3-ketoacyl-CoA thiolase, mitochondrial

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Reviewed, UniProtKB/Swiss-Prot P42765 (THIM_HUMAN)

Last modified February 9, 2010. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase, mitochondrial
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Mitochondrial 3-oxoacyl-CoA thiolase
    T1

Gene names

Name:

ACAA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the thiolase family.

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Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Ref.1 Non-traceable author statement. Source: UniProtKB fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetyl-CoA C-acyltransferase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

3-ketoacyl-CoA thiolase, mitochondrial

PRO_0000223299

Transit peptide

1 – 16

Mitochondrion; not cleaved

Sites

Active site

Acyl-thioester intermediate By similarity

Active site

352

Proton acceptor By similarity

Active site

382

Proton acceptor By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.6

Modified residue

N6-acetyllysine Ref.6

Modified residue

119

Phosphothreonine Ref.4

Modified residue

121

Phosphoserine Ref.4

Modified residue

127

Phosphotyrosine Ref.4

Modified residue

137

N6-acetyllysine Ref.6

Modified residue

181

N6-acetyllysine Ref.6

Modified residue

270

N6-acetyllysine By similarity

Natural variations

Natural variant

217

M → V: dbSNP rs11549285.

VAR_052577

Experimental info

Sequence conflict

A → R in BAA03800. Ref.1

Sequence conflict

169

A → T in BAA03800. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P42765-1 [UniParc].

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

397

41,924

        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

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References

	« Hide 'large scale' referencesShow '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: 8241273] [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: 15489334] [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: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-25; 46-71 AND 341-360. Tissue: Adipocyte.
[4]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-121 AND TYR-127, MASS SPECTROMETRY.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-81; LYS-137 AND LYS-181, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	D16294 mRNA. Translation: BAA03800.1. BC001918 mRNA. Translation: AAH01918.1.
IPI	IPI00001539.
PIR	S43440.
RefSeq	NP_006102.2.
UniGene	Hs.200136
3D structure databases
SMR	P42765. Positions 6-395.
ModBase	Search...
Protein-protein interaction databases
STRING	P42765.
PTM databases
PhosphoSite	P42765.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00001539.
Proteomic databases
PeptideAtlas	P42765.
PRIDE	P42765.
Genome annotation databases
Ensembl	ENST00000285093; ENSP00000285093; ENSG00000167315; Homo sapiens. [Genome view]
GeneID	10449.
KEGG	hsa:10449.
NMPDR	fig\|9606.3.peg.15023.
UCSC	uc002ldw.2. human.
Organism-specific databases
CTD	10449.
GeneCards	GC18M045563.
HGNC	HGNC:83. ACAA2.
MIM	604770. gene.
PharmGKB	PA24420.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06378.
HOGENOM	HBG370930.
HOVERGEN	P42765.
OrthoDB	EOG9C2KW9.
PhylomeDB	P42765.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14817.
BRENDA	2.3.1.16. 247.
Gene expression databases
ArrayExpress	P42765.
Bgee	P42765.
Genevestigator	P42765.
GermOnline	ENSG00000167315. Homo sapiens.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	39605.
SOURCE	Search...

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Entry information

Entry name

THIM_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents