTreeiENSGT00940000155170
    HOVERGENiHBG002145
    InParanoidiQ99714
    KOiK08683
    OMAiLMGLVNC
    OrthoDBiEOG091G0G9O
    PhylomeDBiQ99714
    TreeFamiTF354307

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01071-MONOMER
    BRENDAi1.1.1.178 2681
    1.1.1.35 2681
    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

    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

    Protein Ontology

    More...
    PROi
    PR:Q99714

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000072506 Expressed in 104 organ(s), highest expression level in right lobe of liver
    CleanExiHS_HSD17B10
    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...

    <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_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: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 201 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, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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