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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-Experimental evidence at protein leveli

Functioni

Plays a major role in ketone body metabolism.

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Activated by potassium ions, but not sodium ions.1 Publication

Kineticsi

  1. KM=4 µM for acetoacetyl coenzyme A1 Publication
  2. KM=20 µM for coenzyme A1 Publication
  3. KM=8 µM for 2-methylacetoacetyl coenzyme A1 Publication
  4. KM=508 µM for acetyl coenzyme A1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei126Acyl-thioester intermediateCurated1
    Metal bindingi219Potassium1 Publication1
    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
    Active sitei385Proton acceptorCurated1
    Active sitei413Proton acceptorCurated1

    GO - Molecular functioni

    • acetyl-CoA C-acetyltransferase activity Source: BHF-UCL
    • carbon-carbon lyase activity Source: BHF-UCL
    • coenzyme binding Source: Ensembl
    • ligase activity, forming carbon-carbon bonds Source: BHF-UCL
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • acetyl-CoA biosynthetic process Source: BHF-UCL
    • acetyl-CoA catabolic process Source: BHF-UCL
    • adipose tissue development Source: Ensembl
    • brain development Source: Ensembl
    • branched-chain amino acid catabolic process Source: Reactome
    • coenzyme A biosynthetic process Source: BHF-UCL
    • coenzyme A metabolic process Source: BHF-UCL
    • fatty acid beta-oxidation Source: GO_Central
    • isoleucine catabolic process Source: BHF-UCL
    • ketone body biosynthetic process Source: Reactome
    • ketone body catabolic process Source: BHF-UCL
    • ketone body metabolic process Source: BHF-UCL
    • liver development Source: Ensembl
    • metanephric proximal convoluted tubule development Source: Ensembl
    • propionyl-CoA biosynthetic process Source: BHF-UCL
    • protein homooligomerization Source: Ensembl
    • response to hormone Source: Ensembl
    • response to organic cyclic compound Source: Ensembl
    • response to starvation Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Potassium

    Enzyme and pathway databases

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

    Chemistry databases

    SwissLipidsiSLP:000000701.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    T2
    Gene namesi
    Name:ACAT1
    Synonyms:ACAT, MAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:93. ACAT1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    3-ketothiolase deficiency (3KTD)4 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn 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.
    See also OMIM:203750
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00749785Missing in 3KTD. 1
    Natural variantiVAR_00749893N → S in 3KTD; 10% activity. 1 PublicationCorresponds to variant rs120074145dbSNPEnsembl.1
    Natural variantiVAR_007499152G → A in 3KTD. Corresponds to variant rs762991875dbSNPEnsembl.1
    Natural variantiVAR_007500158N → D in 3KTD; no activity. 1 PublicationCorresponds to variant rs148639841dbSNPEnsembl.1
    Natural variantiVAR_007501183G → R in 3KTD; no activity. 1 PublicationCorresponds to variant rs120074141dbSNPEnsembl.1
    Natural variantiVAR_007502297T → M in 3KTD; 10% normal activity. 1 Publication1
    Natural variantiVAR_007503301A → P in 3KTD; 5% normal activity. 1 Publication1
    Natural variantiVAR_007504312I → T in 3KTD; 10% activity. 1 PublicationCorresponds to variant rs120074146dbSNPEnsembl.1
    Natural variantiVAR_007505333A → P in 3KTD; no activity. 1 PublicationCorresponds to variant rs120074147dbSNPEnsembl.1
    Natural variantiVAR_007506379G → V in 3KTD. Corresponds to variant rs120074143dbSNPEnsembl.1
    Natural variantiVAR_007507380A → T in 3KTD; 7% normal activity. 1 PublicationCorresponds to variant rs120074140dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi38.
    MalaCardsiACAT1.
    MIMi203750. phenotype.
    OpenTargetsiENSG00000075239.
    Orphaneti134. Ketoacidosis due to beta-ketothiolase deficiency.
    PharmGKBiPA24431.

    Chemistry databases

    ChEMBLiCHEMBL2616.
    DrugBankiDB00795. Sulfasalazine.

    Polymorphism and mutation databases

    BioMutaiACAT1.
    DMDMi135755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 33MitochondrionBy similarityAdd BLAST33
    ChainiPRO_000003408534 – 427Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    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

    EPDiP24752.
    MaxQBiP24752.
    PaxDbiP24752.
    PeptideAtlasiP24752.
    PRIDEiP24752.
    TopDownProteomicsiP24752-1. [P24752-1]

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030363.
    UCD-2DPAGEP24752.

    PTM databases

    iPTMnetiP24752.
    PhosphoSitePlusiP24752.
    SwissPalmiP24752.

    Expressioni

    Gene expression databases

    BgeeiENSG00000075239.
    CleanExiHS_ACAT1.
    ExpressionAtlasiP24752. baseline and differential.
    GenevisibleiP24752. HS.

    Organism-specific databases

    HPAiHPA004428.
    HPA007569.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi106556. 61 interactors.
    IntActiP24752. 6 interactors.
    MINTiMINT-5000530.
    STRINGi9606.ENSP00000265838.

    Chemistry databases

    BindingDBiP24752.

