CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038768
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Pyruvate carboxylase 
Protein Synonyms/Alias
  
Gene Name
 Pcx 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
36NVRRLEYKPIKKVMVacetylation[1, 2, 3, 4]
39RLEYKPIKKVMVANRacetylation[2, 3, 4]
80TGQMHRQKADEAYLIacetylation[2, 3, 4, 5]
80TGQMHRQKADEAYLIsuccinylation[5]
80TGQMHRQKADEAYLIubiquitination[6]
105LHIPDIIKVAKENGVacetylation[2, 3, 4]
105LHIPDIIKVAKENGVubiquitination[6]
108PDIIKVAKENGVDAVacetylation[2, 3, 4]
108PDIIKVAKENGVDAVubiquitination[6]
153VVRKMGDKVEARAIAacetylation[2, 4]
238NGALFVEKFIEKPRHacetylation[7]
242FVEKFIEKPRHIEVQacetylation[2]
274SIQRRHQKVVEIAPAubiquitination[6]
298RLTSDSVKLAKQVGYacetylation[1, 2, 3, 4]
298RLTSDSVKLAKQVGYubiquitination[6]
301SDSVKLAKQVGYENAacetylation[2]
301SDSVKLAKQVGYENAubiquitination[6]
317TVEFLVDKHGKHYFIacetylation[1, 2, 3, 4, 7]
317TVEFLVDKHGKHYFIubiquitination[6]
320FLVDKHGKHYFIEVNacetylation[2, 3, 4]
435VKVIAHGKDHPTAATacetylation[2, 3, 4]
443DHPTAATKMSRALAEacetylation[1, 4, 5]
443DHPTAATKMSRALAEsuccinylation[5]
589RVRTHDLKKIAPYVAacetylation[2, 4]
590VRTHDLKKIAPYVAHubiquitination[6]
662YPDNVVFKFCEVAKEacetylation[1, 3, 4]
662YPDNVVFKFCEVAKEubiquitination[6]
668FKFCEVAKENGMDVFacetylation[2, 3, 4]
668FKFCEVAKENGMDVFubiquitination[6]
749KDMAGLLKPAACTMLacetylation[2, 3, 4]
887HSMGLGSKFKEVKKAacetylation[2]
893SKFKEVKKAYVEANQubiquitination[6]
907QMLGDLIKVTPSSKIubiquitination[6]
913IKVTPSSKIVGDLAQacetylation[3]
970PFRSKVLKDLPRIEGacetylation[3]
970PFRSKVLKDLPRIEGubiquitination[6]
989SLPPLNLKELEKDLIacetylation[1, 2, 3, 4, 5]
989SLPPLNLKELEKDLIsuccinylation[5]
989SLPPLNLKELEKDLIubiquitination[6]
993LNLKELEKDLIDRHGacetylation[1, 2, 3, 4, 7, 8]
993LNLKELEKDLIDRHGubiquitination[6]
1057EVELERGKTLHIKALacetylation[4]
1062RGKTLHIKALAVSDLacetylation[2, 3, 4]
1091QLRSILVKDTQAMKEacetylation[1, 2, 3, 4, 8]
1091QLRSILVKDTQAMKEubiquitination[6]
1097VKDTQAMKEMHFHPKacetylation[2, 4, 5]
1097VKDTQAMKEMHFHPKsuccinylation[5]
1110PKALKDVKGQIGAPMacetylation[2, 3, 4]
1120IGAPMPGKVIDIKVAacetylation[2, 3, 4]
1125PGKVIDIKVAAGDKVacetylation[2, 3, 4]
1131IKVAAGDKVAKGQPLacetylation[2, 3, 4]
Reference
 [1] 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]
 [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] 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] 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]
 [7] 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]
 [8] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599] 
Functional Description
 Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (By similarity). 
Sequence Annotation
  
Keyword
 ATP-binding; Biotin; Complete proteome; Ligase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1179 AA 
Protein Sequence
MMLKFQTVRG GLRLLGVRRS SSAPVASPNV RRLEYKPIKK VMVANRGEIA IRVFRACTEL 60
GIRTVAVYSE QDTGQMHRQK ADEAYLIGRG LAPVQAYLHI PDIIKVAKEN GVDAVHPGYG 120
FLSERADFAQ ACQDAGVRFI GPSPEVVRKM GDKVEARAIA IAAGVPVVPG TDSPISSLHE 180
AHEFSNTYGF PIIFKAAYGG GGRGMRVVHS YEELEENYTR AYSEALAAFG NGALFVEKFI 240
EKPRHIEVQI LGDQYGNILH LYERDCSIQR RHQKVVEIAP ATHLDPQLRS RLTSDSVKLA 300
KQVGYENAGT VEFLVDKHGK HYFIEVNSRL QVEHTVTEEI TDVDLVHAQI HVSEGRSLPD 360
LGLRQENIRI NGCAIQCRVT TEDPARSFQP DTGRIEVFRS GEGMGIRLDN ASAFQGAVIS 420
PHYDSLLVKV IAHGKDHPTA ATKMSRALAE FRVRGVKTNI PFLQNVLNNQ QFLAGTVDTQ 480
FIDENPELFQ LRPAQNRAQK LLHYLGHVMV NGPTTPIPVN VSPSPVDPAV PVVPIGPPPA 540
GFRDILLREG PEGFARAVRN HQGLLLMDTT FRDAHQSLLA TRVRTHDLKK IAPYVAHNFN 600
KLFSMENWGG ATFDVAMRFL YECPWRRLQE LRELIPNIPF QMLLRGANAV GYTNYPDNVV 660
FKFCEVAKEN GMDVFRVFDS LNYLPNMLLG MEAAGSAGGV VEAAISYTGD VADPSRTKYS 720
LEYYMGLAEE LVRAGTHILC IKDMAGLLKP AACTMLVSSL RDRFPDLPLH IHTHDTSGAG 780
VAAMLACAQA GADVVDVAVD SMSGMTSQPS MGALVACTKG TPLDTEVPLE RVFDYSEYWE 840
GARGLYAAFD CTATMKSGNS DVYENEIPGG QYTNLHFQAH SMGLGSKFKE VKKAYVEANQ 900
MLGDLIKVTP SSKIVGDLAQ FMVQNGLSRA EAEAQAEELS FPRSVVEFLQ GYIGIPHGGF 960
PEPFRSKVLK DLPRIEGRPG ASLPPLNLKE LEKDLIDRHG EEVTPEDVLS AAMYPDVFAQ 1020
FKDFTATFGP LDSLNTRLFL QGPKIAEEFE VELERGKTLH IKALAVSDLN RAGQRQVFFE 1080
LNGQLRSILV KDTQAMKEMH FHPKALKDVK GQIGAPMPGK VIDIKVAAGD KVAKGQPLCV 1140
LSAMKMETVV TSPMEGTIRK VHVTKDMTLE GDDLILEIE 1179 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0009374; F:biotin binding; IEA:Compara.
 GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004736; F:pyruvate carboxylase activity; IEA:EC.
 GO:0006094; P:gluconeogenesis; IEA:InterPro.
 GO:0006107; P:oxaloacetate metabolic process; IEA:Compara.
 GO:0006090; P:pyruvate metabolic process; IEA:Compara. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR001882; Biotin_BS.
 IPR011764; Biotin_carboxylation_dom.
 IPR005482; Biotin_COase_C.
 IPR000089; Biotin_lipoyl.
 IPR005481; CarbamoylP_synth_lsu_N.
 IPR003379; Carboxylase_cons_dom.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR009057; Homeodomain-like.
 IPR016185; PreATP-grasp_dom.
 IPR000891; PYR_CT.
 IPR005930; Pyruv_COase.
 IPR011054; Rudment_hybrid_motif.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF02785; Biotin_carb_C
 PF00364; Biotin_lipoyl
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2
 PF00682; HMGL-like
 PF02436; PYC_OADA 
SMART
 SM00878; Biotin_carb_C 
PROSITE
 PS50975; ATP_GRASP
 PS50979; BC
 PS00188; BIOTIN
 PS50968; BIOTINYL_LIPOYL
 PS50991; PYR_CT 
PRINTS