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Q9BWD1 (THIC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred by curator Ref.1. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: BHF-UCL

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionacetyl-CoA C-acetyltransferase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Acetyl-CoA acetyltransferase, cytosolic
PRO_0000206409

Sites

Active site921Acyl-thioester intermediate
Active site3531Proton acceptor
Active site3831Proton acceptor

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.10 Ref.11
Modified residue2001N6-acetyllysine Ref.8
Modified residue2331N6-acetyllysine Ref.8
Modified residue2351N6-acetyllysine Ref.8

Natural variations

Natural variant2111K → R. Ref.5
Corresponds to variant rs25683 [ dbSNP | Ensembl ].
VAR_019686

Experimental info

Sequence conflict1691K → T in AAB30856. Ref.1
Sequence conflict2621V → A in AAB30856. Ref.1
Sequence conflict3751R → G in AAM00223. Ref.2

Secondary structure

................................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BWD1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: E3A8DAFB6F341B18

FASTA39741,351
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
CCDSCCDS5268.1.
PIRJC2378.
RefSeqNP_005882.2. NM_005891.2.
UniGeneHs.571037.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortalQ9BWD1.
SMRQ9BWD1. Positions 4-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106557. 20 interactions.
STRING9606.ENSP00000356015.

PTM databases

PhosphoSiteQ9BWD1.

Polymorphism databases

DMDM52000838.

2D gel databases

OGPQ9BWD1.
REPRODUCTION-2DPAGEIPI00291419.

Proteomic databases

MaxQBQ9BWD1.
PaxDbQ9BWD1.
PeptideAtlasQ9BWD1.
PRIDEQ9BWD1.

Protocols and materials databases

DNASU39.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367048; ENSP00000356015; ENSG00000120437.
GeneID39.
KEGGhsa:39.
UCSCuc010kjy.3. human.

Organism-specific databases

CTD39.
GeneCardsGC06P160153.
HGNCHGNC:94. ACAT2.
HPACAB021106.
HPA025736.
HPA025765.
HPA025811.
MIM100678. gene+phenotype.
neXtProtNX_Q9BWD1.
PharmGKBPA19.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0183.
HOVERGENHBG003112.
InParanoidQ9BWD1.
KOK00626.
OrthoDBEOG7JQBNG.
PhylomeDBQ9BWD1.
TreeFamTF300650.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000120437-MONOMER.

Gene expression databases

ArrayExpressQ9BWD1.
BgeeQ9BWD1.
CleanExHS_ACAT2.
GenevestigatorQ9BWD1.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BWD1.
GeneWikiACAT2.
GenomeRNAi39.
NextBio153.
PROQ9BWD1.
SOURCESearch...

Entry information

Entry nameTHIC_HUMAN
AccessionPrimary (citable) accession number: Q9BWD1
Secondary accession number(s): E1P5B1 expand/collapse secondary AC list , Q16146, Q5TCL7, Q8TDM4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM