CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033311
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 3-ketoacyl-CoA thiolase, peroxisomal 
Protein Synonyms/Alias
  
Gene Name
 ACAA1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
251ILLARRSKAEELGLPubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 383 AA 
Protein Sequence
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT 60
PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLRVE SMSLADRGNP 120
GNITSRLMEK EKARDCLIPM GITSENVAER FGISREKQDT FALASQQKAA RAQSKGCFQA 180
EIVPVTTTVH DDKGTKRSIT VTQDEGIRPS TTMEGLAKLK PAFKKDGSTT AGNSSQVSDG 240
AAAILLARRS KAEELGLPIL GVLRSYAVVG VPPDIMGIGP AYAIPVALQK AGLTVSDVDI 300
FEINEAFASQ AAYCVEKLRL PPEKVNPLGG AVALGHPLGC TGARQVITLL NELKRRGKRA 360
YGVVSMCIGT GMGAAAVFEY PGN 383 
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.
 IPR020610; Thiolase_AS.
 IPR020617; Thiolase_C.
 IPR020613; Thiolase_CS.
 IPR020616; Thiolase_N. 
Pfam
 PF02803; Thiolase_C
 PF00108; Thiolase_N 
SMART
  
PROSITE
 PS00737; THIOLASE_2
 PS00099; THIOLASE_3 
PRINTS