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P24752

- THIL_HUMAN

UniProt

P24752 - THIL_HUMAN

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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

ACAT1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.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
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: Chromosome 11

Organism-specific databases

HGNCiHGNC:93. ACAT1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: HPA
Complete GO annotation...

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

BgeeiP24752.
CleanExiHS_ACAT1.
ExpressionAtlasiP24752. baseline and differential.
GenevestigatoriP24752.

Organism-specific databases

HPAiHPA004428.
HPA007569.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi106556. 39 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.
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]

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. Align

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.
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.
PIRiJH0255.
RefSeqiNP_000010.1. NM_000019.3.
UniGeneiHs.232375.

Genome annotation databases

EnsembliENST00000265838; ENSP00000265838; ENSG00000075239. [P24752-1]
ENST00000299355; ENSP00000299355; ENSG00000075239. [P24752-2]
GeneIDi38.
KEGGihsa:38.
UCSCiuc001pjy.3. human. [P24752-1]

Polymorphism databases

DMDMi135755.

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 .
CCDSi CCDS8339.1.
PIRi JH0255.
RefSeqi NP_000010.1. NM_000019.3.
UniGenei Hs.232375.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 39 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 . [P24752-1 ]
ENST00000299355 ; ENSP00000299355 ; ENSG00000075239 . [P24752-2 ]
GeneIDi 38.
KEGGi hsa:38.
UCSCi uc001pjy.3. human. [P24752-1 ]

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.
GeneTreei ENSGT00390000009412.
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

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

Gene expression databases

Bgeei P24752.
CleanExi HS_ACAT1.
ExpressionAtlasi P24752. baseline and differential.
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

« 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. "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].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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: November 26, 2014
This is version 160 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