CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005443
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit alpha, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 ATP5A1 
Gene Synonyms/Alias
 ATP5A; ATP5AL2; ATPM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45ASNTHLQKTGTAEMSubiquitination[1, 2]
123VVVFGNDKLIKEGDIubiquitination[2]
126FGNDKLIKEGDIVKRubiquitination[2, 3]
161LGNAIDGKGPIGSKTacetylation[4]
161LGNAIDGKGPIGSKTubiquitination[1, 2, 3, 5, 6, 7]
167GKGPIGSKTRRRVGLubiquitination[1, 6]
175TRRRVGLKAPGIIPRubiquitination[1, 2, 5, 7, 8]
194EPMQTGIKAVDSLVPubiquitination[1, 2, 3, 5, 7]
218IGDRQTGKTSIAIDTubiquitination[2]
230IDTIINQKRFNDGSDubiquitination[1, 2, 3, 5, 6, 7]
239FNDGSDEKKKLYCIYacetylation[4]
261STVAQLVKRLTDADAacetylation[4]
261STVAQLVKRLTDADAubiquitination[1, 2, 3, 8]
305EYFRDNGKHALIIYDacetylation[4]
305EYFRDNGKHALIIYDubiquitination[1, 2, 3]
316IIYDDLSKQAVAYRQubiquitination[1, 2, 5, 7]
427AAQTRAMKQVAGTMKubiquitination[1, 2]
434KQVAGTMKLELAQYRacetylation[4]
434KQVAGTMKLELAQYRubiquitination[5, 7]
472VRLTELLKQGQYSPMubiquitination[2]
498GVRGYLDKLEPSKITacetylation[4, 9]
498GVRGYLDKLEPSKITubiquitination[1, 2, 5, 7]
506LEPSKITKFENAFLSacetylation[4]
506LEPSKITKFENAFLSubiquitination[1, 2]
531GTIRADGKISEQSDAacetylation[10]
531GTIRADGKISEQSDAubiquitination[2, 3]
539ISEQSDAKLKEIVTNacetylation[4]
539ISEQSDAKLKEIVTNubiquitination[1, 2, 3]
541EQSDAKLKEIVTNFLubiquitination[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [10] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 
Functional Description
 Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). 
Sequence Annotation
 NP_BIND 212 219 ATP (By similarity).
 MOD_RES 44 44 Pyrrolidone carboxylic acid (By
 MOD_RES 76 76 Phosphoserine (By similarity).
 MOD_RES 132 132 N6-acetyllysine (By similarity).
 MOD_RES 161 161 N6-acetyllysine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 230 230 N6-acetyllysine (By similarity).
 MOD_RES 239 239 N6-acetyllysine (By similarity).
 MOD_RES 261 261 N6-acetyllysine.
 MOD_RES 305 305 N6-acetyllysine.
 MOD_RES 427 427 N6-acetyllysine (By similarity).
 MOD_RES 434 434 N6-acetyllysine.
 MOD_RES 498 498 N6-acetyllysine.
 MOD_RES 506 506 N6-acetyllysine.
 MOD_RES 531 531 N6-acetyllysine (By similarity).
 MOD_RES 539 539 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 553 AA 
Protein Sequence
MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE MSSILEERIL 60
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG 120
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII 180
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK 240
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 300
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG 360
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA 420
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA 480
IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVVSQHQ ALLGTIRADG KISEQSDAKL 540
KEIVTNFLAG FEA 553 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:UniProtKB.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0009790; P:embryo development; ISS:UniProtKB.
 GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
 GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
 GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; TAS:Reactome. 
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