UniProtKB - P24752 (THIL_HUMAN)
Protein
Acetyl-CoA acetyltransferase, mitochondrial
Gene
ACAT1
Organism
Homo sapiens (Human)
Status
Functioni
This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (PubMed:1715688, PubMed:7728148, PubMed:9744475). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (PubMed:1715688, PubMed:7728148, PubMed:9744475). The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA (PubMed:17371050). Thereby, it plays a major role in ketone body metabolism (PubMed:17371050, PubMed:1715688, PubMed:7728148, PubMed:9744475).4 Publications
Catalytic activityi
- EC:2.3.1.9PROSITE-ProRule annotation4 Publications
Activity regulationi
Activated by potassium ions, but not sodium ions.1 Publication
Kineticsi
kcat is 21 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 8 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl) (PubMed:17371050). kcat is 61 sec(-1) for the degradation of 2-methylacetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 14 sec(-1) for the degradation of 2-methylacetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl) (PubMed:17371050). kcat is 3.5 sec(-1) for the synthesis of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050).1 Publication
- KM=4 µM for acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
- KM=8 µM for acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
- KM=20 µM for CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
- KM=66 µM for CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
- KM=8 µM for 2-methyl-3-oxobutanoyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
- KM=8 µM for 2-methyl-3-oxobutanoyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)1 Publication
- KM=508 µM for acetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl)1 Publication
: fatty acid beta-oxidation Pathwayi
This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.3 PublicationsView all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 126 | Acyl-thioester intermediate1 Publication | 1 | |
Metal bindingi | 219 | Potassium1 Publication | 1 | |
Binding sitei | 219 | Coenzyme A1 Publication | 1 | |
Binding sitei | 263 | Coenzyme A1 Publication | 1 | |
Metal bindingi | 280 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 281 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 283 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 284 | Coenzyme A1 Publication | 1 | |
Metal bindingi | 381 | Potassium; via carbonyl oxygen1 Publication | 1 | |
Sitei | 385 | Increases nucleophilicity of active site Cys1 Publication | 1 | |
Active sitei | 413 | Proton donor/acceptor1 Publication | 1 |
GO - Molecular functioni
- acetyl-CoA C-acetyltransferase activity Source: BHF-UCL
- acetyl-CoA C-acyltransferase activity Source: GO_Central
- C-acetyltransferase activity Source: BHF-UCL
- enzyme binding Source: Ensembl
- identical protein binding Source: Ensembl
- potassium ion binding Source: BHF-UCL
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
- cholesterol esterification Source: ARUK-UCL
- 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
- response to hormone Source: Ensembl
- response to organic cyclic compound Source: Ensembl
- response to starvation Source: Ensembl
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Ligand | Metal-binding, Potassium |
Enzyme and pathway databases
BioCyci | MetaCyc:HS01167-MONOMER |
PathwayCommonsi | P24752 |
Reactomei | R-HSA-70895, Branched-chain amino acid catabolism R-HSA-77108, Utilization of Ketone Bodies R-HSA-77111, Synthesis of Ketone Bodies |
SABIO-RKi | P24752 |
UniPathwayi | UPA00659 |
Chemistry databases
SwissLipidsi | SLP:000000701 |
Names & Taxonomyi
Protein namesi | Recommended name: Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9PROSITE-ProRule annotation4 Publications)Alternative name(s): Acetoacetyl-CoA thiolase T2 |
Gene namesi | Name:ACAT1 Synonyms:ACAT, MAT |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000075239.13 |
HGNCi | HGNC:93, ACAT1 |
MIMi | 607809, gene |
neXtProti | NX_P24752 |
Subcellular locationi
Mitochondrion
- Mitochondrion 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: UniProtKB
Keywords - Cellular componenti
MitochondrionPathology & 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 autosomal recessive inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_007497 | 85 | Missing in 3KTD. | 1 | |
