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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to hypoxia Source: BHF-UCL
  2. cholesterol biosynthetic process Source: UniProtKB
  3. fatty acid metabolic process Source: UniProtKB-UniPathway
  4. negative regulation of mitochondrial membrane permeability involved in apoptotic process Source: BHF-UCL
  5. 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.
UniPathwayiUPA00199.

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
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:83. ACAA2.

Subcellular locationi

Mitochondrion 1 Publication
Note: Colocalizes with BNIP3 in the mitochondria.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000223299Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleavedAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251N6-acetyllysine; alternateBy similarity
Modified residuei25 – 251N6-succinyllysine; alternateBy similarity
Modified residuei45 – 451N6-succinyllysineBy similarity
Modified residuei119 – 1191Phosphothreonine1 Publication
Modified residuei121 – 1211Phosphoserine1 Publication
Modified residuei127 – 1271Phosphotyrosine1 Publication
Modified residuei137 – 1371N6-acetyllysine; alternateBy similarity
Modified residuei137 – 1371N6-succinyllysine; alternateBy similarity
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei143 – 1431N6-acetyllysine; alternateBy similarity
Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
Modified residuei171 – 1711N6-acetyllysine; alternateBy similarity
Modified residuei171 – 1711N6-succinyllysine; alternateBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
Modified residuei209 – 2091N6-succinyllysine; alternateBy similarity
Modified residuei211 – 2111N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-succinyllysineBy similarity
Modified residuei214 – 2141N6-succinyllysineBy similarity
Modified residuei234 – 2341N6-acetyllysine; alternateBy similarity
Modified residuei234 – 2341N6-succinyllysine; alternateBy similarity
Modified residuei240 – 2401N6-succinyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-acetyllysineBy similarity
Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
Modified residuei312 – 3121N6-acetyllysine; alternateBy similarity
Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei340 – 3401N6-acetyllysineBy similarity
Modified residuei375 – 3751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42765.
PaxDbiP42765.
PeptideAtlasiP42765.
PRIDEiP42765.

2D gel databases

REPRODUCTION-2DPAGEIPI00001539.
UCD-2DPAGEP42765.

PTM databases

PhosphoSiteiP42765.

Expressioni

Gene expression databases

BgeeiP42765.
ExpressionAtlasiP42765. baseline and differential.
GenevestigatoriP42765.

Organism-specific databases

HPAiHPA042303.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3.1 Publication

Protein-protein interaction databases

BioGridi115713. 25 interactions.
IntActiP42765. 2 interactions.
MINTiMINT-5005997.
STRINGi9606.ENSP00000285093.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Turni23 – 264Combined sources
Helixi29 – 4315Combined sources
Helixi48 – 503Combined sources
Beta strandi53 – 575Combined sources
Helixi66 – 683Combined sources
Helixi69 – 768Combined sources
Beta strandi85 – 895Combined sources
Helixi91 – 933Combined sources
Helixi94 – 10714Combined sources
Beta strandi112 – 12211Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi142 – 1465Combined sources
Helixi147 – 1515Combined sources
Turni155 – 1584Combined sources
Helixi161 – 17212Combined sources
Helixi176 – 19621Combined sources
Turni197 – 2026Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi215 – 2173Combined sources
Helixi229 – 2346Combined sources
Beta strandi238 – 2403Combined sources
Turni247 – 2493Combined sources
Beta strandi254 – 26411Combined sources
Helixi265 – 2717Combined sources
Beta strandi277 – 28610Combined sources
Helixi289 – 2946Combined sources
Helixi296 – 30712Combined sources
Helixi311 – 3133Combined sources
Beta strandi315 – 3195Combined sources
Helixi324 – 33411Combined sources
Beta strandi340 – 3423Combined sources
Helixi347 – 3504Combined sources
Turni354 – 3563Combined sources
Helixi357 – 37216Combined sources
Beta strandi375 – 3839Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2JX-ray2.00A/B/C/D1-397[»]
4C2KX-ray2.00A/B/C/D1-397[»]
ProteinModelPortaliP42765.
SMRiP42765. Positions 1-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP42765.
KOiK07508.
OMAiHVSGCDP.
OrthoDBiEOG7JQBNG.
PhylomeDBiP42765.
TreeFamiTF105696.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
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 3, 2005 - v2
Checksum:i380CC8262ACF6D01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → R in BAA03800 (PubMed:8241273).Curated
Sequence conflicti169 – 1691A → T in BAA03800 (PubMed:8241273).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171M → V.
Corresponds to variant rs11549285 [ dbSNP | Ensembl ].
VAR_052577

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.4. human.

Polymorphism databases

DMDMi57015371.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2JX-ray2.00A/B/C/D1-397[»]
4C2KX-ray2.00A/B/C/D1-397[»]
ProteinModelPortaliP42765.
SMRiP42765. Positions 1-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115713. 25 interactions.
IntActiP42765. 2 interactions.
MINTiMINT-5005997.
STRINGi9606.ENSP00000285093.

PTM databases

PhosphoSiteiP42765.

Polymorphism databases

DMDMi57015371.

2D gel databases

REPRODUCTION-2DPAGEIPI00001539.
UCD-2DPAGEP42765.

Proteomic databases

MaxQBiP42765.
PaxDbiP42765.
PeptideAtlasiP42765.
PRIDEiP42765.

Protocols and materials databases

DNASUi10449.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285093; ENSP00000285093; ENSG00000167315.
GeneIDi10449.
KEGGihsa:10449.
UCSCiuc002ldw.4. human.

Organism-specific databases

CTDi10449.
GeneCardsiGC18M047309.
H-InvDBHIX0014445.
HGNCiHGNC:83. ACAA2.
HPAiHPA042303.
MIMi604770. gene.
neXtProtiNX_P42765.
PharmGKBiPA24420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP42765.
KOiK07508.
OMAiHVSGCDP.
OrthoDBiEOG7JQBNG.
PhylomeDBiP42765.
TreeFamiTF105696.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:HS09539-MONOMER.

Miscellaneous databases

ChiTaRSiACAA2. human.
GeneWikiiACAA2.
GenomeRNAii10449.
NextBioi39605.
PROiP42765.
SOURCEiSearch...

Gene expression databases

BgeeiP42765.
ExpressionAtlasiP42765. baseline and differential.
GenevestigatoriP42765.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase."
    Abe H., Ohtake A., Yamamoto S., Satoh Y., Takayanagi M., Amaya Y., Takiguchi M., Sakuraba H., Suzuki Y., Mori M., Niimi H.
    Biochim. Biophys. Acta 1216:304-306(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-25; 46-71 AND 341-360.
    Tissue: Adipocyte.
  4. "Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic effects of BNIP3 in two human cell lines."
    Cao W., Liu N., Tang S., Bao L., Shen L., Yuan H., Zhao X., Lu H.
    Biochim. Biophys. Acta 1780:873-880(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BNIP3.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-121 AND TYR-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHIM_HUMAN
AccessioniPrimary (citable) accession number: P42765
Secondary accession number(s): Q9BUT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: January 3, 2005
Last modified: March 3, 2015
This is version 139 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

External Data

Dasty 3

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 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.