CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018602
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Propionyl-CoA carboxylase alpha chain, mitochondrial 
Protein Synonyms/Alias
 PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha 
Gene Name
 Pcca 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
57VEYEPKEKTFDKILIacetylation[1]
61PKEKTFDKILIANRGacetylation[1]
128DAIMEAIKKTRAQAVacetylation[1]
146YGFLSENKEFAKRLAacetylation[1]
150SENKEFAKRLAAEDVacetylation[1]
196PGFDGVVKDADEAVRacetylation[1]
258DDRLLIEKFIDNPRHacetylation[1]
321EQAVALAKAVKYSSAacetylation[1]
324VALAKAVKYSSAGTVacetylation[1, 2, 3]
324VALAKAVKYSSAGTVsuccinylation[3]
381KGYPLRHKQEDIPISacetylation[1, 3, 4]
381KGYPLRHKQEDIPISsuccinylation[3]
403VYAEDPYKSFGLPSIacetylation[1, 2, 3, 4]
403VYAEDPYKSFGLPSIsuccinylation[3]
403VYAEDPYKSFGLPSIubiquitination[5]
492IINTRFVKGDISTKFacetylation[1, 2, 3, 4]
492IINTRFVKGDISTKFsuccinylation[3]
498VKGDISTKFLSDVYPacetylation[1, 2, 3, 4]
498VKGDISTKFLSDVYPsuccinylation[3]
509DVYPDGFKGHTLTLSacetylation[1, 3]
509DVYPDGFKGHTLTLSsuccinylation[3]
554VIRPDVAKWELSVKLacetylation[1]
637YKVHILTKLAAELNKacetylation[1]
644KLAAELNKFMLEKVPacetylation[1]
649LNKFMLEKVPKDTSSacetylation[1]
704AGKMGKVKLVHCKAGacetylation[1]
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] 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]
 [3] 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]
 [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] 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] 
Functional Description
  
Sequence Annotation
 DOMAIN 58 505 Biotin carboxylation.
 DOMAIN 177 374 ATP-grasp.
 DOMAIN 656 723 Biotinyl-binding.
 ACT_SITE 349 349 By similarity.
 BINDING 173 173 ATP (By similarity).
 BINDING 257 257 ATP (By similarity).
 BINDING 292 292 ATP (By similarity).
 MOD_RES 690 690 N6-biotinyllysine (By similarity).  
Keyword
 ATP-binding; Biotin; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 724 AA 
Protein Sequence
MAGQWVRTVA LLAARRHWRR SSQQQLLGTL KHAPVYSYQC LVVSRSLSSV EYEPKEKTFD 60
KILIANRGEI ACRVIKTCKK MGIKTVAIHS DVDASSVHVK MADEAVCVGP APTSKSYLNM 120
DAIMEAIKKT RAQAVHPGYG FLSENKEFAK RLAAEDVTFI GPDTHAIQAM GDKIESKLLA 180
KRAKVNTIPG FDGVVKDADE AVRIAREIGY PVMIKASAGG GGKGMRIAWD DEETRDGFRF 240
SSQEAASSFG DDRLLIEKFI DNPRHIEIQV LGDKHGNALW LNERECSIQR RNQKVVEEAP 300
SIFLDPETRQ AMGEQAVALA KAVKYSSAGT VEFLVDSQKN FYFLEMNTRL QVEHPVTECI 360
TGLDLVQEMI LVAKGYPLRH KQEDIPISGW AVECRVYAED PYKSFGLPSI GRLSQYQEPI 420
HLPGVRVDSG IQPGSDISIY YDPMISKLVT YGSDRAEALK RMEDALDNYV IRGVTHNIPL 480
LREVIINTRF VKGDISTKFL SDVYPDGFKG HTLTLSERNQ LLAIASSVFV ASQLRAQRFQ 540
EHSRVPVIRP DVAKWELSVK LHDEDHTVVA SNNGPAFTVE VDGSKLNVTS TWNLASPLLS 600
VNVDGTQRTV QCLSREAGGN MSIQFLGTVY KVHILTKLAA ELNKFMLEKV PKDTSSTLCS 660
PMPGVVVAVS VKPGDMVAEG QEICVIEAMK MQNSMTAGKM GKVKLVHCKA GDTVGEGDLL 720
VELE 724 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004658; F:propionyl-CoA carboxylase activity; IMP:MGI. 
Interpro
 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.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR016185; PreATP-grasp_dom.
 IPR011054; Rudment_hybrid_motif.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF02785; Biotin_carb_C
 PF00364; Biotin_lipoyl
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2 
SMART
 SM00878; Biotin_carb_C 
PROSITE
 PS50975; ATP_GRASP
 PS50979; BC
 PS00188; BIOTIN
 PS50968; BIOTINYL_LIPOYL
 PS00866; CPSASE_1
 PS00867; CPSASE_2 
PRINTS