CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018130
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 3-ketoacyl-CoA thiolase B, peroxisomal 
Protein Synonyms/Alias
 Acetyl-CoA acyltransferase B; Beta-ketothiolase B; Peroxisomal 3-oxoacyl-CoA thiolase B 
Gene Name
 Acaa1b 
Gene Synonyms/Alias
 Acaa1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
79VLQDVKLKPEQLGDIubiquitination[1]
173SRLLENEKARDCLIPacetylation[2, 3, 4]
198RFGVSRQKQDAFALAacetylation[4]
198RFGVSRQKQDAFALAubiquitination[1]
209FALASQQKAASAQSRacetylation[3]
209FALASQQKAASAQSRubiquitination[1]
234TTTVLNDKGDKKTITacetylation[2, 4]
234TTTVLNDKGDKKTITubiquitination[1]
237VLNDKGDKKTITVSQacetylation[2, 3, 4]
237VLNDKGDKKTITVSQubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 
Functional Description
  
Sequence Annotation
 ACT_SITE 123 123 Acyl-thioester intermediate (By
 ACT_SITE 377 377 Proton acceptor (By similarity).
 ACT_SITE 408 408 Proton acceptor (By similarity).  
Keyword
 Acyltransferase; Complete proteome; Fatty acid metabolism; Lipid metabolism; Peroxisome; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 424 AA 
Protein Sequence
MHRLQVVLGH LAGRPESSSA LQAAPCSAGF LQASASDVVV VHGRRTPIGR ASRGCFKDTT 60
PDELLSAVLT AVLQDVKLKP EQLGDISVGN VLQPGAGAIM ARIAQFLSGI PETVPLSTVN 120
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMTLSQRGN HGNISSRLLE NEKARDCLIP 180
MGITSENVAE RFGVSRQKQD AFALASQQKA ASAQSRGCFH AEIVPVTTTV LNDKGDKKTI 240
TVSQDEGVRP STTMQGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI 300
LGVLRSYAVV GVPPDVMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS QAVYCVEKLG 360
IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR AYGVVSMCIG TGMGAAAVFE 420
YPGN 424 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
 GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:EC.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway. 
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