Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (T2)

 THIL_HUMAN              Reviewed;         427 AA.
P24752; B2R6H1; G3XAB4; Q96FG8;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
25-OCT-2017, entry version 190.
RecName: Full=Acetyl-CoA acetyltransferase, mitochondrial;
EC=2.3.1.9;
AltName: Full=Acetoacetyl-CoA thiolase;
AltName: Full=T2;
Flags: Precursor;
Name=ACAT1; Synonyms=ACAT, MAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1979337; DOI=10.1172/JCI114946;
Fukao T., Yamaguchi S., Kano M., Orii T., Fujiki Y., Osumi T.,
Hashimoto T.;
"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.";
J. Clin. Invest. 86:2086-2092(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1684944; DOI=10.1016/0378-1119(91)90623-J;
Kano M., Fukao T., Yamaguchi S., Orii T., Osumi T., Hashimoto T.;
"Structure and expression of the human mitochondrial acetoacetyl-CoA
thiolase-encoding gene.";
Gene 109:285-290(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-5.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 50-78 AND 312-338.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[8]
PROTEIN SEQUENCE OF 50-78 AND 231-243, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-181; LYS-251 AND
LYS-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 35-427 IN COMPLEX WITH
COENZYME A AND POTASSIUM, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=17371050; DOI=10.1021/bi6026192;
Haapalainen A.M., Merilaeinen G., Pirilae P.L., Kondo N., Fukao T.,
Wierenga R.K.;
"Crystallographic and kinetic studies of human mitochondrial
acetoacetyl-CoA thiolase: the importance of potassium and chloride
ions for its structure and function.";
Biochemistry 46:4305-4321(2007).
[15]
REVIEW ON 3KTD VARIANTS.
PubMed=7749408; DOI=10.1002/humu.1380050203;
Fukao T., Yamaguchi S., Orii T., Hashimoto T.;
"Molecular basis of beta-ketothiolase deficiency: mutations and
polymorphisms in the human mitochondrial acetoacetyl-coenzyme A
thiolase gene.";
Hum. Mutat. 5:113-120(1995).
[16]
VARIANT 3KTD ARG-183.
PubMed=1346617; DOI=10.1172/JCI115608;
Fukao T., Yamaguchi S., Orii T., Schutgens R.B.H., Osumi T.,
Hashimoto T.;
"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.";
J. Clin. Invest. 89:474-479(1992).
[17]
VARIANT 3KTD THR-380.
PubMed=1715688; DOI=10.1016/0006-291X(91)91343-B;
Fukao T., Yamaguchi S., Tomatsu S., Orii T., Frauendienst-Egger G.,
Schrod L., Osumi T., Hashimoto T.;
"Evidence for a structural mutation (347Ala to Thr) in a German family
with 3-ketothiolase deficiency.";
Biochem. Biophys. Res. Commun. 179:124-129(1991).
[18]
VARIANTS 3KTD ASP-158; MET-297 AND PRO-301.
PubMed=7728148; DOI=10.1002/humu.1380050105;
Wakazono A., Fukao T., Yamaguchi S., Hori T., Orii T., Lambert M.,
Mitchell G.A., Lee G.W., Hashimoto T.;
"Molecular, biochemical, and clinical characterization of
mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two
further patients.";
Hum. Mutat. 5:34-42(1995).
[19]
VARIANTS 3KTD SER-93; THR-312 AND PRO-333.
PubMed=9744475;
DOI=10.1002/(SICI)1098-1004(1998)12:4<245::AID-HUMU5>3.0.CO;2-E;
Fukao T., Nakamura H., Song X.-Q., Nakamura K., Orii K.E., Kohno Y.,
Kano M., Yamaguchi S., Hashimoto T., Orii T., Kondo N.;
"Characterization of N93S, I312T, and A333P missense mutations in two
Japanese families with mitochondrial acetoacetyl-CoA thiolase
deficiency.";
Hum. Mutat. 12:245-254(1998).
-!- FUNCTION: Plays a major role in ketone body metabolism.
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000255|PROSITE-ProRule:PRU10020,
ECO:0000269|PubMed:17371050}.
