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P24752

- THIL_HUMAN

UniProt

P24752 - THIL_HUMAN

Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

ACAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Plays a major role in ketone body metabolism.

    Catalytic activityi

    2 acetyl-CoA = CoA + acetoacetyl-CoA.1 PublicationPROSITE-ProRule annotation

    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

    1. acetyl-CoA C-acetyltransferase activity Source: Reactome
    2. coenzyme binding Source: Ensembl
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. adipose tissue development Source: Ensembl
    2. brain development Source: Ensembl
    3. branched-chain amino acid catabolic process Source: Reactome
    4. cellular ketone body metabolic process Source: Reactome
    5. cellular lipid metabolic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. ketone body biosynthetic process Source: Reactome
    8. ketone body catabolic process Source: Reactome
    9. liver development Source: Ensembl
    10. metanephric proximal convoluted tubule development Source: Ensembl
    11. protein homooligomerization Source: Ensembl
    12. response to hormone Source: Ensembl
    13. response to organic cyclic compound Source: Ensembl
    14. response to starvation Source: Ensembl
    15. small molecule metabolic process Source: Reactome

    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:93. ACAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    3-ketothiolase deficiency (3KTD) [MIM:203750]: An 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP24752.
    BgeeiP24752.
    CleanExiHS_ACAT1.
    GenevestigatoriP24752.

    Organism-specific databases

    HPAiHPA004428.
    HPA007569.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi106556. 37 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 – 498
    Turni58 – 614
    Helixi64 – 7916
    Helixi83 – 853
    Beta strandi88 – 925
    Helixi103 – 1108
    Beta strandi119 – 1235
    Helixi125 – 1273
    Helixi128 – 14114
    Beta strandi146 – 15510
    Helixi156 – 1583
    Beta strandi161 – 1633
    Beta strandi165 – 1673
    Beta strandi173 – 1775
    Helixi178 – 1825
    Turni187 – 1904
    Helixi193 – 20412
    Helixi208 – 22720
    Turni228 – 2347
    Beta strandi238 – 2403
    Beta strandi248 – 2503
    Helixi255 – 2573
    Turni261 – 2633
    Helixi264 – 2663
    Beta strandi273 – 2753
    Turni280 – 2823
    Beta strandi287 – 29711
    Helixi298 – 3036
    Beta strandi310 – 31910
    Helixi322 – 3276
    Helixi328 – 34013
    Helixi344 – 3463
    Beta strandi347 – 3526
    Helixi357 – 36711
    Helixi371 – 3733
    Helixi380 – 3834
    Turni387 – 3893
    Helixi390 – 40112
    Beta strandi407 – 4148
    Turni415 – 4173
    Beta strandi418 – 4269

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000012238.
    HOVERGENiHBG003112.
    InParanoidiP24752.
    KOiK00626.
    OMAiDQVAIWE.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P24752-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVLAALLRS GARSRSPLLR RLVQEIRYVE RSYVSKPTLK EVVIVSATRT    50
    PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG 100
    QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA 150
    GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK IHMGSCAENT 200
    AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV 250
    KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA 300
    AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW 350
    EVNEAFSLVV LANIKMLEID PQKVNINGGA VSLGHPIGMS GARIVGHLTH 400
    ALKQGEYGLA SICNGGGGAS AMLIQKL 427
    Length:427
    Mass (Da):45,200
    Last modified:March 1, 1992 - v1
    Checksum:i2E81168EB39D0142
    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.
    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90228 mRNA. Translation: BAA14278.1.
    D10511 Genomic DNA. Translation: BAA01387.1.
    AK312574 mRNA. Translation: BAG35468.1.
    CH471065 Genomic DNA. Translation: EAW67104.1.
    CCDSiCCDS8339.1.
    PIRiJH0255.
    RefSeqiNP_000010.1. NM_000019.3.
    UniGeneiHs.232375.

    Genome annotation databases

    EnsembliENST00000265838; ENSP00000265838; ENSG00000075239.
    GeneIDi38.
    KEGGihsa:38.
    UCSCiuc001pjy.3. human.

    Polymorphism databases

    DMDMi135755.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90228 mRNA. Translation: BAA14278.1 .
    D10511 Genomic DNA. Translation: BAA01387.1 .
    AK312574 mRNA. Translation: BAG35468.1 .
    CH471065 Genomic DNA. Translation: EAW67104.1 .
    CCDSi CCDS8339.1.
    PIRi JH0255.
    RefSeqi NP_000010.1. NM_000019.3.
    UniGenei Hs.232375.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F2S X-ray 2.00 A/B/C/D 41-427 [» ]
    2IB7 X-ray 2.05 A/B/C/D 34-427 [» ]
    2IB8 X-ray 1.85 A/B/C/D 34-427 [» ]
    2IB9 X-ray 2.05 A/B/C/D 34-427 [» ]
    2IBU X-ray 1.90 A/B/C/D 34-427 [» ]
    2IBW X-ray 1.90 A/B/C/D 34-427 [» ]
    2IBY X-ray 1.85 A/B/C/D 34-427 [» ]
    ProteinModelPortali P24752.
    SMRi P24752. Positions 35-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106556. 37 interactions.
    IntActi P24752. 3 interactions.
    MINTi MINT-5000530.
    STRINGi 9606.ENSP00000265838.

    Chemistry

    BindingDBi P24752.
    DrugBanki DB00795. Sulfasalazine.

    PTM databases

    PhosphoSitei P24752.

    Polymorphism databases

    DMDMi 135755.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00030363.
    UCD-2DPAGE P24752.

    Proteomic databases

    MaxQBi P24752.
    PaxDbi P24752.
    PeptideAtlasi P24752.
    PRIDEi P24752.

    Protocols and materials databases

    DNASUi 38.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265838 ; ENSP00000265838 ; ENSG00000075239 .
    GeneIDi 38.
    KEGGi hsa:38.
    UCSCi uc001pjy.3. human.

    Organism-specific databases

    CTDi 38.
    GeneCardsi GC11P107992.
    HGNCi HGNC:93. ACAT1.
    HPAi HPA004428.
    HPA007569.
    MIMi 203750. phenotype.
    607809. gene.
    neXtProti NX_P24752.
    Orphaneti 134. Ketoacidosis due to beta-ketothiolase deficiency.
    PharmGKBi PA24431.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0183.
    HOGENOMi HOG000012238.
    HOVERGENi HBG003112.
    InParanoidi P24752.
    KOi K00626.
    OMAi DQVAIWE.
    OrthoDBi EOG7JQBNG.
    PhylomeDBi P24752.
    TreeFami TF300650.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01167-MONOMER.
    Reactomei REACT_1464. Synthesis of Ketone Bodies.
    REACT_197. Branched-chain amino acid catabolism.
    REACT_59. Utilization of Ketone Bodies.

    Miscellaneous databases

    EvolutionaryTracei P24752.
    GeneWikii ACAT1.
    GenomeRNAii 38.
    NextBioi 149.
    PROi P24752.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24752.
    Bgeei P24752.
    CleanExi HS_ACAT1.
    Genevestigatori P24752.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. 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 ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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.
    6. 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.
    7. "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].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 158 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