CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031543
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 3-ketoacyl-CoA thiolase 
Protein Synonyms/Alias
 cDNA FLJ56214, highly similar to Trifunctional enzyme subunit beta, mitochondrial 
Gene Name
 HADHB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50LLSGTSYKDLMPHDLacetylation[1, 2, 3]
50LLSGTSYKDLMPHDLubiquitination[4]
166KLMLDLNKAKSMGQRacetylation[1, 2]
179QRLSLISKFRFNFLAacetylation[3]
246LSDVVPFKVPGKDTVubiquitination[4]
269SSLEQMAKLKPAFIKacetylation[1, 2]
271LEQMAKLKPAFIKPYacetylation[2]
326MYVSQDPKDQLLLGPacetylation[2]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Acyltransferase; Complete proteome; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MTLVSGWLLY GWIIAVQTKT KKTLAKPNIR NVVVVDGVRT PFLLSGTSYK DLMPHDLARA 60
ALTGLLHRTS VPKEVVDYII FGTVIQEVKT SNVAREAALG AGFSDKTPAH TVTMACISAN 120
QAMTTGVGLI ASGQCDVIVA GGVELMSDVP IRHSRKMRKL MLDLNKAKSM GQRLSLISKF 180
RFNFLAPELP AVSEFSTSET MGHSADRLAA AFAVSRLEQD EYALRSHSLA KKAQDEGLLS 240
DVVPFKVPGK DTVTKDNGIR PSSLEQMAKL KPAFIKPYGT VTAANSSFLT DGASAMLIMA 300
EEKALAMGYK PKAYLRDFMY VSQDPKDQLL LGPTYATPKV LEKAGLTMND IDAFEFHEAF 360
SGQILANFKA MDSDWFAENY MGRKTKVGLP PLEKFNNWGG SLSLGHPFGA TGCRLVMAAA 420
NRLRKEGGQY GLVAACAAGG QGHAMIVEAY PK 452 
Gene Ontology
 GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. 
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