CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008193
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-coenzyme A thioesterase 2, mitochondrial 
Protein Synonyms/Alias
 Acyl-CoA thioesterase 2; Acyl-coenzyme A thioester hydrolase 2a; CTE-Ia; Long-chain acyl-CoA thioesterase 2; ZAP128 
Gene Name
 ACOT2 
Gene Synonyms/Alias
 PTE2; PTE2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
104RASLRDEKGALFQAHacetylation[1]
348RNRIKVTKDGYADIVubiquitination[2, 3, 4]
368PLEGPDQKSFIPVERubiquitination[3, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs. 
Sequence Annotation
 MOTIF 481 483 Microbody targeting signal (Potential).
 ACT_SITE 294 294 Charge relay system (By similarity).
 ACT_SITE 388 388 Charge relay system (By similarity).
 ACT_SITE 422 422 Charge relay system (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Hydrolase; Mitochondrion; Polymorphism; Reference proteome; Serine esterase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL RQVGQIIRVP 60
ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL RDEKGALFQA HARYRADTLG 120
ELDLERAPAL GGSFAGLEPM GLLWALEPEK PLVRLVKRDV RTPLAVELEV LDGHDPDPGR 180
LLCQTRHERY FLPPGVRREP VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL 240
AGKGFAVMAL AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC 300
LSMASFLKGI TAAVVINGSV ANVGGTLHYK GETLPPVGVN RNRIKVTKDG YADIVDVLNS 360
PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA CKRLQAHGRR KPQIICYPET 420
GHYIEPPYFP LCRASLHALV GSPIIWGGEP RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP 480
SKV 483 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HGNC.
 GO:0047617; F:acyl-CoA hydrolase activity; IDA:HGNC.
 GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
 GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:EC.
 GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC.
 GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC.
 GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC. 
Interpro
 IPR016662; Acyl-CoA_thioEstase_long-chain.
 IPR014940; BAAT_C.
 IPR006862; Thio_Ohase/aa_AcTrfase. 
Pfam
 PF08840; BAAT_C
 PF04775; Bile_Hydr_Trans 
SMART
  
PROSITE
  
PRINTS