CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034471
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit alpha 
Protein Synonyms/Alias
  
Gene Name
 Atp5a1 
Gene Synonyms/Alias
 mCG_18273 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
73VVVFGNDKLIKEGDVacetylation[1, 2, 3]
73VVVFGNDKLIKEGDVubiquitination[4]
76FGNDKLIKEGDVVKRacetylation[1, 2, 3]
82IKEGDVVKRTGAIVDacetylation[2, 3]
111LGNAIDGKGPIGSKTacetylation[1, 2, 3, 5]
111LGNAIDGKGPIGSKTsuccinylation[5]
111LGNAIDGKGPIGSKTubiquitination[4]
117GKGPIGSKTRRRVGLacetylation[2, 5]
117GKGPIGSKTRRRVGLsuccinylation[5]
117GKGPIGSKTRRRVGLubiquitination[4]
125TRRRVGLKAPGIIPRubiquitination[4]
144EPMQTGIKAVDSLVPacetylation[6]
144EPMQTGIKAVDSLVPubiquitination[4]
168IGDRQTGKTSIAIDTubiquitination[4]
180IDTIINQKRFNDGTDacetylation[2, 3, 5]
180IDTIINQKRFNDGTDsuccinylation[5]
180IDTIINQKRFNDGTDubiquitination[4]
189FNDGTDEKKKLYCIYacetylation[1, 2, 3, 5, 7, 8]
189FNDGTDEKKKLYCIYsuccinylation[5]
190NDGTDEKKKLYCIYVacetylation[1, 2]
191DGTDEKKKLYCIYVAacetylation[1, 2]
211STVAQLVKRLTDADAacetylation[1, 2, 3, 5, 6]
211STVAQLVKRLTDADAsuccinylation[5]
211STVAQLVKRLTDADAubiquitination[4]
220LTDADAMKYTIVVSAacetylation[3]
255EYFRDNGKHALIIYDacetylation[1, 2, 3, 5]
255EYFRDNGKHALIIYDsuccinylation[5]
255EYFRDNGKHALIIYDubiquitination[4]
266IIYDDLSKQAVAYRQacetylation[3]
377AAQTRAMKQVAGTMKacetylation[1, 2, 3, 5]
377AAQTRAMKQVAGTMKsuccinylation[5]
377AAQTRAMKQVAGTMKubiquitination[4]
384KQVAGTMKLELAQYRacetylation[1, 2, 3, 6]
384KQVAGTMKLELAQYRubiquitination[4]
422VRLTELLKQGQYSPMacetylation[3]
448GVRGYLDKLEPSKITacetylation[1, 2, 3, 5, 6, 7, 8, 9]
448GVRGYLDKLEPSKITsuccinylation[5]
448GVRGYLDKLEPSKITubiquitination[4]
453LDKLEPSKITKFENAacetylation[2, 3]
453LDKLEPSKITKFENAubiquitination[4]
456LEPSKITKFENAFLSacetylation[2, 3, 5, 8]
456LEPSKITKFENAFLSsuccinylation[5]
481GNIRSDGKISEQSDAacetylation[1, 2, 3, 5, 7, 8]
481GNIRSDGKISEQSDAsuccinylation[5]
489ISEQSDAKLKEIVTNacetylation[1, 2, 3, 5, 7, 8, 9]
489ISEQSDAKLKEIVTNsuccinylation[5]
489ISEQSDAKLKEIVTNsuccinylation[5]
489ISEQSDAKLKEIVTNubiquitination[4]
491EQSDAKLKEIVTNFLacetylation[1, 2, 3, 6, 7, 10]
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] 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] 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 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]
 [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] 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]
 [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]
 [9] 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]
 [10] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379
Functional Description
 Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). 
Sequence Annotation
  
Keyword
 ATP synthesis; ATP-binding; CF(1); Complete proteome; Hydrogen ion transport; Ion transport; Nucleotide-binding; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 503 AA 
Protein Sequence
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE 60
PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR 120
RVGLKAPGII PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK 180
RFNDGTDEKK KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP 240
YSGCSMGEYF RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 300
RAAKMNDSFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV 360
GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL 420
LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ SLLGNIRSDG 480
KISEQSDAKL KEIVTNFLAG FEP 503 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IMP:MGI.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:MGI.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
 GO:0009790; P:embryo development; IMP:MGI.
 GO:0006629; P:lipid metabolic process; IMP:MGI.
 GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Compara. 
Interpro
 IPR020003; ATPase_a/bsu_AS.
 IPR004100; ATPase_a/bsu_N.
 IPR005294; ATPase_F1-cplx_asu.
 IPR023366; ATPase_F1/A1-cplx_a_su_N.
 IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
  
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS