CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019869
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
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
49KSKKTLAKPNMKNIVacetylation[1]
53TLAKPNMKNIVVVEGacetylation[1]
73LLSGTSYKDLMPHDLacetylation[1]
73LLSGTSYKDLMPHDLubiquitination[2]
129LGAGFSDKTPAHTVTacetylation[3]
189KMMLDLNKAKTLGQRacetylation[1, 3, 4, 5, 6]
189KMMLDLNKAKTLGQRsuccinylation[6]
189KMMLDLNKAKTLGQRsuccinylation[6]
191MLDLNKAKTLGQRLSacetylation[1, 3, 6]
191MLDLNKAKTLGQRLSsuccinylation[6]
202QRLSLLSKFRLNFLSacetylation[1, 3, 5, 6, 7, 8, 9, 10]
202QRLSLLSKFRLNFLSsuccinylation[6]
202QRLSLLSKFRLNFLSubiquitination[2]
254LRSHSLAKKAQDEGHacetylation[1]
273VPFKVPGKDTVTKDNacetylation[1, 3, 5, 6]
273VPFKVPGKDTVTKDNsuccinylation[6]
278PGKDTVTKDNGIRPSacetylation[1, 3, 6]
278PGKDTVTKDNGIRPSsuccinylation[6]
292SSLEQMAKLKPAFIKacetylation[4, 6]
292SSLEQMAKLKPAFIKsuccinylation[6]
294LEQMAKLKPAFIKPYacetylation[1, 3, 5, 6]
294LEQMAKLKPAFIKPYsuccinylation[6]
299KLKPAFIKPYGTVTAacetylation[1, 3, 5, 6]
299KLKPAFIKPYGTVTAsuccinylation[6]
333RALAMGYKPKAYLRDacetylation[1, 3, 5, 6]
333RALAMGYKPKAYLRDsuccinylation[6]
335LAMGYKPKAYLRDFIacetylation[1, 3]
349IYVSQDPKDQLLLGPacetylation[1, 3, 4, 5, 7, 11]
362GPTYATPKVLEKAGLacetylation[5, 11]
362GPTYATPKVLEKAGLubiquitination[2]
417VGSPPLEKFNIWGGSacetylation[3, 5]
475MIVEAYPK*******acetylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [9] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [10] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [11] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
  
Sequence Annotation
 ACT_SITE 139 139 Acyl-thioester intermediate (By
 ACT_SITE 429 429 Proton acceptor (By similarity).
 ACT_SITE 459 459 Proton acceptor (By similarity).
 MOD_RES 73 73 N6-acetyllysine (By similarity).
 MOD_RES 189 189 N6-acetyllysine (By similarity).
 MOD_RES 202 202 N6-acetyllysine.
 MOD_RES 349 349 N6-acetyllysine.  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP NMKNIVVVEG 60
VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD YIIFGTVIQE VKTSNVAREA 120
ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM 180
RKMMLDLNKA KTLGQRLSLL SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM 240
EQDEYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP 300
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT 360
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GSPPLEKFNI 420
WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK 475 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
 GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IC:MGI.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
 GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:Compara.
 GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:MGI.
 GO:0004300; F:enoyl-CoA hydratase activity; IEA:Compara.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:Compara.
 GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IMP:MGI.
 GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IEA:Compara.
 GO:0051287; F:NAD binding; IEA:Compara.
 GO:0006635; P:fatty acid beta-oxidation; TAS:MGI. 
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