CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004714
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase-coupling factor 6, mitochondrial 
Protein Synonyms/Alias
 ATPase subunit F6 
Gene Name
 ATP5J 
Gene Synonyms/Alias
 ATP5A; ATPM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41KELDPIQKLFVDKIRacetylation[1]
41KELDPIQKLFVDKIRubiquitination[2, 3]
46IQKLFVDKIREYKSKacetylation[1]
46IQKLFVDKIREYKSKubiquitination[2, 3]
79ERELFKLKQMFGNADubiquitination[2, 3, 4]
94MNTFPTFKFEDPKFEacetylation[5]
94MNTFPTFKFEDPKFEubiquitination[4]
99TFKFEDPKFEVIEKPacetylation[1, 6, 7, 8]
99TFKFEDPKFEVIEKPubiquitination[2, 3]
105PKFEVIEKPQA****acetylation[1, 5, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. 
Sequence Annotation
 MOD_RES 41 41 N6-acetyllysine.
 MOD_RES 46 46 N6-acetyllysine.
 MOD_RES 99 99 N6-acetyllysine.
 MOD_RES 105 105 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; CF(0); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 108 AA 
Protein Sequence
MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP 60
VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA 108 
Gene Ontology
 GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
 GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
 GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
 GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
 GO:0006200; P:ATP catabolic process; IDA:GOC.
 GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; TAS:Reactome. 
Interpro
 IPR008387; ATPase_F0-cplx_f6su_mt.
 IPR016349; ATPase_F0-cplx_f6su_mt_subgr. 
Pfam
 PF05511; ATP-synt_F6 
SMART
  
PROSITE
  
PRINTS