-!- ENZYME REGULATION: Activated by potassium ions, but not sodium
ions. {ECO:0000269|PubMed:17371050}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4 uM for acetoacetyl coenzyme A
{ECO:0000269|PubMed:17371050};
KM=20 uM for coenzyme A {ECO:0000269|PubMed:17371050};
KM=8 uM for 2-methylacetoacetyl coenzyme A
{ECO:0000269|PubMed:17371050};
KM=508 uM for acetyl coenzyme A {ECO:0000269|PubMed:17371050};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17371050}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P24752-1; Sequence=Displayed;
Name=2;
IsoId=P24752-2; Sequence=VSP_056844, VSP_056845;
Note=No experimental confirmation available.;
-!- PTM: Succinylation at Lys-268, adjacent to a coenzyme A binding
site. Desuccinylated by SIRT5 (By similarity). {ECO:0000250}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:1346617, ECO:0000269|PubMed:1715688,
ECO:0000269|PubMed:7728148, ECO:0000269|PubMed:9744475}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D90228; BAA14278.1; -; mRNA.
EMBL; D10511; BAA01387.1; -; Genomic_DNA.
EMBL; AK312574; BAG35468.1; -; mRNA.
EMBL; AP002433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67104.1; -; Genomic_DNA.
EMBL; CH471065; EAW67105.1; -; Genomic_DNA.
EMBL; BC010942; AAH10942.1; -; mRNA.
CCDS; CCDS8339.1; -. [P24752-1]
PIR; JH0255; JH0255.
RefSeq; NP_000010.1; NM_000019.3. [P24752-1]
UniGene; Hs.232375; -.
PDB; 2F2S; X-ray; 2.00 A; A/B/C/D=41-427.
PDB; 2IB7; X-ray; 2.05 A; A/B/C/D=34-427.
PDB; 2IB8; X-ray; 1.85 A; A/B/C/D=34-427.
PDB; 2IB9; X-ray; 2.05 A; A/B/C/D=34-427.
PDB; 2IBU; X-ray; 1.90 A; A/B/C/D=34-427.
PDB; 2IBW; X-ray; 1.90 A; A/B/C/D=34-427.
PDB; 2IBY; X-ray; 1.85 A; A/B/C/D=34-427.
PDBsum; 2F2S; -.
PDBsum; 2IB7; -.
PDBsum; 2IB8; -.
PDBsum; 2IB9; -.
PDBsum; 2IBU; -.
PDBsum; 2IBW; -.
PDBsum; 2IBY; -.
ProteinModelPortal; P24752; -.
SMR; P24752; -.
BioGrid; 106556; 64.
IntAct; P24752; 7.
MINT; MINT-5000530; -.
STRING; 9606.ENSP00000265838; -.
ChEMBL; CHEMBL2616; -.
DrugBank; DB00795; Sulfasalazine.
SwissLipids; SLP:000000701; -.
iPTMnet; P24752; -.
PhosphoSitePlus; P24752; -.
SwissPalm; P24752; -.
BioMuta; ACAT1; -.
DMDM; 135755; -.
REPRODUCTION-2DPAGE; IPI00030363; -.
UCD-2DPAGE; P24752; -.
EPD; P24752; -.
MaxQB; P24752; -.
PaxDb; P24752; -.
PeptideAtlas; P24752; -.
PRIDE; P24752; -.
TopDownProteomics; P24752-1; -. [P24752-1]
DNASU; 38; -.
Ensembl; ENST00000265838; ENSP00000265838; ENSG00000075239. [P24752-1]
Ensembl; ENST00000299355; ENSP00000299355; ENSG00000075239. [P24752-2]
GeneID; 38; -.
KEGG; hsa:38; -.
UCSC; uc001pjw.2; human. [P24752-1]
CTD; 38; -.
DisGeNET; 38; -.
EuPathDB; HostDB:ENSG00000075239.13; -.
GeneCards; ACAT1; -.
HGNC; HGNC:93; ACAT1.
HPA; HPA004428; -.
HPA; HPA007569; -.
MalaCards; ACAT1; -.
MIM; 203750; phenotype.
MIM; 607809; gene.
neXtProt; NX_P24752; -.
OpenTargets; ENSG00000075239; -.
Orphanet; 134; Ketoacidosis due to beta-ketothiolase deficiency.
PharmGKB; PA24431; -.
eggNOG; KOG1390; Eukaryota.
eggNOG; COG0183; LUCA.
GeneTree; ENSGT00390000009412; -.
HOGENOM; HOG000012238; -.
HOVERGEN; HBG003112; -.
InParanoid; P24752; -.
KO; K00626; -.
OMA; WDVYNKF; -.
OrthoDB; EOG091G09C6; -.
PhylomeDB; P24752; -.
TreeFam; TF300650; -.
BioCyc; MetaCyc:HS01167-MONOMER; -.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
Reactome; R-HSA-77108; Utilization of Ketone Bodies.
