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, cytosolic (EC 2.3.1.9) (Acetyl-CoA transferase-like protein) (Cytosolic acetoacetyl-CoA thiolase)

 THIC_HUMAN              Reviewed;         397 AA.
Q9BWD1; B7Z233; E1P5B1; Q16146; Q5TCL7; Q8TDM4;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 2.
23-MAY-2018, entry version 160.
RecName: Full=Acetyl-CoA acetyltransferase, cytosolic;
EC=2.3.1.9;
AltName: Full=Acetyl-CoA transferase-like protein;
AltName: Full=Cytosolic acetoacetyl-CoA thiolase;
Name=ACAT2; Synonyms=ACTL;
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), AND PARTIAL PROTEIN SEQUENCE.
PubMed=7911016; DOI=10.1006/bbrc.1994.1726;
Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T.,
Orii T.;
"Molecular cloning and nucleotide sequence of complementary DNA for
human hepatic cytosolic acetoacetyl-coenzyme A thiolase.";
Biochem. Biophys. Res. Commun. 201:478-485(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Chen H., Peng J., Huang C.-H.;
"Identification of the human acetyl CoA transferase like (ACTL)
protein by yeast two-hybrid screen.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala;
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=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-211.
TISSUE=Lung;
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 16-39; 195-210; 280-302 AND 342-361, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-233 AND LYS-235,
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).
[10]
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
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).
[14]
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).
[15]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
PubMed=15733928; DOI=10.1016/j.jmb.2005.01.018;
Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K.;
"High resolution crystal structures of human cytosolic thiolase (CT):
a comparison of the active sites of human CT, bacterial thiolase, and
bacterial KAS I.";
J. Mol. Biol. 347:189-201(2005).
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000255|PROSITE-ProRule:PRU10020}.
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-1047273, EBI-739832;
P54274:TERF1; NbExp=2; IntAct=EBI-1047273, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BWD1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BWD1-2; Sequence=VSP_056217;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S70154; AAB30856.1; -; mRNA.
EMBL; AF356877; AAM00223.1; -; mRNA.
EMBL; AK294273; BAH11719.1; -; mRNA.
EMBL; AL135914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47619.1; -; Genomic_DNA.
EMBL; CH471051; EAW47620.1; -; Genomic_DNA.
EMBL; BC000408; AAH00408.1; -; mRNA.
CCDS; CCDS5268.1; -. [Q9BWD1-1]
PIR; JC2378; JC2378.
RefSeq; NP_001290182.1; NM_001303253.1. [Q9BWD1-2]
RefSeq; NP_005882.2; NM_005891.2. [Q9BWD1-1]
UniGene; Hs.571037; -.
PDB; 1WL4; X-ray; 1.55 A; A=1-397.
PDB; 1WL5; X-ray; 2.26 A; A=1-397.
PDBsum; 1WL4; -.
PDBsum; 1WL5; -.
ProteinModelPortal; Q9BWD1; -.
SMR; Q9BWD1; -.
BioGrid; 106557; 39.
IntAct; Q9BWD1; 5.
STRING; 9606.ENSP00000356015; -.
DrugBank; DB01992; Coenzyme A.
DrugBank; DB01915; S-Hydroxycysteine.
SwissLipids; SLP:000001266; -.
iPTMnet; Q9BWD1; -.
PhosphoSitePlus; Q9BWD1; -.
SwissPalm; Q9BWD1; -.
BioMuta; ACAT2; -.
DMDM; 52000838; -.
OGP; Q9BWD1; -.
REPRODUCTION-2DPAGE; IPI00291419; -.
EPD; Q9BWD1; -.
MaxQB; Q9BWD1; -.
PaxDb; Q9BWD1; -.
PeptideAtlas; Q9BWD1; -.
PRIDE; Q9BWD1; -.
DNASU; 39; -.
Ensembl; ENST00000367048; ENSP00000356015; ENSG00000120437. [Q9BWD1-1]
GeneID; 39; -.
KEGG; hsa:39; -.
UCSC; uc010kjy.4; human. [Q9BWD1-1]
CTD; 39; -.
DisGeNET; 39; -.
EuPathDB; HostDB:ENSG00000120437.8; -.
GeneCards; ACAT2; -.
HGNC; HGNC:94; ACAT2.
HPA; CAB021106; -.
HPA; HPA025736; -.
HPA; HPA025765; -.
HPA; HPA025811; -.
MalaCards; ACAT2; -.
MIM; 100678; gene+phenotype.
neXtProt; NX_Q9BWD1; -.
OpenTargets; ENSG00000120437; -.
PharmGKB; PA19; -.
eggNOG; KOG1391; Eukaryota.
eggNOG; COG0183; LUCA.
GeneTree; ENSGT00390000009412; -.
HOGENOM; HOG000012238; -.
HOVERGEN; HBG003112; -.
InParanoid; Q9BWD1; -.
KO; K00626; -.
OMA; ICPSIAI; -.
OrthoDB; EOG091G09C6; -.
PhylomeDB; Q9BWD1; -.
TreeFam; TF300650; -.
BioCyc; MetaCyc:ENSG00000120437-MONOMER; -.
BRENDA; 2.3.1.9; 2681.
Reactome; R-HSA-191273; Cholesterol biosynthesis.
ChiTaRS; ACAT2; human.
EvolutionaryTrace; Q9BWD1; -.
GeneWiki; ACAT2; -.
GenomeRNAi; 39; -.
PRO; PR:Q9BWD1; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000120437; -.
CleanEx; HS_ACAT2; -.
Genevisible; Q9BWD1; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 4.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
Complete proteome; Cytoplasm; Direct protein sequencing; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 397 Acetyl-CoA acetyltransferase, cytosolic.
/FTId=PRO_0000206409.
ACT_SITE 92 92 Acyl-thioester intermediate.
ACT_SITE 353 353 Proton acceptor.
ACT_SITE 383 383 Proton acceptor.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 200 200 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 235 235 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 19 MNAGSDPVVIVSAARTIIG -> MGSHPVLRIWGNRRATAA
SLGRSGGRLSSPRLLRVVAPTLTFAQTSRC (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056217.
VARIANT 211 211 K -> R (in dbSNP:rs25683).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_019686.
CONFLICT 169 169 K -> T (in Ref. 1; AAB30856).
{ECO:0000305}.
CONFLICT 262 262 V -> A (in Ref. 1; AAB30856).
{ECO:0000305}.
CONFLICT 375 375 R -> G (in Ref. 2; AAM00223).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:1WL4}.
TURN 24 27 {ECO:0000244|PDB:1WL4}.
HELIX 30 45 {ECO:0000244|PDB:1WL4}.
HELIX 49 51 {ECO:0000244|PDB:1WL4}.
STRAND 54 58 {ECO:0000244|PDB:1WL4}.
HELIX 69 76 {ECO:0000244|PDB:1WL4}.
STRAND 85 88 {ECO:0000244|PDB:1WL4}.
HELIX 91 93 {ECO:0000244|PDB:1WL4}.
HELIX 94 107 {ECO:0000244|PDB:1WL4}.
STRAND 112 122 {ECO:0000244|PDB:1WL4}.
STRAND 136 138 {ECO:0000244|PDB:1WL4}.
HELIX 145 149 {ECO:0000244|PDB:1WL4}.
TURN 154 156 {ECO:0000244|PDB:1WL4}.
HELIX 160 171 {ECO:0000244|PDB:1WL4}.
HELIX 175 194 {ECO:0000244|PDB:1WL4}.
TURN 195 201 {ECO:0000244|PDB:1WL4}.
STRAND 205 209 {ECO:0000244|PDB:1WL4}.
STRAND 212 216 {ECO:0000244|PDB:1WL4}.
HELIX 228 232 {ECO:0000244|PDB:1WL4}.
TURN 240 243 {ECO:0000244|PDB:1WL5}.
HELIX 248 250 {ECO:0000244|PDB:1WL5}.
STRAND 255 265 {ECO:0000244|PDB:1WL4}.
HELIX 266 271 {ECO:0000244|PDB:1WL4}.
STRAND 277 287 {ECO:0000244|PDB:1WL4}.
HELIX 290 295 {ECO:0000244|PDB:1WL4}.
HELIX 297 308 {ECO:0000244|PDB:1WL4}.
HELIX 312 314 {ECO:0000244|PDB:1WL4}.
STRAND 317 320 {ECO:0000244|PDB:1WL4}.
HELIX 325 335 {ECO:0000244|PDB:1WL4}.
HELIX 339 341 {ECO:0000244|PDB:1WL4}.
HELIX 348 351 {ECO:0000244|PDB:1WL4}.
TURN 355 357 {ECO:0000244|PDB:1WL4}.
HELIX 358 373 {ECO:0000244|PDB:1WL4}.
STRAND 377 384 {ECO:0000244|PDB:1WL4}.
TURN 385 387 {ECO:0000244|PDB:1WL4}.
STRAND 388 396 {ECO:0000244|PDB:1WL4}.
SEQUENCE 397 AA; 41351 MW; E3A8DAFB6F341B18 CRC64;
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV
LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME
NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK
VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT
DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC
RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE


Related products :

Catalog number Product name Quantity
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
EIAAB42248 Acat2,Acetyl-CoA acetyltransferase, cytosolic,Cytosolic acetoacetyl-CoA thiolase,Mouse,Mus musculus
EIAAB42258 ACAT1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Bos taurus,Bovine
EIAAB42259 Acat1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Mouse,Mus musculus
EIAAB42257 Acat1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Rat,Rattus norvegicus
EIAAB42256 ACAT,ACAT1,Acetoacetyl-CoA thiolase,Acetyl-CoA acetyltransferase, mitochondrial,Homo sapiens,Human,MAT,T2
GWB-B0ACA4 Anti- ACAT2 (acetyl-Coenzyme A acetyltransferase 2 (acetoacetyl Coenzyme A thiolase)) Antibody
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
XW-7912 Acetyl-CoA acetyltransferase, cytosolic Antibody 0.05 mg
10-288-22016F Acetyl-CoA acetyltransferase. cytosolic variant - 0.1 mg
10-288-22016F Acetyl-CoA acetyltransferase. cytosolic variant - 0.05 mg
18-003-42288 Acetyl-CoA acetyltransferase. cytosolic variant - N_A Polyclonal 0.1 mg Protein A
18-003-42287 Acetyl-CoA acetyltransferase. cytosolic variant - N_A Polyclonal 0.1 mg Protein A
PROM2_RAT Human ELISA Kit FOR Acetyl-CoA acetyltransferase, cytosolic 96T
CSB-EL001135RA Rat Acetyl-CoA acetyltransferase, cytosolic(ACAT2) ELISA kit 96T
15-288-22016 Acetyl-CoA acetyltransferase. cytosolic variant - Polyclonal 0.05 mg
EH480 Acetyl Coenzyme A Acetyltransferase 2, cytosolic Elisa Kit 96T
E0441d Human ELISA Kit FOR Acetyl-CoA acetyltransferase, cytosolic 96T
15-288-22016 Acetyl-CoA acetyltransferase. cytosolic variant - Polyclonal 0.1 mg
CSB-EL001135HU Human Acetyl-CoA acetyltransferase, cytosolic(ACAT2) ELISA kit 96T
CSB-EL001135MO Mouse Acetyl-CoA acetyltransferase, cytosolic(ACAT2) ELISA kit 96T
CSB-EL001135RA Rat Acetyl-CoA acetyltransferase, cytosolic(ACAT2) ELISA kit SpeciesRat 96T
CSB-EL001135GU Guinea pig Acetyl-CoA acetyltransferase, cytosolic(ACAT2) ELISA kit 96T


 

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