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Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

ACAA2

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

Functioni

Abolishes BNIP3-mediated apoptosis and mitochondrial damage.1 Publication

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei92Acyl-thioester intermediateBy similarity1
Active sitei352Proton acceptorPROSITE-ProRule annotation1
Active sitei382Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • acetyl-CoA C-acyltransferase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to hypoxia Source: BHF-UCL
  • cholesterol biosynthetic process Source: UniProtKB
  • fatty acid beta-oxidation Source: GO_Central
  • negative regulation of mitochondrial membrane permeability involved in apoptotic process Source: BHF-UCL
  • negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS09539-MONOMER.
ZFISH:HS09539-MONOMER.
ReactomeiR-HSA-77289. Mitochondrial Fatty Acid Beta-Oxidation.
UniPathwayiUPA00199.

Chemistry databases

SwissLipidsiSLP:000001273.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase, mitochondrial (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Mitochondrial 3-oxoacyl-CoA thiolase
T1
Gene namesi
Name:ACAA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:83. ACAA2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi10449.
OpenTargetsiENSG00000167315.
PharmGKBiPA24420.

Polymorphism and mutation databases

BioMutaiACAA2.
DMDMi57015371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002232991 – 3973-ketoacyl-CoA thiolase, mitochondrialAdd BLAST397
Transit peptidei1 – 16Mitochondrion; not cleavedAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25N6-acetyllysine; alternateBy similarity1
Modified residuei25N6-succinyllysine; alternateBy similarity1
Modified residuei45N6-succinyllysineBy similarity1
Modified residuei119PhosphothreonineCombined sources1
Modified residuei121PhosphoserineCombined sources1
Modified residuei127PhosphotyrosineCombined sources1
Modified residuei136PhosphothreonineBy similarity1
Modified residuei137N6-acetyllysine; alternateBy similarity1
Modified residuei137N6-succinyllysine; alternateBy similarity1
Modified residuei140PhosphoserineCombined sources1
Modified residuei143N6-acetyllysine; alternateBy similarity1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysine; alternateBy similarity1
Modified residuei171N6-succinyllysine; alternateBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1
Modified residuei211N6-succinyllysineBy similarity1
Modified residuei212N6-succinyllysineBy similarity1
Modified residuei214N6-succinyllysineBy similarity1
Modified residuei234N6-acetyllysine; alternateBy similarity1
Modified residuei234N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-succinyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei269N6-acetyllysineBy similarity1
Modified residuei270N6-acetyllysineBy similarity1
Modified residuei305N6-acetyllysine; alternateBy similarity1
Modified residuei305N6-succinyllysine; alternateBy similarity1
Modified residuei310PhosphoserineBy similarity1
Modified residuei312N6-acetyllysine; alternateBy similarity1
Modified residuei312N6-succinyllysine; alternateBy similarity1
Modified residuei333PhosphoserineCombined sources1
Modified residuei340N6-acetyllysineBy similarity1
Modified residuei375N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP42765.
MaxQBiP42765.
PaxDbiP42765.
PeptideAtlasiP42765.
PRIDEiP42765.
TopDownProteomicsiP42765.

2D gel databases

REPRODUCTION-2DPAGEIPI00001539.
UCD-2DPAGEP42765.

PTM databases

iPTMnetiP42765.
PhosphoSitePlusiP42765.
SwissPalmiP42765.

Expressioni

Gene expression databases

BgeeiENSG00000167315.
ExpressionAtlasiP42765. baseline and differential.
GenevisibleiP42765. HS.

Organism-specific databases

HPAiHPA042303.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3.1 Publication

Protein-protein interaction databases

BioGridi115713. 54 interactors.
IntActiP42765. 4 interactors.
MINTiMINT-5005997.
STRINGi9606.ENSP00000285093.

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Turni23 – 26Combined sources4
Helixi29 – 43Combined sources15
Helixi48 – 50Combined sources3
Beta strandi53 – 57Combined sources5
Helixi66 – 68Combined sources3
Helixi69 – 76Combined sources8
Beta strandi85 – 89Combined sources5
Helixi91 – 93Combined sources3
Helixi94 – 107Combined sources14
Beta strandi112 – 122Combined sources11
Beta strandi127 – 129Combined sources3
Beta strandi142 – 146Combined sources5
Helixi147 – 151Combined sources5
Turni155 – 158Combined sources4
Helixi161 – 172Combined sources12
Helixi176 – 196Combined sources21
Turni197 – 202Combined sources6
Beta strandi206 – 208Combined sources3
Beta strandi215 – 217Combined sources3
Helixi229 – 234Combined sources6
Beta strandi238 – 240Combined sources3
Turni247 – 249Combined sources3
Beta strandi254 – 264Combined sources11
Helixi265 – 271Combined sources7
Beta strandi277 – 286Combined sources10
Helixi289 – 294Combined sources6
Helixi296 – 307Combined sources12
Helixi311 – 313Combined sources3
Beta strandi315 – 319Combined sources5
Helixi324 – 334Combined sources11
Beta strandi340 – 342Combined sources3
Helixi347 – 350Combined sources4
Turni354 – 356Combined sources3
Helixi357 – 372Combined sources16
Beta strandi375 – 383Combined sources9
Turni384 – 386Combined sources3
Beta strandi387 – 395Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2JX-ray2.00A/B/C/D1-397[»]
4C2KX-ray2.00A/B/C/D1-397[»]
ProteinModelPortaliP42765.
SMRiP42765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP42765.
KOiK07508.
OMAiHVSGCDP.
OrthoDBiEOG091G09C6.
PhylomeDBiP42765.
TreeFamiTF105696.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
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.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42765-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET
60 70 80 90 100
VDSVIMGNVL QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV
110 120 130 140 150
NGCQEICVKE AEVVLCGGTE SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV
160 170 180 190 200
SLTDQHVQLP MAMTAENLAV KHKISREECD KYALQSQQRW KAANDAGYFN
210 220 230 240 250
DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK KDGTVTAGNA
260 270 280 290 300
SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI
310 320 330 340 350
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL
360 370 380 390
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA
Length:397
Mass (Da):41,924
Last modified:January 4, 2005 - v2
Checksum:i380CC8262ACF6D01
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → R in BAA03800 (PubMed:8241273).Curated1
Sequence conflicti169A → T in BAA03800 (PubMed:8241273).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052577217M → V.Corresponds to variant rs11549285dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16294 mRNA. Translation: BAA03800.1.
BC001918 mRNA. Translation: AAH01918.1.
CCDSiCCDS11939.1.
PIRiS43440.
RefSeqiNP_006102.2. NM_006111.2.
UniGeneiHs.200136.

Genome annotation databases

EnsembliENST00000285093; ENSP00000285093; ENSG00000167315.
GeneIDi10449.
KEGGihsa:10449.
UCSCiuc002ldw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16294 mRNA. Translation: BAA03800.1.
BC001918 mRNA. Translation: AAH01918.1.
CCDSiCCDS11939.1.
PIRiS43440.
RefSeqiNP_006102.2. NM_006111.2.
UniGeneiHs.200136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4C2JX-ray2.00A/B/C/D1-397[»]
4C2KX-ray2.00A/B/C/D1-397[»]
ProteinModelPortaliP42765.
SMRiP42765.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115713. 54 interactors.
IntActiP42765. 4 interactors.
MINTiMINT-5005997.
STRINGi9606.ENSP00000285093.

Chemistry databases

SwissLipidsiSLP:000001273.

PTM databases

iPTMnetiP42765.
PhosphoSitePlusiP42765.
SwissPalmiP42765.

Polymorphism and mutation databases

BioMutaiACAA2.
DMDMi57015371.

2D gel databases

REPRODUCTION-2DPAGEIPI00001539.
UCD-2DPAGEP42765.

Proteomic databases

EPDiP42765.
MaxQBiP42765.
PaxDbiP42765.
PeptideAtlasiP42765.
PRIDEiP42765.
TopDownProteomicsiP42765.

Protocols and materials databases

DNASUi10449.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285093; ENSP00000285093; ENSG00000167315.
GeneIDi10449.
KEGGihsa:10449.
UCSCiuc002ldw.5. human.

Organism-specific databases

CTDi10449.
DisGeNETi10449.
GeneCardsiACAA2.
H-InvDBHIX0014445.
HGNCiHGNC:83. ACAA2.
HPAiHPA042303.
MIMi604770. gene.
neXtProtiNX_P42765.
OpenTargetsiENSG00000167315.
PharmGKBiPA24420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP42765.
KOiK07508.
OMAiHVSGCDP.
OrthoDBiEOG091G09C6.
PhylomeDBiP42765.
TreeFamiTF105696.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:HS09539-MONOMER.
ZFISH:HS09539-MONOMER.
ReactomeiR-HSA-77289. Mitochondrial Fatty Acid Beta-Oxidation.

Miscellaneous databases

ChiTaRSiACAA2. human.
GeneWikiiACAA2.
GenomeRNAii10449.
PROiP42765.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167315.
ExpressionAtlasiP42765. baseline and differential.
GenevisibleiP42765. HS.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
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.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIM_HUMAN
AccessioniPrimary (citable) accession number: P42765
Secondary accession number(s): Q9BUT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 4, 2005
Last modified: November 30, 2016
This is version 156 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 18
    Human chromosome 18: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.