Q9BWD1 (THIC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA acetyltransferase, cytosolic
EC=2.3.1.9

Alternative name(s):
Acetyl-CoA transferase-like protein
Cytosolic acetoacetyl-CoA thiolase

Gene names

Name:	ACAT2
Synonyms:	ACTL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred by curator Ref.1. Source: BHF-UCL
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular_function	acetyl-CoA C-acetyltransferase activity Inferred from direct assay Ref.1. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

Acetyl-CoA acetyltransferase, cytosolic

PRO_0000206409

Sites

Active site

92

1

Acyl-thioester intermediate

Active site

353

1

Proton acceptor

Active site

383

1

Proton acceptor

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7 Ref.10

Modified residue

200

1

N6-acetyllysine Ref.8

Modified residue

233

1

N6-acetyllysine Ref.8

Modified residue

235

1

N6-acetyllysine Ref.8

Natural variations

Natural variant

211

1

K → R. Ref.5
Corresponds to variant rs25683 [ dbSNP | Ensembl ].

VAR_019686

Experimental info

Sequence conflict

169

1

K → T in AAB30856. Ref.1

Sequence conflict

262

1

V → A in AAB30856. Ref.1

Sequence conflict

375

1

R → G in AAM00223. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

397

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Turn

24 – 27

4

Helix

30 – 45

16

Helix

49 – 51

3

Beta strand

54 – 58

5

Helix

69 – 76

8

Beta strand

85 – 88

4

Helix

91 – 93

3

Helix

94 – 107

14

Beta strand

112 – 122

11

Beta strand

136 – 138

3

Helix

145 – 149

5

Turn

154 – 156

3

Helix

160 – 171

12

Helix

175 – 194

20

Turn

195 – 201

7

Beta strand

205 – 209

5

Beta strand

212 – 216

5

Helix

228 – 232

5

Turn

240 – 243

4

Helix

248 – 250

3

Beta strand

255 – 265

11

Helix

266 – 271

6

Beta strand

277 – 287

11

Helix

290 – 295

6

Helix

297 – 308

12

Helix

312 – 314

3

Beta strand

317 – 320

4

Helix

325 – 335

11

Helix

339 – 341

3

Helix

348 – 351

4

Turn

355 – 357

3

Helix

358 – 373

16

Beta strand

377 – 384

8

Turn

385 – 387

3

Beta strand

388 – 396

9

Sequences

	Sequence		Length	Mass (Da)
	Q9BWD1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: E3A8DAFB6F341B18	FASTA	397	41,351
	10 20 30 40 50 60 MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV 70 80 90 100 110 120 LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME 130 140 150 160 170 180 NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK 190 200 210 220 230 240 VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT 250 260 270 280 290 300 DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA 310 320 330 340 350 360 IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC 370 380 390 RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase." Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T., Orii T. Biochem. Biophys. Res. Commun. 201:478-485(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Identification of the human acetyl CoA transferase like (ACTL) protein by yeast two-hybrid screen." Chen H., Peng J., Huang C.-H. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT ARG-211. Tissue: Lung.
[6]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-39; 195-210; 280-302 AND 342-361, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[8]	"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-200; LYS-233 AND LYS-235, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." 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. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[11]	"High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I." Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K. J. Mol. Biol. 347:189-201(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AL135914 Genomic DNA. Translation: CAI21850.1.
CH471051 Genomic DNA. Translation: EAW47619.1.
CH471051 Genomic DNA. Translation: EAW47620.1.
BC000408 mRNA. Translation: AAH00408.1.

PIR

JC2378.

RefSeq

NP_005882.2. NM_005891.2.

UniGene

Hs.571037.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WL4	X-ray	1.55	A	1-397	[»]
1WL5	X-ray	2.26	A	1-397	[»]

ProteinModelPortal

Q9BWD1.

SMR

Q9BWD1. Positions 4-397.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

106557. 10 interactions.

STRING

9606.ENSP00000356015.

Chemistry

ChEMBL

CHEMBL2240.

PTM databases

PhosphoSite

Q9BWD1.

Polymorphism databases

DMDM

52000838.

2D gel databases

OGP

Q9BWD1.

REPRODUCTION-2DPAGE

IPI00291419.

Proteomic databases

PaxDb

Q9BWD1.

PeptideAtlas

Q9BWD1.

PRIDE

Q9BWD1.

Protocols and materials databases

DNASU

39.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367048; ENSP00000356015; ENSG00000120437.

GeneID

39.

KEGG

hsa:39.

UCSC

uc010kjy.3. human.

Organism-specific databases

CTD

39.

GeneCards

GC06P160153.

HGNC

HGNC:94. ACAT2.

HPA

CAB021106.
HPA025736.
HPA025765.
HPA025811.

MIM

100678. gene+phenotype.

neXtProt

NX_Q9BWD1.

PharmGKB

PA19.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0183.

HOVERGEN

HBG003112.

InParanoid

Q9BWD1.

KO

K00626.

OrthoDB

EOG7JQBNG.

PhylomeDB

Q9BWD1.

TreeFam

TF300650.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000120437-MONOMER.

Gene expression databases

ArrayExpress

Q9BWD1.

Bgee

Q9BWD1.

CleanEx

HS_ACAT2.

Genevestigator

Q9BWD1.

Family and domain databases

Gene3D

3.40.47.10. 4 hits.

InterPro

IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]

PANTHER

PTHR18919. PTHR18919. 1 hit.

Pfam

PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

SUPFAM

SSF53901. SSF53901. 2 hits.

TIGRFAMs

TIGR01930. AcCoA-C-Actrans. 1 hit.

PROSITE

PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BWD1.

GeneWiki

ACAT2.

GenomeRNAi

39.

NextBio

153.

PRO

Q9BWD1.

SOURCE

Search...

Entry information

Entry name

THIC_HUMAN

Accession

Primary (citable) accession number: Q9BWD1
Secondary accession number(s): E1P5B1 , Q16146, Q5TCL7, Q8TDM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	February 19, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.