Natural variantiVAR_007498 | 93 | N → S in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074145EnsemblClinVar. | 1 | |
Natural variantiVAR_007499 | 152 | G → A in 3KTD. Corresponds to variant dbSNP:rs762991875EnsemblClinVar. | 1 | |
Natural variantiVAR_007500 | 158 | N → D in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs148639841EnsemblClinVar. | 1 | |
Natural variantiVAR_007501 | 183 | G → R in 3KTD; no activity. 1 PublicationCorresponds to variant dbSNP:rs120074141EnsemblClinVar. | 1 | |
Natural variantiVAR_007502 | 297 | T → M in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs886041122EnsemblClinVar. | 1 | |
Natural variantiVAR_007503 | 301 | A → P in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs1420321267EnsemblClinVar. | 1 | |
Natural variantiVAR_007504 | 312 | I → T in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074146EnsemblClinVar. | 1 | |
Natural variantiVAR_007505 | 333 | A → P in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074147EnsemblClinVar. | 1 | |
Natural variantiVAR_007506 | 379 | G → V in 3KTD. Corresponds to variant dbSNP:rs120074143EnsemblClinVar. | 1 | |
Natural variantiVAR_007507 | 380 | A → T in 3KTD; decreased protein stability. 1 PublicationCorresponds to variant dbSNP:rs120074140EnsemblClinVar. | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 38 |
MalaCardsi | ACAT1 |
MIMi | 203750, phenotype |
OpenTargetsi | ENSG00000075239 |
Orphaneti | 134, Beta-ketothiolase deficiency |
PharmGKBi | PA24431 |
Miscellaneous databases
Pharosi | P24752, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2616 |
DrugBanki | DB09061, Cannabidiol DB14009, Medical Cannabis DB14011, Nabiximols DB00795, Sulfasalazine |
DrugCentrali | P24752 |
GuidetoPHARMACOLOGYi | 2435 |
Polymorphism and mutation databases
BioMutai | ACAT1 |
DMDMi | 135755 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 33 | MitochondrionBy similarityAdd BLAST | 33 | |
ChainiPRO_0000034085 | 34 – 427 | Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST | 394 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 66 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 66 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 78 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 174 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 174 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 181 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 181 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 190 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 190 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 202 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 202 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 223 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 223 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 230 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 230 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 243 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 251 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 257 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 263 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 263 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 266 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 268 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 273 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 338 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
Succinylation at Lys-268, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity
Keywords - PTMi
AcetylationProteomic databases
EPDi | P24752 |
jPOSTi | P24752 |
MassIVEi | P24752 |
MaxQBi | P24752 |
PaxDbi | P24752 |
PeptideAtlasi | P24752 |
PRIDEi | P24752 |
ProteomicsDBi | 33702 54224 [P24752-1] |
TopDownProteomicsi | P24752-1 [P24752-1] |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00030363 |
UCD-2DPAGEi | P24752 |
PTM databases
iPTMneti | P24752 |
MetOSitei | P24752 |
PhosphoSitePlusi | P24752 |
SwissPalmi | P24752 |
Expressioni
Gene expression databases
Bgeei | ENSG00000075239, Expressed in nephron tubule and 245 other tissues |
ExpressionAtlasi | P24752, baseline and differential |
Genevisiblei | P24752, HS |
Organism-specific databases
