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Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene

ACAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei92Acyl-thioester intermediate1
Active sitei353Proton acceptor1
Active sitei383Proton acceptor1

GO - Molecular functioni

  • acetyl-CoA C-acetyltransferase activity Source: BHF-UCL

GO - Biological processi

  • fatty acid beta-oxidation Source: GO_Central
  • lipid metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000120437-MONOMER.
ZFISH:ENSG00000120437-MONOMER.
BRENDAi2.3.1.9. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.

Chemistry databases

SwissLipidsiSLP:000001266.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, cytosolic (EC:2.3.1.9)
Alternative name(s):
Acetyl-CoA transferase-like protein
Cytosolic acetoacetyl-CoA thiolase
Gene namesi
Name:ACAT2
Synonyms:ACTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:94. ACAT2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: GO_Central
  • nucleolus Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi39.
MalaCardsiACAT2.
MIMi100678. gene+phenotype.
OpenTargetsiENSG00000120437.
PharmGKBiPA19.

Polymorphism and mutation databases

BioMutaiACAT2.
DMDMi52000838.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002064091 – 397Acetyl-CoA acetyltransferase, cytosolicAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei200N6-acetyllysineCombined sources1
Modified residuei233N6-acetyllysineCombined sources1
Modified residuei235N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BWD1.
MaxQBiQ9BWD1.
PaxDbiQ9BWD1.
PeptideAtlasiQ9BWD1.
PRIDEiQ9BWD1.

2D gel databases

OGPiQ9BWD1.
REPRODUCTION-2DPAGEIPI00291419.

PTM databases

iPTMnetiQ9BWD1.
PhosphoSitePlusiQ9BWD1.
SwissPalmiQ9BWD1.

Expressioni

Gene expression databases

BgeeiENSG00000120437.
CleanExiHS_ACAT2.
GenevisibleiQ9BWD1. HS.

Organism-specific databases

HPAiCAB021106.
HPA025736.
HPA025765.
HPA025811.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
LNX1Q8TBB13EBI-1047273,EBI-739832
TERF1P542742EBI-1047273,EBI-710997

Protein-protein interaction databases

BioGridi106557. 39 interactors.
IntActiQ9BWD1. 3 interactors.
STRINGi9606.ENSP00000356015.

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 15Combined sources8
Turni24 – 27Combined sources4
Helixi30 – 45Combined sources16
Helixi49 – 51Combined sources3
Beta strandi54 – 58Combined sources5
Helixi69 – 76Combined sources8
Beta strandi85 – 88Combined sources4
Helixi91 – 93Combined sources3
Helixi94 – 107Combined sources14
Beta strandi112 – 122Combined sources11
Beta strandi136 – 138Combined sources3
Helixi145 – 149Combined sources5
Turni154 – 156Combined sources3
Helixi160 – 171Combined sources12
Helixi175 – 194Combined sources20
Turni195 – 201Combined sources7
Beta strandi205 – 209Combined sources5
Beta strandi212 – 216Combined sources5
Helixi228 – 232Combined sources5
Turni240 – 243Combined sources4
Helixi248 – 250Combined sources3
Beta strandi255 – 265Combined sources11
Helixi266 – 271Combined sources6
Beta strandi277 – 287Combined sources11
Helixi290 – 295Combined sources6
Helixi297 – 308Combined sources12
Helixi312 – 314Combined sources3
Beta strandi317 – 320Combined sources4
Helixi325 – 335Combined sources11
Helixi339 – 341Combined sources3
Helixi348 – 351Combined sources4
Turni355 – 357Combined sources3
Helixi358 – 373Combined sources16
Beta strandi377 – 384Combined sources8
Turni385 – 387Combined sources3
Beta strandi388 – 396Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortaliQ9BWD1.
SMRiQ9BWD1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BWD1.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ9BWD1.
KOiK00626.
OMAiMRMGARM.
OrthoDBiEOG091G09C6.
PhylomeDBiQ9BWD1.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BWD1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE
60 70 80 90 100
DVSEVIFGHV LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC
110 120 130 140 150
LAVQSIGIGD SSIVVAGGME NMSKAPHLAY LRTGVKIGEM PLTDSILCDG
160 170 180 190 200
LTDAFHNCHM GITAENVAKK WQVSREDQDK VAVLSQNRTE NAQKAGHFDK
210 220 230 240 250
EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT DGTGTVTPAN
260 270 280 290 300
ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA
310 320 330 340 350
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA
360 370 380 390
LGHPLGASGC RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE
Length:397
Mass (Da):41,351
Last modified:September 13, 2004 - v2
Checksum:iE3A8DAFB6F341B18
GO
Isoform 2 (identifier: Q9BWD1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MNAGSDPVVIVSAARTIIG → MGSHPVLRIWGNRRATAASLGRSGGRLSSPRLLRVVAPTLTFAQTSRC

