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UniProtKB - P24752 (THIL_HUMAN)

Entry version 209 (16 Oct 2019)
Sequence version 1 (01 Mar 1992)
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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

ACAT1

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

This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (PubMed:1715688, PubMed:7728148, PubMed:9744475). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (PubMed:1715688, PubMed:7728148, PubMed:9744475). The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA (PubMed:17371050). Thereby, it plays a major role in ketone body metabolism (PubMed:17371050, PubMed:1715688, PubMed:7728148, PubMed:9744475).4 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 <a href="http://www.uniprot.org/help/function_section">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

Activated by potassium ions, but not sodium ions.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 21 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 8 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl) (PubMed:17371050). kcat is 61 sec(-1) for the degradation of 2-methylacetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 14 sec(-1) for the degradation of 2-methylacetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl) (PubMed:17371050). kcat is 3.5 sec(-1) for the synthesis of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050).1 Publication
  1. KM=4 µM for acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
  2. KM=8 µM for acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
  3. KM=20 µM for CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
  4. KM=66 µM for CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
  5. KM=8 µM for 2-methyl-3-oxobutanoyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
  6. KM=8 µM for 2-methyl-3-oxobutanoyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
  7. KM=508 µM for acetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei126Acyl-thioester intermediate1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi219Potassium1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei219Coenzyme A1 Publication1
    Binding sitei263Coenzyme A1 Publication1
    Metal bindingi280Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi281Potassium; via carbonyl oxygen1 Publication1
    Metal bindingi283Potassium; via carbonyl oxygen1 Publication1
    Binding sitei284Coenzyme A1 Publication1
    Metal bindingi381Potassium; via carbonyl oxygen1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei385Increases nucleophilicity of active site Cys1 Publication1
    Active sitei413Proton donor/acceptor1 Publication1

    <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 functionAcyltransferase, Transferase
    Biological processFatty acid metabolism, Lipid metabolism
    LigandMetal-binding, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS01167-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-70895 Branched-chain amino acid catabolism
    R-HSA-77108 Utilization of Ketone Bodies
    R-HSA-77111 Synthesis of Ketone Bodies

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P24752

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

    More...    UniPathwayi    		UPA00659

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000000701

    <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:
    Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9PROSITE-ProRule annotation4 Publications)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    T2
    <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:ACAT1
    Synonyms:ACAT, MAT
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:93 ACAT1

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		607809 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P24752

    <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

    <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

    3-ketothiolase deficiency (3KTD)4 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype.
    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_00749785Missing in 3KTD. 1
    Natural variantiVAR_00749893N → S in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074145EnsemblClinVar.1
    Natural variantiVAR_007499152G → A in 3KTD. Corresponds to variant dbSNP:rs762991875EnsemblClinVar.1
    Natural variantiVAR_007500158N → D in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs148639841EnsemblClinVar.1
    Natural variantiVAR_007501183G → R in 3KTD; no activity. 1 PublicationCorresponds to variant dbSNP:rs120074141EnsemblClinVar.1
    Natural variantiVAR_007502297T → M in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs886041122EnsemblClinVar.1
    Natural variantiVAR_007503301A → P in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs1420321267Ensembl.1
    Natural variantiVAR_007504312I → T in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074146EnsemblClinVar.1
    Natural variantiVAR_007505333A → P in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074147EnsemblClinVar.1
    Natural variantiVAR_007506379G → V in 3KTD. Corresponds to variant dbSNP:rs120074143EnsemblClinVar.1
    Natural variantiVAR_007507380A → T in 3KTD; decreased protein stability. 1 PublicationCorresponds to variant dbSNP:rs120074140EnsemblClinVar.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		38

    MalaCards human disease database

    More...    MalaCardsi    		ACAT1
    MIMi203750 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000075239

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

    More...    Orphaneti    		134 Beta-ketothiolase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA24431

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		P24752

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL2616

    Drug and drug target database

    More...    DrugBanki    		DB09061 Cannabidiol
    DB14009 Medical Cannabis
    DB14011 Nabiximols
    DB00795 Sulfasalazine
    DB09328 Vayarin