HPAi | ENSG00000075239, Tissue enhanced (liver) |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationGO - Molecular functioni
- enzyme binding Source: Ensembl
- identical protein binding Source: Ensembl
Protein-protein interaction databases
BioGRIDi | 106556, 112 interactors |
IntActi | P24752, 25 interactors |
MINTi | P24752 |
STRINGi | 9606.ENSP00000265838 |
Miscellaneous databases
RNActi | P24752, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P24752 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P24752 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 258 – 260 | Coenzyme A binding1 Publication | 3 |
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1390, Eukaryota |
GeneTreei | ENSGT01010000222371 |
HOGENOMi | CLU_031026_0_1_1 |
InParanoidi | P24752 |
OMAi | TNVCCTT |
PhylomeDBi | P24752 |
TreeFami | TF300650 |
Family and domain databases
CDDi | cd00751, thiolase, 1 hit |
Gene3Di | 3.40.47.10, 2 hits |
InterProi | View protein in InterPro IPR002155, Thiolase IPR016039, Thiolase-like IPR020615, Thiolase_acyl_enz_int_AS IPR020610, Thiolase_AS IPR020617, Thiolase_C IPR020613, Thiolase_CS IPR020616, Thiolase_N |
Pfami | View protein in Pfam PF02803, Thiolase_C, 1 hit PF00108, Thiolase_N, 1 hit |
PIRSFi | PIRSF000429, Ac-CoA_Ac_transf, 1 hit |
SUPFAMi | SSF53901, SSF53901, 2 hits |
TIGRFAMsi | TIGR01930, AcCoA-C-Actrans, 1 hit |
PROSITEi | View protein in PROSITE PS00098, THIOLASE_1, 1 hit PS00737, THIOLASE_2, 1 hit PS00099, THIOLASE_3, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P24752-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A5F9ZHL1 | A0A5F9ZHL1_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 434 | Annotation score: | ||
A0A5F9ZHJ0 | A0A5F9ZHJ0_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 337 | Annotation score: | ||
A0A5F9ZHD4 | A0A5F9ZHD4_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 306 | Annotation score: | ||
A0A5F9ZI66 | A0A5F9ZI66_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 322 | Annotation score: | ||
H0YEL7 | H0YEL7_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 136 | Annotation score: | ||
E9PRQ6 | E9PRQ6_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 141 | Annotation score: | ||
A0A5F9ZHJ7 | A0A5F9ZHJ7_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 315 | Annotation score: | ||
A0A5F9ZHH9 | A0A5F9ZHH9_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 197 | Annotation score: | ||
A0A5F9ZHL7 | A0A5F9ZHL7_HUMAN | Acetyl-CoA acetyltransferase, mitoc... | ACAT1 | 106 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 340 | V → M in BAA01387 (PubMed:1684944).Curated | 1 | |
Sequence conflicti | 346 | D → N in BAA01387 (PubMed:1684944).Curated | 1 | |
Sequence conflicti | 380 | A → S in BAA01387 (PubMed:1684944).Curated | 1 | |
Sequence conflicti | 412 | I → F in BAA01387 (PubMed:1684944).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_007496 | 5 | A → P1 PublicationCorresponds to variant dbSNP:rs3741056EnsemblClinVar. | 1 | |
Natural variantiVAR_007497 | 85 | Missing in 3KTD. | 1 | |
Natural variantiVAR_007498 | 93 | N → S in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074145EnsemblClinVar. | 1 | |
Natural variantiVAR_007499 | 152 | G → A in 3KTD. Corresponds to variant dbSNP:rs762991875EnsemblClinVar. | 1 | |
Natural variantiVAR_007500 | 158 | N → D in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs148639841EnsemblClinVar. | 1 | |
Natural variantiVAR_007501 | 183 | G → R in 3KTD; no activity. 1 PublicationCorresponds to variant dbSNP:rs120074141EnsemblClinVar. | 1 | |
Natural variantiVAR_007502 | 297 | T → M in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs886041122EnsemblClinVar. | 1 | |
Natural variantiVAR_007503 | 301 | A → P in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs1420321267EnsemblClinVar. | 1 | |
Natural variantiVAR_007504 | 312 | I → T in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074146EnsemblClinVar. | 1 | |
Natural variantiVAR_007505 | 333 | A → P in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity. 1 PublicationCorresponds to variant dbSNP:rs120074147EnsemblClinVar. | 1 | |
Natural variantiVAR_007506 | 379 | G → V in 3KTD. Corresponds to variant dbSNP:rs120074143EnsemblClinVar. | 1 | |
Natural variantiVAR_007507 | 380 | A → T in 3KTD; decreased protein stability. 1 PublicationCorresponds to variant dbSNP:rs120074140EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056844 | 146 – 162 | DVMVA…NVPYV → IKQETGSLAKICCHVRR in isoform 2. 1 PublicationAdd BLAST | 17 | |
Alternative sequenceiVSP_056845 | 163 – 427 | Missing in isoform 2. 1 PublicationAdd BLAST | 265 |
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 [P24752-1] |
PIRi | JH0255 |
RefSeqi | NP_000010.1, NM_000019.3 [P24752-1] |
Genome annotation databases
Ensembli | ENST00000265838; ENSP00000265838; ENSG00000075239 [P24752-1] ENST00000299355; ENSP00000299355; ENSG00000075239 [P24752-2] |
GeneIDi | 38 |
KEGGi | hsa:38 |
UCSCi | uc001pjw.2, human [P24752-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
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 [P24752-1] |
PIRi | JH0255 |
RefSeqi | NP_000010.1, NM_000019.3 [P24752-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P24752 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106556, 112 interactors |
IntActi | P24752, 25 interactors |
MINTi | P24752 |
STRINGi | 9606.ENSP00000265838 |
Chemistry databases
ChEMBLi | CHEMBL2616 |
DrugBanki | DB09061, Cannabidiol DB14009, Medical Cannabis DB14011, Nabiximols DB00795, Sulfasalazine |
DrugCentrali | P24752 |
GuidetoPHARMACOLOGYi | 2435 |
SwissLipidsi | SLP:000000701 |
PTM databases
iPTMneti | P24752 |
MetOSitei | P24752 |
PhosphoSitePlusi | P24752 |
SwissPalmi | P24752 |
Polymorphism and mutation databases
BioMutai | ACAT1 |
DMDMi | 135755 |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00030363 |
UCD-2DPAGEi | P24752 |
Proteomic databases
EPDi | P24752 |
jPOSTi | P24752 |
MassIVEi | P24752 |
MaxQBi | P24752 |
PaxDbi | P24752 |
PeptideAtlasi | P24752 |
PRIDEi | P24752 |
ProteomicsDBi | 33702 54224 [P24752-1] |
TopDownProteomicsi | P24752-1 [P24752-1] |
Protocols and materials databases
Antibodypediai | 1354, 565 antibodies |
DNASUi | 38 |
Genome annotation databases
Ensembli | ENST00000265838; ENSP00000265838; ENSG00000075239 [P24752-1] ENST00000299355; ENSP00000299355; ENSG00000075239 [P24752-2] |
GeneIDi | 38 |
KEGGi | hsa:38 |
UCSCi | uc001pjw.2, human [P24752-1] |
Organism-specific databases
CTDi | 38 |
DisGeNETi | 38 |
EuPathDBi | HostDB:ENSG00000075239.13 |
GeneCardsi | ACAT1 |
HGNCi | HGNC:93, ACAT1 |
HPAi | ENSG00000075239, Tissue enhanced (liver) |
MalaCardsi | ACAT1 |
MIMi | 203750, phenotype 607809, gene |
neXtProti | NX_P24752 |
OpenTargetsi | ENSG00000075239 |
Orphaneti | 134, Beta-ketothiolase deficiency |
PharmGKBi | PA24431 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1390, Eukaryota |
GeneTreei | ENSGT01010000222371 |
HOGENOMi | CLU_031026_0_1_1 |
InParanoidi | P24752 |
OMAi | TNVCCTT |
PhylomeDBi | P24752 |
TreeFami | TF300650 |
Enzyme and pathway databases
UniPathwayi | UPA00659 |
BioCyci | MetaCyc:HS01167-MONOMER |
PathwayCommonsi | P24752 |
Reactomei | R-HSA-70895, Branched-chain amino acid catabolism R-HSA-77108, Utilization of Ketone Bodies R-HSA-77111, Synthesis of Ketone Bodies |
SABIO-RKi | P24752 |
Miscellaneous databases
BioGRID-ORCSi | 38, 20 hits in 846 CRISPR screens |
ChiTaRSi | ACAT1, human |
EvolutionaryTracei | P24752 |
GeneWikii | ACAT1 |
GenomeRNAii | 38 |
Pharosi | P24752, Tchem |
PROi | PR:P24752 |
RNActi | P24752, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000075239, Expressed in nephron tubule and 245 other tissues |
ExpressionAtlasi | P24752, baseline and differential |
Genevisiblei | P24752, HS |
Family and domain databases
CDDi | cd00751, thiolase, 1 hit |
Gene3Di | 3.40.47.10, 2 hits |
InterProi | View protein in InterPro IPR002155, Thiolase IPR016039, Thiolase-like IPR020615, Thiolase_acyl_enz_int_AS IPR020610, Thiolase_AS IPR020617, Thiolase_C IPR020613, Thiolase_CS IPR020616, Thiolase_N |
Pfami | View protein in Pfam PF02803, Thiolase_C, 1 hit PF00108, Thiolase_N, 1 hit |
PIRSFi | PIRSF000429, Ac-CoA_Ac_transf, 1 hit |
SUPFAMi | SSF53901, SSF53901, 2 hits |
TIGRFAMsi | TIGR01930, AcCoA-C-Actrans, 1 hit |
PROSITEi | View protein in PROSITE PS00098, THIOLASE_1, 1 hit PS00737, THIOLASE_2, 1 hit PS00099, THIOLASE_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | THIL_HUMAN | |
Accessioni | P24752Primary (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: | December 2, 2020 | |
This is version 216 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations