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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei126 – 1261Acyl-thioester intermediateCurated
    Metal bindingi219 – 2191Potassium1 Publication
    Binding sitei219 – 2191Coenzyme A1 Publication
    Binding sitei263 – 2631Coenzyme A1 Publication
    Metal bindingi280 – 2801Potassium; via carbonyl oxygen1 Publication
    Metal bindingi281 – 2811Potassium; via carbonyl oxygen1 Publication
    Metal bindingi283 – 2831Potassium; via carbonyl oxygen1 Publication
    Binding sitei284 – 2841Coenzyme A1 Publication
    Metal bindingi381 – 3811Potassium; via carbonyl oxygen1 Publication
    Active sitei385 – 3851Proton acceptorCurated
    Active sitei413 – 4131Proton acceptorCurated

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Potassium

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01167-MONOMER.
    ReactomeiREACT_1464. Synthesis of Ketone Bodies.
    REACT_197. Branched-chain amino acid catabolism.
    REACT_59. Utilization of Ketone Bodies.

    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
    ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851Missing in 3KTD.
    VAR_007497
    Natural varianti93 – 931N → S in 3KTD; 10% activity. 1 Publication
    VAR_007498
    Natural varianti152 – 1521G → A in 3KTD.
    VAR_007499
    Natural varianti158 – 1581N → D in 3KTD; no activity. 1 Publication
    VAR_007500
    Natural varianti183 – 1831G → R in 3KTD; no activity. 1 Publication
    VAR_007501
    Natural varianti297 – 2971T → M in 3KTD; 10% normal activity. 1 Publication
    VAR_007502
    Natural varianti301 – 3011A → P in 3KTD; 5% normal activity. 1 Publication
    VAR_007503
    Natural varianti312 – 3121I → T in 3KTD; 10% activity. 1 Publication
    VAR_007504
    Natural varianti333 – 3331A → P in 3KTD; no activity. 1 Publication
    VAR_007505
    Natural varianti379 – 3791G → V in 3KTD.
    VAR_007506
    Natural varianti380 – 3801A → T in 3KTD; 7% normal activity. 1 Publication
    VAR_007507

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    Chemistry

    DrugBankiDB00795. Sulfasalazine.

    Polymorphism and mutation databases

    BioMutaiACAT1.
    DMDMi135755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionBy similarityAdd
    BLAST
    Chaini34 – 427394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000034085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
    Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
    Modified residuei78 – 781N6-succinyllysineBy similarity
    Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
    Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity
    Modified residuei181 – 1811N6-acetyllysine; alternate1 Publication
    Modified residuei181 – 1811N6-succinyllysine; alternateBy similarity
    Modified residuei190 – 1901N6-acetyllysine; alternateBy similarity
    Modified residuei190 – 1901N6-succinyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-acetyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
    Modified residuei223 – 2231N6-acetyllysine; alternateBy similarity
    Modified residuei223 – 2231N6-succinyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-acetyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-succinyllysine; alternateBy similarity
    Modified residuei243 – 2431N6-succinyllysineBy similarity
    Modified residuei251 – 2511N6-acetyllysine1 Publication
    Modified residuei257 – 2571N6-acetyllysineBy similarity
    Modified residuei263 – 2631N6-acetyllysine; alternate1 Publication
    Modified residuei263 – 2631N6-succinyllysine; alternateBy similarity
    Modified residuei266 – 2661N6-succinyllysineBy similarity
    Modified residuei268 – 2681N6-succinyllysineBy similarity
    Modified residuei273 – 2731N6-acetyllysineBy similarity
    Modified residuei338 – 3381N6-acetyllysineBy similarity

    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

    MaxQBiP24752.
    PaxDbiP24752.
    PeptideAtlasiP24752.
    PRIDEiP24752.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030363.
    UCD-2DPAGEP24752.

    PTM databases

    PhosphoSiteiP24752.

    Expressioni

    Gene expression databases

    BgeeiP24752.
    CleanExiHS_ACAT1.
    ExpressionAtlasiP24752. baseline and differential.
    GenevisibleiP24752. HS.

    Organism-specific databases

    HPAiHPA004428.
    HPA007569.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi106556. 40 interactions.
    IntActiP24752. 3 interactions.
    MINTiMINT-5000530.
    STRINGi9606.ENSP00000265838.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 498Combined sources
    Turni58 – 614Combined sources
    Helixi64 – 7916Combined sources
    Helixi83 – 853Combined sources
    Beta strandi88 – 925Combined sources
    Helixi103 – 1108Combined sources
    Beta strandi119 – 1235Combined sources
    Helixi125 – 1273Combined sources
    Helixi128 – 14114Combined sources
    Beta strandi146 – 15510Combined sources
    Helixi156 – 1583Combined sources
    Beta strandi161 – 1633Combined sources
    Beta strandi165 – 1673Combined sources
    Beta strandi173 – 1775Combined sources
    Helixi178 – 1825Combined sources
    Turni187 – 1904Combined sources
    Helixi193 – 20412Combined sources
    Helixi208 – 22720Combined sources
    Turni228 – 2347Combined sources
    Beta strandi238 – 2403Combined sources
    Beta strandi248 – 2503Combined sources
    Helixi255 – 2573Combined sources
    Turni261 – 2633Combined sources
    Helixi264 – 2663Combined sources
    Beta strandi273 – 2753Combined sources
    Turni280 – 2823Combined sources
    Beta strandi287 – 29711Combined sources
    Helixi298 – 3036Combined sources
    Beta strandi310 – 31910Combined sources
    Helixi322 – 3276Combined sources
    Helixi328 – 34013Combined sources
    Helixi344 – 3463Combined sources
    Beta strandi347 – 3526Combined sources
    Helixi357 – 36711Combined sources
    Helixi371 – 3733Combined sources
    Helixi380 – 3834Combined sources
    Turni387 – 3893Combined sources
    Helixi390 – 40112Combined sources
    Beta strandi407 – 4148Combined sources
    Turni415 – 4173Combined sources
    Beta strandi418 – 4269Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 35-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24752.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni258 – 2603Coenzyme A binding

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP24752.
    KOiK00626.
    OMAiMFTTAPV.
    OrthoDBiEOG7JQBNG.
    PhylomeDBiP24752.
    TreeFamiTF300650.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti340 – 3401V → M in BAA01387 (PubMed:1684944).Curated
    Sequence conflicti346 – 3461D → N in BAA01387 (PubMed:1684944).Curated
    Sequence conflicti380 – 3801A → S in BAA01387 (PubMed:1684944).Curated
    Sequence conflicti412 – 4121I → F in BAA01387 (PubMed:1684944).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51A → P.1 Publication
    Corresponds to variant rs3741056 [ dbSNP | Ensembl ].
    VAR_007496
    Natural varianti85 – 851Missing in 3KTD.
    VAR_007497
    Natural varianti93 – 931N → S in 3KTD; 10% activity. 1 Publication
    VAR_007498
    Natural varianti152 – 1521G → A in 3KTD.
    VAR_007499
    Natural varianti158 – 1581N → D in 3KTD; no activity. 1 Publication
    VAR_007500
    Natural varianti183 – 1831G → R in 3KTD; no activity. 1 Publication
    VAR_007501
    Natural varianti297 – 2971T → M in 3KTD; 10% normal activity. 1 Publication
    VAR_007502
    Natural varianti301 – 3011A → P in 3KTD; 5% normal activity. 1 Publication
    VAR_007503
    Natural varianti312 – 3121I → T in 3KTD; 10% activity. 1 Publication
    VAR_007504
    Natural varianti333 – 3331A → P in 3KTD; no activity. 1 Publication
    VAR_007505
    Natural varianti379 – 3791G → V in 3KTD.
    VAR_007506
    Natural varianti380 – 3801A → T in 3KTD; 7% normal activity. 1 Publication
    VAR_007507

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei146 – 16217DVMVA…NVPYV → IKQETGSLAKICCHVRR in isoform 2. 1 PublicationVSP_056844Add
    BLAST
    Alternative sequencei163 – 427265Missing in isoform 2. 1 PublicationVSP_056845Add
    BLAST

    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.1. human.
    uc001pjy.3. 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
    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. Positions 35-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106556. 40 interactions.
    IntActiP24752. 3 interactions.
    MINTiMINT-5000530.
    STRINGi9606.ENSP00000265838.

    Chemistry

    BindingDBiP24752.
    ChEMBLiCHEMBL2616.
    DrugBankiDB00795. Sulfasalazine.

    PTM databases

    PhosphoSiteiP24752.

    Polymorphism and mutation databases

    BioMutaiACAT1.
    DMDMi135755.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030363.
    UCD-2DPAGEP24752.

    Proteomic databases

    MaxQBiP24752.
    PaxDbiP24752.
    PeptideAtlasiP24752.
    PRIDEiP24752.

    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.1. human.
    uc001pjy.3. human. [P24752-1]

    Organism-specific databases

    CTDi38.
    GeneCardsiGC11P107992.
    HGNCiHGNC:93. ACAT1.
    HPAiHPA004428.
    HPA007569.
    MIMi203750. phenotype.
    607809. gene.
    neXtProtiNX_P24752.
    Orphaneti134. Ketoacidosis due to beta-ketothiolase deficiency.
    PharmGKBiPA24431.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP24752.
    KOiK00626.
    OMAiMFTTAPV.
    OrthoDBiEOG7JQBNG.
    PhylomeDBiP24752.
    TreeFamiTF300650.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01167-MONOMER.
    ReactomeiREACT_1464. Synthesis of Ketone Bodies.
    REACT_197. Branched-chain amino acid catabolism.
    REACT_59. Utilization of Ketone Bodies.

    Miscellaneous databases

    ChiTaRSiACAT1. human.
    EvolutionaryTraceiP24752.
    GeneWikiiACAT1.
    GenomeRNAii38.
    NextBioi149.
    PROiP24752.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP24752.
    CleanExiHS_ACAT1.
    ExpressionAtlasiP24752. baseline and differential.
    GenevisibleiP24752. HS.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning and sequence of the complementary DNA encoding human mitochondrial acetoacetyl-coenzyme A thiolase and study of the variant enzymes in cultured fibroblasts from patients with 3-ketothiolase deficiency."
      Fukao T., Yamaguchi S., Kano M., Orii T., Fujiki Y., Osumi T., Hashimoto T.
      J. Clin. Invest. 86:2086-2092(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure and expression of the human mitochondrial acetoacetyl-CoA thiolase-encoding gene."
      Kano M., Fukao T., Yamaguchi S., Orii T., Osumi T., Hashimoto T.
      Gene 109:285-290(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-5.
      Tissue: Brain.
    7. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 50-78 AND 312-338.
      Tissue: Adipocyte.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 50-78 AND 231-243, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-181; LYS-251 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function."
      Haapalainen A.M., Merilaeinen G., Pirilae P.L., Kondo N., Fukao T., Wierenga R.K.
      Biochemistry 46:4305-4321(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 35-427 IN COMPLEX WITH COENZYME A AND POTASSIUM, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ENZYME REGULATION.
    14. "Molecular basis of beta-ketothiolase deficiency: mutations and polymorphisms in the human mitochondrial acetoacetyl-coenzyme A thiolase gene."
      Fukao T., Yamaguchi S., Orii T., Hashimoto T.
      Hum. Mutat. 5:113-120(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON 3KTD VARIANTS.
    15. "Identification of three mutant alleles of the gene for mitochondrial acetoacetyl-coenzyme A thiolase. A complete analysis of two generations of a family with 3-ketothiolase deficiency."
      Fukao T., Yamaguchi S., Orii T., Schutgens R.B.H., Osumi T., Hashimoto T.
      J. Clin. Invest. 89:474-479(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT 3KTD ARG-183.
    16. "Evidence for a structural mutation (347Ala to Thr) in a German family with 3-ketothiolase deficiency."
      Fukao T., Yamaguchi S., Tomatsu S., Orii T., Frauendienst-Egger G., Schrod L., Osumi T., Hashimoto T.
      Biochem. Biophys. Res. Commun. 179:124-129(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT 3KTD THR-380.
    17. "Molecular, biochemical, and clinical characterization of mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two further patients."
      Wakazono A., Fukao T., Yamaguchi S., Hori T., Orii T., Lambert M., Mitchell G.A., Lee G.W., Hashimoto T.
      Hum. Mutat. 5:34-42(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS 3KTD ASP-158; MET-297 AND PRO-301.
    18. "Characterization of N93S, I312T, and A333P missense mutations in two Japanese families with mitochondrial acetoacetyl-CoA thiolase deficiency."
      Fukao T., Nakamura H., Song X.-Q., Nakamura K., Orii K.E., Kohno Y., Kano M., Yamaguchi S., Hashimoto T., Orii T., Kondo N.
      Hum. Mutat. 12:245-254(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS 3KTD SER-93; THR-312 AND PRO-333.

    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: June 24, 2015
    This is version 167 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

    External Data

    Dasty 3

    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 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.