CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020271
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-CoA acetyltransferase, cytosolic 
Protein Synonyms/Alias
 Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase 
Gene Name
 ACAT2 
Gene Synonyms/Alias
 ACTL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39DLGSTVIKEVLKRATubiquitination[1]
136AYLRTGVKIGEMPLTubiquitination[1]
170TAENVAKKWQVSREDubiquitination[1]
180VSREDQDKVAVLSQNubiquitination[1]
200QKAGHFDKEIVPVLVacetylation[2]
200QKAGHFDKEIVPVLVubiquitination[1]
211PVLVSTRKGLIEVKTubiquitination[1]
217RKGLIEVKTDEFPRHubiquitination[1]
233SNIEAMSKLKPYFLTacetylation[2]
233SNIEAMSKLKPYFLTubiquitination[1]
235IEAMSKLKPYFLTDGacetylation[2]
235IEAMSKLKPYFLTDGubiquitination[1, 3]
265AAAVVLMKKSEADKRubiquitination[1]
266AAVVLMKKSEADKRGubiquitination[1]
302IGPIPAIKQAVTKAGubiquitination[4]
341ELGLNPEKVNIEGGAubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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]
 [3] 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]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
  
Sequence Annotation
 ACT_SITE 92 92 Acyl-thioester intermediate.
 ACT_SITE 353 353 Proton acceptor.
 ACT_SITE 383 383 Proton acceptor.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 200 200 N6-acetyllysine.
 MOD_RES 233 233 N6-acetyllysine.
 MOD_RES 235 235 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Acyltransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 397 AA 
Protein Sequence
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV 60
LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME 120
NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK 180
VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT 240
DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA 300
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC 360
RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE 397 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
 GO:0006629; P:lipid metabolic process; IC:BHF-UCL. 
Interpro
 IPR002155; Thiolase.
 IPR016039; Thiolase-like.
 IPR016038; Thiolase-like_subgr.
 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