CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008546
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carnitine O-palmitoyltransferase 2, mitochondrial 
Protein Synonyms/Alias
 Carnitine palmitoyltransferase II; CPT II 
Gene Name
 Cpt2 
Gene Synonyms/Alias
 Cpt-2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
69KRYLSAQKPLLNDSQacetylation[1]
79LNDSQFRKTEVLCKDacetylation[1]
85RKTEVLCKDFENGIGacetylation[1]
93DFENGIGKELHAHLLacetylation[1]
104AHLLAQDKQNKHTSYacetylation[1]
239DELFTDTKARHLLVLacetylation[1]
305VWAELRQKLIHGGNEacetylation[1, 2, 3, 4]
414DSSVSVQKLSFKLSSacetylation[4]
418SVQKLSFKLSSALKAacetylation[1, 3, 4, 5]
418SVQKLSFKLSSALKAsuccinylation[5]
424FKLSSALKAGVTAAKacetylation[1, 5]
424FKLSSALKAGVTAAKsuccinylation[5]
433GVTAAKEKFDATMKTacetylation[1, 4]
439EKFDATMKTLTIDAIacetylation[1, 5]
439EKFDATMKTLTIDAIsuccinylation[5]
453IQFQRGGKEFLKKKKacetylation[1, 3, 4]
457RGGKEFLKKKKLSPDacetylation[1, 3]
495SCSTAAFKHGRTETIacetylation[3]
510RPASIFTKRCSEAFVacetylation[1, 3, 5]
510RPASIFTKRCSEAFVsuccinylation[5]
537HMMAECSKYHGQLTKacetylation[3, 4]
544KYHGQLTKEAAMGQGacetylation[1, 3, 4, 5, 6, 7]
544KYHGQLTKEAAMGQGsuccinylation[5]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
 REGION 452 464 Coenzyme A binding (By similarity).
 ACT_SITE 372 372 Proton acceptor (By similarity).
 BINDING 486 486 Carnitine (By similarity).
 BINDING 488 488 Carnitine (By similarity).
 BINDING 499 499 Carnitine (By similarity).
 MOD_RES 544 544 N6-acetyllysine.  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transferase; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 658 AA 
Protein Sequence
MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP RLPIPKLEDT 60
MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL AQDKQNKHTS YISGPWFDMY 120
LTARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLRAGL LEPEVFHLNP 180
ARSDTDAFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPKPS RDELFTDTKA 240
RHLLVLRKGH FYVFDVLDQD GNIVNPSEIQ AHLKYILSDS SPVPEFPLAY LTSENRDVWA 300
ELRQKLIHGG NEETLRKVDS AVFCLCLDDF PMKDLVHLSH TMLHGDGTNR WFDKSFNLIV 360
AKDGTAAVHF EHAWGDGVAV LRFFNEVFRD STQTPAIAPQ SQPAATDSSV SVQKLSFKLS 420
SALKAGVTAA KEKFDATMKT LTIDAIQFQR GGKEFLKKKK LSPDAVAQLA FQMAFLRQYG 480
QTVATYESCS TAAFKHGRTE TIRPASIFTK RCSEAFVREP SKHSVGELQH MMAECSKYHG 540
QLTKEAAMGQ GFDRHLFALR YLAAARGVTL PELYQDPAYQ RINHNILSTS TLSSPAVSLG 600
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDMFDA LEGKAIKT 658 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:EC.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
 GO:0006810; P:transport; IEA:UniProtKB-KW. 
Interpro
 IPR000542; Carn_acyl_trans. 
Pfam
 PF00755; Carn_acyltransf 
SMART
  
PROSITE
 PS00439; ACYLTRANSF_C_1
 PS00440; ACYLTRANSF_C_2 
PRINTS