Reactome; R-HSA-77111; Synthesis of Ketone Bodies.
ChiTaRS; ACAT1; human.
EvolutionaryTrace; P24752; -.
GeneWiki; ACAT1; -.
GenomeRNAi; 38; -.
PRO; PR:P24752; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000075239; -.
CleanEx; HS_ACAT1; -.
ExpressionAtlas; P24752; baseline and differential.
Genevisible; P24752; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
GO; GO:0016830; F:carbon-carbon lyase activity; IDA:BHF-UCL.
GO; GO:0050662; F:coenzyme binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0016885; F:ligase activity, forming carbon-carbon bonds; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:BHF-UCL.
GO; GO:0046356; P:acetyl-CoA catabolic process; IDA:BHF-UCL.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:BHF-UCL.
GO; GO:0015936; P:coenzyme A metabolic process; IDA:BHF-UCL.
GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
GO; GO:0006550; P:isoleucine catabolic process; IMP:BHF-UCL.
GO; GO:0046951; P:ketone body biosynthetic process; TAS:Reactome.
GO; GO:0046952; P:ketone body catabolic process; IMP:BHF-UCL.
GO; GO:1902224; P:ketone body metabolic process; IC:BHF-UCL.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0072229; P:metanephric proximal convoluted tubule development; IEA:Ensembl.
GO; GO:1902860; P:propionyl-CoA biosynthetic process; IDA:BHF-UCL.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
InterPro; IPR020610; Thiolase_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
PROSITE; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
Complete proteome; Direct protein sequencing; Disease mutation;
Metal-binding; Mitochondrion; Polymorphism; Potassium;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 33 Mitochondrion. {ECO:0000250}.
CHAIN 34 427 Acetyl-CoA acetyltransferase,
mitochondrial.
/FTId=PRO_0000034085.
REGION 258 260 Coenzyme A binding.
ACT_SITE 126 126 Acyl-thioester intermediate.
{ECO:0000305}.
ACT_SITE 385 385 Proton acceptor. {ECO:0000305}.
ACT_SITE 413 413 Proton acceptor. {ECO:0000305}.
METAL 219 219 Potassium. {ECO:0000269|PubMed:17371050}.
METAL 280 280 Potassium; via carbonyl oxygen.
{ECO:0000269|PubMed:17371050}.
METAL 281 281 Potassium; via carbonyl oxygen.
{ECO:0000269|PubMed:17371050}.
METAL 283 283 Potassium; via carbonyl oxygen.
{ECO:0000269|PubMed:17371050}.
METAL 381 381 Potassium; via carbonyl oxygen.
{ECO:0000269|PubMed:17371050}.
BINDING 219 219 Coenzyme A.
{ECO:0000269|PubMed:17371050}.
BINDING 263 263 Coenzyme A.
{ECO:0000269|PubMed:17371050}.
BINDING 284 284 Coenzyme A.
{ECO:0000269|PubMed:17371050}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 78 78 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 174 174 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 174 174 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 181 181 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 181 181 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 190 190 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 190 190 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 202 202 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 202 202 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 223 223 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 223 223 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 230 230 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 230 230 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 243 243 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 251 251 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 257 257 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 263 263 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 263 263 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 266 266 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 268 268 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
MOD_RES 338 338 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8QZT1}.
VAR_SEQ 146 162 DVMVAGGMESMSNVPYV -> IKQETGSLAKICCHVRR
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056844.
VAR_SEQ 163 427 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056845.
VARIANT 5 5 A -> P (in dbSNP:rs3741056).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_007496.
VARIANT 85 85 Missing (in 3KTD).
/FTId=VAR_007497.
VARIANT 93 93 N -> S (in 3KTD; 10% activity;
dbSNP:rs120074145).
{ECO:0000269|PubMed:9744475}.
/FTId=VAR_007498.
VARIANT 152 152 G -> A (in 3KTD; dbSNP:rs762991875).
/FTId=VAR_007499.
VARIANT 158 158 N -> D (in 3KTD; no activity;
dbSNP:rs148639841).
{ECO:0000269|PubMed:7728148}.
/FTId=VAR_007500.
VARIANT 183 183 G -> R (in 3KTD; no activity;
dbSNP:rs120074141).
{ECO:0000269|PubMed:1346617}.
/FTId=VAR_007501.
VARIANT 297 297 T -> M (in 3KTD; 10% normal activity).
{ECO:0000269|PubMed:7728148}.
