CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007595
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 3-ketoacyl-CoA thiolase, mitochondrial 
Protein Synonyms/Alias
 Acetyl-CoA acyltransferase; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1 
Gene Name
 ACAA2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25GAYGGLLKDFTATDLacetylation[1, 2]
38DLSEFAAKAALSAGKacetylation[3]
81GLRVGIPKETPALTIacetylation[1]
137RNVRFGTKLGSDIKLacetylation[1]
181ISREECDKYALQSQQacetylation[1]
234TTLEQLQKLPPVFKKacetylation[2]
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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Abolishes BNIP3-mediated apoptosis and mitochondrial damage. 
Sequence Annotation
 ACT_SITE 92 92 Acyl-thioester intermediate (By
 ACT_SITE 352 352 Proton acceptor (By similarity).
 ACT_SITE 382 382 Proton acceptor (By similarity).
 MOD_RES 119 119 Phosphothreonine.
 MOD_RES 121 121 Phosphoserine.
 MOD_RES 127 127 Phosphotyrosine.
 MOD_RES 137 137 N6-acetyllysine (By similarity).
 MOD_RES 270 270 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Fatty acid metabolism; Lipid metabolism; Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 397 AA 
Protein Sequence
MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET VDSVIMGNVL 60
QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV NGCQEICVKE AEVVLCGGTE 120
SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV SLTDQHVQLP MAMTAENLAV KHKISREECD 180
KYALQSQQRW KAANDAGYFN DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK 240
KDGTVTAGNA SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI 300
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL GHPLGGSGSR 360
ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA 397 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0003988; F:acetyl-CoA C-acyltransferase activity; NAS:UniProtKB.
 GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
 GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization; IDA:UniProtKB. 
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. 
Pfam
 PF02803; Thiolase_C
 PF00108; Thiolase_N 
SMART
  
PROSITE
 PS00098; THIOLASE_1
 PS00737; THIOLASE_2
 PS00099; THIOLASE_3 
PRINTS