Note: No experimental confirmation available.
Show »
Length:426
Mass (Da):44,643
Checksum:i5C4390424BB96169
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169K → T in AAB30856 (PubMed:7911016).Curated1
Sequence conflicti262V → A in AAB30856 (PubMed:7911016).Curated1
Sequence conflicti375R → G in AAM00223 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019686211K → R.1 PublicationCorresponds to variant rs25683dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562171 – 19MNAGS…RTIIG → MGSHPVLRIWGNRRATAASL GRSGGRLSSPRLLRVVAPTL TFAQTSRC in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AK294273 mRNA. Translation: BAH11719.1.
AL135914 Genomic DNA. Translation: CAI21850.1.
CH471051 Genomic DNA. Translation: EAW47619.1.
CH471051 Genomic DNA. Translation: EAW47620.1.
BC000408 mRNA. Translation: AAH00408.1.
CCDSiCCDS5268.1. [Q9BWD1-1]
PIRiJC2378.
RefSeqiNP_001290182.1. NM_001303253.1. [Q9BWD1-2]
NP_005882.2. NM_005891.2. [Q9BWD1-1]
UniGeneiHs.571037.

Genome annotation databases

EnsembliENST00000367048; ENSP00000356015; ENSG00000120437. [Q9BWD1-1]
GeneIDi39.
KEGGihsa:39.
UCSCiuc010kjy.4. human. [Q9BWD1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70154 mRNA. Translation: AAB30856.1.
AF356877 mRNA. Translation: AAM00223.1.
AK294273 mRNA. Translation: BAH11719.1.
AL135914 Genomic DNA. Translation: CAI21850.1.
CH471051 Genomic DNA. Translation: EAW47619.1.
CH471051 Genomic DNA. Translation: EAW47620.1.
BC000408 mRNA. Translation: AAH00408.1.
CCDSiCCDS5268.1. [Q9BWD1-1]
PIRiJC2378.
RefSeqiNP_001290182.1. NM_001303253.1. [Q9BWD1-2]
NP_005882.2. NM_005891.2. [Q9BWD1-1]
UniGeneiHs.571037.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WL4X-ray1.55A1-397[»]
1WL5X-ray2.26A1-397[»]
ProteinModelPortaliQ9BWD1.
SMRiQ9BWD1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106557. 39 interactors.
IntActiQ9BWD1. 3 interactors.
STRINGi9606.ENSP00000356015.

Chemistry databases

SwissLipidsiSLP:000001266.

PTM databases

iPTMnetiQ9BWD1.
PhosphoSitePlusiQ9BWD1.
SwissPalmiQ9BWD1.

Polymorphism and mutation databases

BioMutaiACAT2.
DMDMi52000838.

2D gel databases

OGPiQ9BWD1.
REPRODUCTION-2DPAGEIPI00291419.

Proteomic databases

EPDiQ9BWD1.
MaxQBiQ9BWD1.
PaxDbiQ9BWD1.
PeptideAtlasiQ9BWD1.
PRIDEiQ9BWD1.

Protocols and materials databases

DNASUi39.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367048; ENSP00000356015; ENSG00000120437. [Q9BWD1-1]
GeneIDi39.
KEGGihsa:39.
UCSCiuc010kjy.4. human. [Q9BWD1-1]

Organism-specific databases

CTDi39.
DisGeNETi39.
GeneCardsiACAT2.
HGNCiHGNC:94. ACAT2.
HPAiCAB021106.
HPA025736.
HPA025765.
HPA025811.
MalaCardsiACAT2.
MIMi100678. gene+phenotype.
neXtProtiNX_Q9BWD1.
OpenTargetsiENSG00000120437.
PharmGKBiPA19.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ9BWD1.
KOiK00626.
OMAiMRMGARM.
OrthoDBiEOG091G09C6.
PhylomeDBiQ9BWD1.
TreeFamiTF300650.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000120437-MONOMER.
ZFISH:ENSG00000120437-MONOMER.
BRENDAi2.3.1.9. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSiACAT2. human.
EvolutionaryTraceiQ9BWD1.
GeneWikiiACAT2.
GenomeRNAii39.
PROiQ9BWD1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120437.
CleanExiHS_ACAT2.
GenevisibleiQ9BWD1. HS.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIC_HUMAN
AccessioniPrimary (citable) accession number: Q9BWD1
Secondary accession number(s): B7Z233
, E1P5B1, Q16146, Q5TCL7, Q8TDM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 2, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.