/FTId=VAR_007502.
VARIANT 301 301 A -> P (in 3KTD; 5% normal activity).
{ECO:0000269|PubMed:7728148}.
/FTId=VAR_007503.
VARIANT 312 312 I -> T (in 3KTD; 10% activity;
dbSNP:rs120074146).
{ECO:0000269|PubMed:9744475}.
/FTId=VAR_007504.
VARIANT 333 333 A -> P (in 3KTD; no activity;
dbSNP:rs120074147).
{ECO:0000269|PubMed:9744475}.
/FTId=VAR_007505.
VARIANT 379 379 G -> V (in 3KTD; dbSNP:rs120074143).
/FTId=VAR_007506.
VARIANT 380 380 A -> T (in 3KTD; 7% normal activity;
dbSNP:rs120074140).
{ECO:0000269|PubMed:1715688}.
/FTId=VAR_007507.
CONFLICT 340 340 V -> M (in Ref. 2; BAA01387).
{ECO:0000305}.
CONFLICT 346 346 D -> N (in Ref. 2; BAA01387).
{ECO:0000305}.
CONFLICT 380 380 A -> S (in Ref. 2; BAA01387).
{ECO:0000305}.
CONFLICT 412 412 I -> F (in Ref. 2; BAA01387).
{ECO:0000305}.
STRAND 42 49 {ECO:0000244|PDB:2IB8}.
TURN 58 61 {ECO:0000244|PDB:2IB8}.
HELIX 64 79 {ECO:0000244|PDB:2IB8}.
HELIX 83 85 {ECO:0000244|PDB:2IB8}.
STRAND 88 92 {ECO:0000244|PDB:2IB8}.
HELIX 103 110 {ECO:0000244|PDB:2IB8}.
STRAND 119 123 {ECO:0000244|PDB:2IB8}.
HELIX 125 127 {ECO:0000244|PDB:2IB8}.
HELIX 128 141 {ECO:0000244|PDB:2IB8}.
STRAND 146 155 {ECO:0000244|PDB:2IB8}.
HELIX 156 158 {ECO:0000244|PDB:2IB8}.
STRAND 161 163 {ECO:0000244|PDB:2IB8}.
STRAND 165 167 {ECO:0000244|PDB:2IB8}.
STRAND 173 177 {ECO:0000244|PDB:2IB8}.
HELIX 178 182 {ECO:0000244|PDB:2IB8}.
TURN 187 190 {ECO:0000244|PDB:2IB8}.
HELIX 193 204 {ECO:0000244|PDB:2IB8}.
HELIX 208 227 {ECO:0000244|PDB:2IB8}.
TURN 228 234 {ECO:0000244|PDB:2IB8}.
STRAND 238 240 {ECO:0000244|PDB:2IB8}.
STRAND 248 250 {ECO:0000244|PDB:2IB8}.
HELIX 255 257 {ECO:0000244|PDB:2IB8}.
TURN 261 263 {ECO:0000244|PDB:2IB8}.
HELIX 264 266 {ECO:0000244|PDB:2IB8}.
STRAND 273 275 {ECO:0000244|PDB:2IB8}.
TURN 280 282 {ECO:0000244|PDB:2IB8}.
STRAND 287 297 {ECO:0000244|PDB:2IB8}.
HELIX 298 303 {ECO:0000244|PDB:2IB8}.
STRAND 310 319 {ECO:0000244|PDB:2IB8}.
HELIX 322 327 {ECO:0000244|PDB:2IB8}.
HELIX 328 340 {ECO:0000244|PDB:2IB8}.
HELIX 344 346 {ECO:0000244|PDB:2IB8}.
STRAND 347 352 {ECO:0000244|PDB:2IB8}.
HELIX 357 367 {ECO:0000244|PDB:2IB8}.
HELIX 371 373 {ECO:0000244|PDB:2IB8}.
HELIX 380 383 {ECO:0000244|PDB:2IB8}.
TURN 387 389 {ECO:0000244|PDB:2IB8}.
HELIX 390 401 {ECO:0000244|PDB:2IB8}.
STRAND 407 414 {ECO:0000244|PDB:2IB8}.
TURN 415 417 {ECO:0000244|PDB:2IB8}.
STRAND 418 426 {ECO:0000244|PDB:2IB8}.
SEQUENCE 427 AA; 45200 MW; 2E81168EB39D0142 CRC64;
MAVLAALLRS GARSRSPLLR RLVQEIRYVE RSYVSKPTLK EVVIVSATRT PIGSFLGSLS
LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPTRQAVLG AGLPISTPCT
TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV
KDGLTDVYNK IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV
TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA
AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV
LANIKMLEID PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS
AMLIQKL


Related products :

Catalog number Product name Quantity
EIAAB42259 Acat1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Mouse,Mus musculus
EIAAB42257 Acat1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Rat,Rattus norvegicus
EIAAB42258 ACAT1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Bos taurus,Bovine
EIAAB42256 ACAT,ACAT1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Homo sapiens,Human,MAT,T2
EIAAB42250 ACAT2,Acetyl-CoA acetyltransferase, cytosolic,Acetyl-CoA transferase-like protein,ACTL,Cytosolic acetoacetyl-CoA thiolase,Homo sapiens,Human
EIAAB42249 Acat2,Acetyl-CoA acetyltransferase, cytosolic,Cytosolic acetoacetyl-CoA thiolase,Rat,Rattus norvegicus
GWB-B0ACA4 Anti- ACAT2 (acetyl-Coenzyme A acetyltransferase 2 (acetoacetyl Coenzyme A thiolase)) Antibody
EIAAB42248 Acat2,Acetyl-CoA acetyltransferase, cytosolic,Cytosolic acetoacetyl-CoA thiolase,Mouse,Mus musculus
GWB-678FF0 Anti- ACAT2 (acetyl-Coenzyme A acetyltransferase 2 (acetoacetyl Coenzyme A thiolase)) Antibody
201-20-0127 ACAT1{Homo sapiens acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase),}rabbit.pAb 0.1ml
EIAAB42261 3-ketoacyl-CoA thiolase, mitochondrial,Acaa2,Acetyl-CoA acyltransferase,Beta-ketothiolase,Mitochondrial 3-oxoacyl-CoA thiolase,Mouse,Mus musculus
EIAAB42262 3-ketoacyl-CoA thiolase, mitochondrial,ACAA2,Acetyl-CoA acyltransferase,Beta-ketothiolase,Bos taurus,Bovine,Mitochondrial 3-oxoacyl-CoA thiolase
EIAAB42263 3-ketoacyl-CoA thiolase, mitochondrial,Acaa2,Acetyl-CoA acyltransferase,Beta-ketothiolase,Mitochondrial 3-oxoacyl-CoA thiolase,Rat,Rattus norvegicus
EIAAB42260 3-ketoacyl-CoA thiolase, mitochondrial,ACAA2,Acetyl-CoA acyltransferase,Beta-ketothiolase,Homo sapiens,Human,Mitochondrial 3-oxoacyl-CoA thiolase,T1
EIAAB42253 3-ketoacyl-CoA thiolase A, peroxisomal,Acaa1a,Acetyl-CoA acyltransferase A,Beta-ketothiolase A,Peroxisomal 3-oxoacyl-CoA thiolase A,Rat,Rattus norvegicus
EIAAB42255 3-ketoacyl-CoA thiolase B, peroxisomal,Acaa1,Acaa1b,Acetyl-CoA acyltransferase B,Beta-ketothiolase B,Peroxisomal 3-oxoacyl-CoA thiolase B,Rat,Rattus norvegicus
EIAAB42252 3-ketoacyl-CoA thiolase A, peroxisomal,Acaa1,Acaa1a,Acetyl-CoA acyltransferase A,Beta-ketothiolase A,Mouse,Mus musculus,Peroxisomal 3-oxoacyl-CoA thiolase A
EIAAB42254 3-ketoacyl-CoA thiolase B, peroxisomal,Acaa1,Acaa1b,Acetyl-CoA acyltransferase B,Beta-ketothiolase B,Mouse,Mus musculus,Peroxisomal 3-oxoacyl-CoA thiolase B
EIAAB42251 3-ketoacyl-CoA thiolase, peroxisomal,ACAA,ACAA1,Acetyl-CoA acyltransferase,Beta-ketothiolase,Homo sapiens,Human,Peroxisomal 3-oxoacyl-CoA thiolase,PTHIO
EIAAB30023 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr
EIAAB30028 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr
EIAAB30027 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr
EIAAB30026 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr
EIAAB30025 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr
EIAAB30024 1-acylglycerophosphocholine O-acyltransferase,1-alkylglycerophosphocholine O-acetyltransferase,Acetyl-CoA lyso-PAF acetyltransferase,Acetyl-CoA lyso-platelet-activating factor acetyltransferase,Acyltr


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur