CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008947
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Trifunctional enzyme subunit beta, mitochondrial 
Protein Synonyms/Alias
 TP-beta; 3-ketoacyl-CoA thiolase; Acetyl-CoA acyltransferase; Beta-ketothiolase 
Gene Name
 HADHB 
Gene Synonyms/Alias
 MSTP029 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
72LLSGTSYKDLMPHDLacetylation[1, 2]
72LLSGTSYKDLMPHDLubiquitination[3, 4]
181RHSRKMRKLMLDLNKacetylation[5]
188KLMLDLNKAKSMGQRacetylation[1]
201QRLSLISKFRFNFLAacetylation[5]
268LSDVVPFKVPGKDTVubiquitination[3, 4]
291SSLEQMAKLKPAFIKacetylation[1]
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] 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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 
Functional Description
  
Sequence Annotation
 ACT_SITE 138 138 Acyl-thioester intermediate (By
 ACT_SITE 428 428 Proton acceptor (By similarity).
 ACT_SITE 458 458 Proton acceptor (By similarity).
 MOD_RES 72 72 N6-acetyllysine.
 MOD_RES 188 188 N6-acetyllysine.
 MOD_RES 201 201 N6-acetyllysine (By similarity).
 MOD_RES 348 348 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane; Polymorphism; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 474 AA 
Protein Sequence
MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN IRNVVVVDGV 60
RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA 120
LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR 180
KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE 240
QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY 300
GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP 360
KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW 420
GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK 474 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
 GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; TAS:ProtInc.
 GO:0003988; F:acetyl-CoA C-acyltransferase activity; TAS:ProtInc.
 GO:0004300; F:enoyl-CoA hydratase activity; TAS:ProtInc.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:Compara.
 GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IEA:Compara.
 GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IEA:Compara.
 GO:0051287; F:NAD binding; IEA:Compara.
 GO:0035965; P:cardiolipin acyl-chain remodeling; TAS:Reactome.
 GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
 GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome. 
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