    DrugCentral

    More...    DrugCentrali    		P24752

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		2435

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		ACAT1

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		135755

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 33MitochondrionBy similarityAdd BLAST33
    <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_000003408534 – 427Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

    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 residuei66N6-acetyllysine; alternateBy similarity1
    Modified residuei66N6-succinyllysine; alternateBy similarity1
    Modified residuei78N6-succinyllysineBy similarity1
    Modified residuei174N6-acetyllysine; alternateCombined sources1
    Modified residuei174N6-succinyllysine; alternateBy similarity1
    Modified residuei181N6-acetyllysine; alternateCombined sources1
    Modified residuei181N6-succinyllysine; alternateBy similarity1
    Modified residuei190N6-acetyllysine; alternateBy similarity1
    Modified residuei190N6-succinyllysine; alternateBy similarity1
    Modified residuei202N6-acetyllysine; alternateBy similarity1
    Modified residuei202N6-succinyllysine; alternateBy similarity1
    Modified residuei223N6-acetyllysine; alternateBy similarity1
    Modified residuei223N6-succinyllysine; alternateBy similarity1
    Modified residuei230N6-acetyllysine; alternateBy similarity1
    Modified residuei230N6-succinyllysine; alternateBy similarity1
    Modified residuei243N6-succinyllysineBy similarity1
    Modified residuei251N6-acetyllysineCombined sources1
    Modified residuei257N6-acetyllysineBy similarity1
    Modified residuei263N6-acetyllysine; alternateCombined sources1
    Modified residuei263N6-succinyllysine; alternateBy similarity1
    Modified residuei266N6-succinyllysineBy similarity1
    Modified residuei268N6-succinyllysineBy similarity1
    Modified residuei273N6-acetyllysineBy similarity1
    Modified residuei338N6-acetyllysineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Succinylation at Lys-268, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P24752

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P24752

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		P24752

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P24752

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

    More...    PaxDbi    		P24752

    PeptideAtlas

    More...    PeptideAtlasi    		P24752

    PRoteomics IDEntifications database

    More...    PRIDEi    		P24752

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		33702
    54224 [P24752-1]

    Consortium for Top Down Proteomics

    More...    TopDownProteomicsi    		P24752-1 [P24752-1]

    2D gel databases

    REPRODUCTION-2DPAGE

    More...    REPRODUCTION-2DPAGEi    		IPI00030363

    University College Dublin 2-DE Proteome Database

    More...    UCD-2DPAGEi    		P24752

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P24752

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

    More...    PhosphoSitePlusi    		P24752

    SwissPalm database of S-palmitoylation events

    More...    SwissPalmi    		P24752

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000075239 Expressed in 233 organ(s), highest expression level in nephron tubule

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P24752 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P24752 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA004428
    HPA007569

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

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

    Homotetramer.

    1 Publication

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		106556, 87 interactors

    Protein interaction database and analysis system

    More...    IntActi    		P24752, 19 interactors

    Molecular INTeraction database

    More...    MINTi    		P24752

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000265838

    <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

    1427
    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    		P24752

    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    		P24752

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni258 – 260Coenzyme A binding1 Publication3

    <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 thiolase-like superfamily. Thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG1390 Eukaryota
    COG0183 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00950000182771

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000012238

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P24752

    KEGG Orthology (KO)

    More...    KOi    		K00626

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		LMAGQGQ

    Database of Orthologous Groups

    More...    OrthoDBi    		1011220at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P24752

    TreeFam database of animal gene trees

    More...    TreeFami    		TF300650

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00751 thiolase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.47.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000429 Ac-CoA_Ac_transf, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53901 SSF53901, 2 hits