    Structurei

    Secondary structure

    1427
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi42 – 49Combined sources8
    Turni58 – 61Combined sources4
    Helixi64 – 79Combined sources16
    Helixi83 – 85Combined sources3
    Beta strandi88 – 92Combined sources5
    Helixi103 – 110Combined sources8
    Beta strandi119 – 123Combined sources5
    Helixi125 – 127Combined sources3
    Helixi128 – 141Combined sources14
    Beta strandi146 – 155Combined sources10
    Helixi156 – 158Combined sources3
    Beta strandi161 – 163Combined sources3
    Beta strandi165 – 167Combined sources3
    Beta strandi173 – 177Combined sources5
    Helixi178 – 182Combined sources5
    Turni187 – 190Combined sources4
    Helixi193 – 204Combined sources12
    Helixi208 – 227Combined sources20
    Turni228 – 234Combined sources7
    Beta strandi238 – 240Combined sources3
    Beta strandi248 – 250Combined sources3
    Helixi255 – 257Combined sources3
    Turni261 – 263Combined sources3
    Helixi264 – 266Combined sources3
    Beta strandi273 – 275Combined sources3
    Turni280 – 282Combined sources3
    Beta strandi287 – 297Combined sources11
    Helixi298 – 303Combined sources6
    Beta strandi310 – 319Combined sources10
    Helixi322 – 327Combined sources6
    Helixi328 – 340Combined sources13
    Helixi344 – 346Combined sources3
    Beta strandi347 – 352Combined sources6
    Helixi357 – 367Combined sources11
    Helixi371 – 373Combined sources3
    Helixi380 – 383Combined sources4
    Turni387 – 389Combined sources3
    Helixi390 – 401Combined sources12
    Beta strandi407 – 414Combined sources8
    Turni415 – 417Combined sources3
    Beta strandi418 – 426Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP24752.
    SMRiP24752.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24752.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni258 – 260Coenzyme A binding3

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1390. Eukaryota.
    COG0183. LUCA.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP24752.
    KOiK00626.
    OMAiEPIDFPV.
    OrthoDBiEOG091G09C6.
    PhylomeDBiP24752.
    TreeFamiTF300650.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P24752-1) [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
    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
    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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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 → P.1 PublicationCorresponds to variant rs3741056dbSNPEnsembl.1
    Natural variantiVAR_00749785Missing in 3KTD. 1
    Natural variantiVAR_00749893N → S in 3KTD; 10% activity. 1 PublicationCorresponds to variant rs120074145dbSNPEnsembl.1
    Natural variantiVAR_007499152G → A in 3KTD. Corresponds to variant rs762991875dbSNPEnsembl.1
    Natural variantiVAR_007500158N → D in 3KTD; no activity. 1 PublicationCorresponds to variant rs148639841dbSNPEnsembl.1
    Natural variantiVAR_007501183G → R in 3KTD; no activity. 1 PublicationCorresponds to variant rs120074141dbSNPEnsembl.1
    Natural variantiVAR_007502297T → M in 3KTD; 10% normal activity. 1 Publication1
    Natural variantiVAR_007503301A → P in 3KTD; 5% normal activity. 1 Publication1
    Natural variantiVAR_007504312I → T in 3KTD; 10% activity. 1 PublicationCorresponds to variant rs120074146dbSNPEnsembl.1
    Natural variantiVAR_007505333A → P in 3KTD; no activity. 1 PublicationCorresponds to variant rs120074147dbSNPEnsembl.1
    Natural variantiVAR_007506379G → V in 3KTD. Corresponds to variant rs120074143dbSNPEnsembl.1
    Natural variantiVAR_007507380A → T in 3KTD; 7% normal activity. 1 PublicationCorresponds to variant rs120074140dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    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]
    UniGeneiHs.232375.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    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]
    UniGeneiHs.232375.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP24752.
    SMRiP24752.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106556. 61 interactors.
    IntActiP24752. 6 interactors.
    MINTiMINT-5000530.
    STRINGi9606.ENSP00000265838.

    Chemistry databases

    BindingDBiP24752.
    ChEMBLiCHEMBL2616.
    DrugBankiDB00795. Sulfasalazine.
    SwissLipidsiSLP:000000701.

    PTM databases

    iPTMnetiP24752.
    PhosphoSitePlusiP24752.
    SwissPalmiP24752.

    Polymorphism and mutation databases

    BioMutaiACAT1.
    DMDMi135755.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030363.
    UCD-2DPAGEP24752.

    Proteomic databases

    EPDiP24752.
    MaxQBiP24752.
    PaxDbiP24752.
    PeptideAtlasiP24752.
    PRIDEiP24752.
    TopDownProteomicsiP24752-1. [P24752-1]

    Protocols and materials databases

    DNASUi38.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi38.
    DisGeNETi38.
    GeneCardsiACAT1.
    HGNCiHGNC:93. ACAT1.
    HPAiHPA004428.
    HPA007569.
    MalaCardsiACAT1.
    MIMi203750. phenotype.
    607809. gene.
    neXtProtiNX_P24752.
    OpenTargetsiENSG00000075239.
    Orphaneti134. Ketoacidosis due to beta-ketothiolase deficiency.
    PharmGKBiPA24431.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1390. Eukaryota.
    COG0183. LUCA.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP24752.
    KOiK00626.
    OMAiEPIDFPV.
    OrthoDBiEOG091G09C6.
    PhylomeDBiP24752.
    TreeFamiTF300650.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSiACAT1. human.
    EvolutionaryTraceiP24752.
    GeneWikiiACAT1.
    GenomeRNAii38.
    PROiP24752.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000075239.
    CleanExiHS_ACAT1.
    ExpressionAtlasiP24752. baseline and differential.
    GenevisibleiP24752. HS.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTHIL_HUMAN
    AccessioniPrimary (citable) accession number: P24752
    Secondary accession number(s): B2R6H1, G3XAB4, Q96FG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: November 2, 2016
    This is version 182 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.