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P42765

- THIM_HUMAN

UniProt

P42765 - THIM_HUMAN

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Protein
3-ketoacyl-CoA thiolase, mitochondrial
Gene
ACAA2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 intermediate By similarity
Active sitei352 – 3521Proton acceptor By similarity
Active sitei382 – 3821Proton acceptor By similarity

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. protein 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: Chromosome 18

Organism-specific databases

HGNCiHGNC:83. ACAA2.

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  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, mitochondrial
PRO_0000223299Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleaved
Add
BLAST

Amino acid modifications

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

ArrayExpressiP42765.
BgeeiP42765.
GenevestigatoriP42765.

Organism-specific databases

HPAiHPA042303.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3.1 Publication

Protein-protein interaction databases

BioGridi115713. 21 interactions.
IntActiP42765. 2 interactions.
MINTiMINT-5005997.
STRINGi9606.ENSP00000285093.

Structurei

3D structure databases

ProteinModelPortaliP42765.
SMRiP42765. Positions 4-393.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
KOiK07508.
OMAiQTLACAD.
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

MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET    50
VDSVIMGNVL QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV 100
NGCQEICVKE AEVVLCGGTE SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV 150
SLTDQHVQLP MAMTAENLAV KHKISREECD KYALQSQQRW KAANDAGYFN 200
DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK KDGTVTAGNA 250
SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI 300
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL 350
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA 397
Length:397
Mass (Da):41,924
Last modified:January 4, 2005 - v2
Checksum:i380CC8262ACF6D01
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → R in BAA03800. 1 Publication
Sequence conflicti169 – 1691A → T in BAA03800. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D16294 mRNA. Translation: BAA03800.1 .
BC001918 mRNA. Translation: AAH01918.1 .
CCDSi CCDS11939.1.
PIRi S43440.
RefSeqi NP_006102.2. NM_006111.2.
UniGenei Hs.200136.

3D structure databases

ProteinModelPortali P42765.
SMRi P42765. Positions 4-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115713. 21 interactions.
IntActi P42765. 2 interactions.
MINTi MINT-5005997.
STRINGi 9606.ENSP00000285093.

PTM databases

PhosphoSitei P42765.

Polymorphism databases

DMDMi 57015371.

2D gel databases

REPRODUCTION-2DPAGE IPI00001539.
UCD-2DPAGE P42765.

Proteomic databases

MaxQBi P42765.
PaxDbi P42765.
PeptideAtlasi P42765.
PRIDEi P42765.

Protocols and materials databases

DNASUi 10449.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285093 ; ENSP00000285093 ; ENSG00000167315 .
GeneIDi 10449.
KEGGi hsa:10449.
UCSCi uc002ldw.4. human.

Organism-specific databases

CTDi 10449.
GeneCardsi GC18M047309.
H-InvDB HIX0014445.
HGNCi HGNC:83. ACAA2.
HPAi HPA042303.
MIMi 604770. gene.
neXtProti NX_P42765.
PharmGKBi PA24420.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0183.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
KOi K07508.
OMAi QTLACAD.
OrthoDBi EOG7JQBNG.
PhylomeDBi P42765.
TreeFami TF105696.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci MetaCyc:HS09539-MONOMER.

Miscellaneous databases

ChiTaRSi ACAA2. human.
GeneWikii ACAA2.
GenomeRNAii 10449.
NextBioi 39605.
PROi P42765.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42765.
Bgeei P42765.
Genevestigatori P42765.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. 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 ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(2004) [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(2004) [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(2008) [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].

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: September 3, 2014
This is version 134 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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