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01930 AcCoA-C-Actrans, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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 3 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P24752-1) [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
    MAVLAALLRS GARSRSPLLR RLVQEIRYVE RSYVSKPTLK EVVIVSATRT 
            60         70         80         90        100
    PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG 
           110        120        130        140        150
    QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA 
           160        170        180        190        200
    GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK IHMGSCAENT 
           210        220        230        240        250
    AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV 
           260        270        280        290        300
    KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA 
           310        320        330        340        350
    AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW 
           360        370        380        390        400
    EVNEAFSLVV LANIKMLEID PQKVNINGGA VSLGHPIGMS GARIVGHLTH 
           410        420 
    ALKQGEYGLA SICNGGGGAS AMLIQKL
    Length:427
    Mass (Da):45,200
    Last modified:March 1, 1992 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2E81168EB39D0142
    GO
    Isoform 2 (identifier: P24752-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-162: DVMVAGGMESMSNVPYV → IKQETGSLAKICCHVRR
         163-427: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:162
    Mass (Da):17,175
    Checksum:iC76EA13AED1868FC
    GO

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

    There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    H0YEL7H0YEL7_HUMAN
    Acetyl-CoA acetyltransferase, mitoc...
    ACAT1
    		136Annotation 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>
    E9PKF3E9PKF3_HUMAN
    Acetyl-CoA acetyltransferase, mitoc...
    ACAT1
    		54Annotation 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>
    E9PRQ6E9PRQ6_HUMAN
    Acetyl-CoA acetyltransferase, mitoc...
    ACAT1
    		141Annotation score:

    Annotation score:1 out of 5

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti340V → M in BAA01387 (PubMed:1684944).Curated1
    Sequence conflicti346D → N in BAA01387 (PubMed:1684944).Curated1
    Sequence conflicti380A → S in BAA01387 (PubMed:1684944).Curated1
    Sequence conflicti412I → F in BAA01387 (PubMed:1684944).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0074965A → P1 PublicationCorresponds to variant dbSNP:rs3741056EnsemblClinVar.1
    Natural variantiVAR_00749785Missing in 3KTD. 1
    Natural variantiVAR_00749893N → S in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074145EnsemblClinVar.1
    Natural variantiVAR_007499152G → A in 3KTD. Corresponds to variant dbSNP:rs762991875EnsemblClinVar.1
    Natural variantiVAR_007500158N → D in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs148639841EnsemblClinVar.1
    Natural variantiVAR_007501183G → R in 3KTD; no activity. 1 PublicationCorresponds to variant dbSNP:rs120074141EnsemblClinVar.1
    Natural variantiVAR_007502297T → M in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs886041122EnsemblClinVar.1
    Natural variantiVAR_007503301A → P in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs1420321267Ensembl.1
    Natural variantiVAR_007504312I → T in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074146EnsemblClinVar.1
    Natural variantiVAR_007505333A → P in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074147EnsemblClinVar.1
    Natural variantiVAR_007506379G → V in 3KTD. Corresponds to variant dbSNP:rs120074143EnsemblClinVar.1
    Natural variantiVAR_007507380A → T in 3KTD; decreased protein stability. 1 PublicationCorresponds to variant dbSNP:rs120074140EnsemblClinVar.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_056844146 – 162DVMVA…NVPYV → IKQETGSLAKICCHVRR in isoform 2. 1 PublicationAdd BLAST17
    Alternative sequenceiVSP_056845163 – 427Missing in isoform 2. 1 PublicationAdd BLAST265

    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
    		D90228 mRNA Translation: BAA14278.1
    D10511 Genomic DNA Translation: BAA01387.1
    AK312574 mRNA Translation: BAG35468.1
    AP002433 Genomic DNA No translation available.
    CH471065 Genomic DNA Translation: EAW67104.1
    CH471065 Genomic DNA Translation: EAW67105.1
    BC010942 mRNA Translation: AAH10942.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS8339.1 [P24752-1]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		JH0255

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000010.1, NM_000019.3 [P24752-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000265838; ENSP00000265838; ENSG00000075239 [P24752-1]
    ENST00000299355; ENSP00000299355; ENSG00000075239 [P24752-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		38

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:38

    UCSC genome browser

    More...    UCSCi    		uc001pjw.2 human [P24752-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <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
    		D90228 mRNA Translation: BAA14278.1
    D10511 Genomic DNA Translation: BAA01387.1
    AK312574 mRNA Translation: BAG35468.1
    AP002433 Genomic DNA No translation available.
    CH471065 Genomic DNA Translation: EAW67104.1
    CH471065 Genomic DNA Translation: EAW67105.1
    BC010942 mRNA Translation: AAH10942.1
    CCDSiCCDS8339.1 [P24752-1]
    PIRiJH0255
    RefSeqiNP_000010.1, NM_000019.3 [P24752-1]

    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
    2F2SX-ray2.00A/B/C/D41-427[»]
    2IB7X-ray2.05A/B/C/D34-427[»]
    2IB8X-ray1.85A/B/C/D34-427[»]
    2IB9X-ray2.05A/B/C/D34-427[»]
    2IBUX-ray1.90A/B/C/D34-427[»]
    2IBWX-ray1.90A/B/C/D34-427[»]
    2IBYX-ray1.85A/B/C/D34-427[»]
    SMRiP24752
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi106556, 87 interactors
    IntActiP24752, 19 interactors
    MINTiP24752
    STRINGi9606.ENSP00000265838

    Chemistry databases

    ChEMBLiCHEMBL2616
    DrugBankiDB09061 Cannabidiol
    DB14009 Medical Cannabis
    DB14011 Nabiximols
    DB00795 Sulfasalazine
    DB09328 Vayarin
    DrugCentraliP24752
    GuidetoPHARMACOLOGYi2435
    SwissLipidsiSLP:000000701

    PTM databases

    iPTMnetiP24752
    PhosphoSitePlusiP24752
    SwissPalmiP24752

    Polymorphism and mutation databases

    BioMutaiACAT1
    DMDMi135755

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00030363
    UCD-2DPAGEiP24752

    Proteomic databases

    EPDiP24752
    jPOSTiP24752
    MassIVEiP24752
    MaxQBiP24752
    PaxDbiP24752
    PeptideAtlasiP24752
    PRIDEiP24752
    ProteomicsDBi33702
    54224 [P24752-1]
    TopDownProteomicsiP24752-1 [P24752-1]

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		38

    Genome annotation databases

    EnsembliENST00000265838; ENSP00000265838; ENSG00000075239 [P24752-1]
    ENST00000299355; ENSP00000299355; ENSG00000075239 [P24752-2]
    GeneIDi38
    KEGGihsa:38
    UCSCiuc001pjw.2 human [P24752-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		38
    DisGeNETi38

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		ACAT1
    HGNCiHGNC:93 ACAT1
    HPAiHPA004428
    HPA007569
    MalaCardsiACAT1
    MIMi203750 phenotype
    607809 gene
    neXtProtiNX_P24752
    OpenTargetsiENSG00000075239
    Orphaneti134 Beta-ketothiolase deficiency
    PharmGKBiPA24431

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG1390 Eukaryota
    COG0183 LUCA
    GeneTreeiENSGT00950000182771
    HOGENOMiHOG000012238
    InParanoidiP24752
    KOiK00626
    OMAiLMAGQGQ
    OrthoDBi1011220at2759
    PhylomeDBiP24752
    TreeFamiTF300650

    Enzyme and pathway databases

    UniPathwayiUPA00659
    BioCyciMetaCyc:HS01167-MONOMER
    ReactomeiR-HSA-70895 Branched-chain amino acid catabolism
    R-HSA-77108 Utilization of Ketone Bodies
    R-HSA-77111 Synthesis of Ketone Bodies
    SABIO-RKiP24752

    Miscellaneous databases

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

    More...    ChiTaRSi    		ACAT1 human
    EvolutionaryTraceiP24752

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		ACAT1

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

    More...    GenomeRNAii    		38
    PharosiP24752

    Protein Ontology

    More...    PROi    		PR:P24752

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000075239 Expressed in 233 organ(s), highest expression level in nephron tubule
    ExpressionAtlasiP24752 baseline and differential
    GenevisibleiP24752 HS

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 2 hits
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 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 nameiTHIL_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: P24752
    Secondary accession number(s): B2R6H1, G3XAB4, Q96FG8
    <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: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 16, 2019
    This is version 209 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. Human chromosome 11
      Human chromosome 11: 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
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