CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010677
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carnitine O-palmitoyltransferase 1, liver isoform 
Protein Synonyms/Alias
 CPT1-L; Carnitine O-palmitoyltransferase I, liver isoform; CPT I; CPTI-L; Carnitine palmitoyltransferase 1A 
Gene Name
 Cpt1a 
Gene Synonyms/Alias
 Cpt-1; Cpt1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
29RLSHEALKQICLSGLubiquitination[1]
161VKVFSGRKPMLYSFQubiquitination[1]
180RLPVPAVKDTVSRYLubiquitination[1]
195ESVRPLMKEGDFQRMacetylation[2]
195ESVRPLMKEGDFQRMubiquitination[1]
292TVDREELKPIRLLGSacetylation[2, 3, 4]
292TVDREELKPIRLLGSubiquitination[1]
329TDTIQHVKDSRHIVVubiquitination[1]
393ADRVPWAKCRQTYFAubiquitination[1]
441ASIDSYAKSLLHGRCubiquitination[1]
463SITFVVFKNSKIGINubiquitination[1]
508DGHCKGDKNPNIPKPacetylation[2, 4]
514DKNPNIPKPTRLQWDubiquitination[1]
634EQRFKLFKIACEKHQacetylation[2, 4]
752TDSHRFGKHLRQAMMacetylation[4, 5, 6]
772FGLTANSKK******ubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [6] Proteomics of mitochondrial inner and outer membranes.
 Distler AM, Kerner J, Hoppel CL.
 Proteomics. 2008 Oct;8(19):4066-82. [PMID: 18763707] 
Functional Description
 Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism. 
Sequence Annotation
 REGION 555 567 Coenzyme A binding (By similarity).
 ACT_SITE 473 473 Proton acceptor (By similarity).
 BINDING 589 589 Carnitine (By similarity).
 BINDING 602 602 Carnitine (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 282 282 Nitrated tyrosine (By similarity).
 MOD_RES 588 588 Phosphothreonine (By similarity).
 MOD_RES 589 589 Nitrated tyrosine (By similarity).
 MOD_RES 604 604 Phosphothreonine (By similarity).
 MOD_RES 741 741 Phosphoserine (By similarity).
 MOD_RES 747 747 Phosphoserine (By similarity).  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; Nitration; Phosphoprotein; Reference proteome; Transferase; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 773 AA 
Protein Sequence
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPASPS 60
SWLIVVVGVI SSMHTKVDPS LGMIAKINRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAIIM 120
TMRYSLKVLL SYHGWMFAEH GKMSRSTRIW MAMVKVFSGR KPMLYSFQTS LPRLPVPAVK 180
DTVSRYLESV RPLMKEGDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI 240
YLRGRGPIMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTVDREE LKPIRLLGST 300
IPLCSAQWER LFNTSRIPGE ETDTIQHVKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE 360
QQMQQILDDT SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL 420
DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPI 480
VGHLWEYVMA TDVFQLGYSE DGHCKGDKNP NIPKPTRLQW DIPGECQEVI ETSLSSASFL 540
ANDVDLHSFP FDTFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG 600
RTETVRSCTT ESCNFVLAMM DPTTTAEQRF KLFKIACEKH QHLYRLAMTG AGIDRHLFCL 660
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KYPDYVSCGG GFGPVADDGY 720
GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTAN SKK 773 
Gene Ontology
 GO:0031307; C:integral to mitochondrial outer membrane; ISS:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:UniProtKB.
 GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
 GO:0042755; P:eating behavior; IEA:Compara.
 GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
 GO:0006006; P:glucose metabolic process; IEA:Compara.
 GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
 GO:0032000; P:positive regulation of fatty acid beta-oxidation; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0050796; P:regulation of insulin secretion; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0006810; P:transport; IEA:UniProtKB-KW.
 GO:0006641; P:triglyceride metabolic process; IEA:Compara. 
Interpro
 IPR000542; Carn_acyl_trans. 
Pfam
 PF00755; Carn_acyltransf 
SMART
  
PROSITE
 PS00439; ACYLTRANSF_C_1
 PS00440; ACYLTRANSF_C_2 
PRINTS