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P42765 (THIM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ACAA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Abolishes BNIP3-mediated apoptosis and mitochondrial damage. Ref.4

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homotetramer. Interacts with BNIP3. Ref.4

Subcellular location

Mitochondrion. Note: Colocalizes with BNIP3 in the mitochondria. Ref.4

Sequence similarities

Belongs to the thiolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3973973-ketoacyl-CoA thiolase, mitochondrial
PRO_0000223299
Transit peptide1 – 1616Mitochondrion; not cleaved

Sites

Active site921Acyl-thioester intermediate By similarity
Active site3521Proton acceptor By similarity
Active site3821Proton acceptor By similarity

Amino acid modifications

Modified residue1191Phosphothreonine Ref.5
Modified residue1211Phosphoserine Ref.5
Modified residue1271Phosphotyrosine Ref.5
Modified residue1371N6-acetyllysine By similarity
Modified residue2701N6-acetyllysine By similarity

Natural variations

Natural variant2171M → V.
Corresponds to variant rs11549285 [ dbSNP | Ensembl ].
VAR_052577

Experimental info

Sequence conflict21A → R in BAA03800. Ref.1
Sequence conflict1691A → T in BAA03800. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42765 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 380CC8262ACF6D01

FASTA39741,924
        10         20         30         40         50         60 
MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET VDSVIMGNVL 

        70         80         90        100        110        120 
QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV NGCQEICVKE AEVVLCGGTE 

       130        140        150        160        170        180 
SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV SLTDQHVQLP MAMTAENLAV KHKISREECD 

       190        200        210        220        230        240 
KYALQSQQRW KAANDAGYFN DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK 

       250        260        270        280        290        300 
KDGTVTAGNA SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI 

       310        320        330        340        350        360 
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL GHPLGGSGSR 

       370        380        390 
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-121 AND TYR-127, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16294 mRNA. Translation: BAA03800.1.
BC001918 mRNA. Translation: AAH01918.1.
IPIIPI00001539.
PIRS43440.
RefSeqNP_006102.2. NM_006111.2.
UniGeneHs.200136.

3D structure databases

ProteinModelPortalP42765.
ModBaseSearch...

Protein-protein interaction databases

IntActP42765. 2 interactions.
STRING9606.ENSP00000285093.

PTM databases

PhosphoSiteP42765.

Polymorphism databases

DMDM57015371.

2D gel databases

REPRODUCTION-2DPAGEIPI00001539.
UCD-2DPAGEP42765.

Proteomic databases

PaxDbP42765.
PeptideAtlasP42765.
PRIDEP42765.

Protocols and materials databases

DNASU10449.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285093; ENSP00000285093; ENSG00000167315.
GeneID10449.
KEGGhsa:10449.
UCSCuc002ldw.4. human.

Organism-specific databases

CTD10449.
GeneCardsGC18M047309.
H-InvDBHIX0014445.
HGNCHGNC:83. ACAA2.
HPAHPA042303.
MIM604770. gene.
neXtProtNX_P42765.
PharmGKBPA24420.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000012238.
HOVERGENHBG003112.
KOK07508.
OMAMSQSPYC.
OrthoDBEOG4H19VX.
PhylomeDBP42765.

Enzyme and pathway databases

BioCycMetaCyc:HS09539-MONOMER.
UniPathwayUPA00199.

Gene expression databases

BgeeP42765.
GenevestigatorP42765.
GermOnlineENSG00000167315. Homo sapiens.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. 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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACAA2. human.
GenomeRNAi10449.
NextBio39605.
SOURCESearch...

Entry information

Entry nameTHIM_HUMAN
AccessionPrimary (citable) accession number: P42765
Secondary accession number(s): Q9BUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 120 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

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents