CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029463
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
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41KELDPIQKLFVDKIRacetylation[1, 2]
41KELDPIQKLFVDKIRubiquitination[3]
46IQKLFVDKIREYKSKacetylation[1, 2, 4]
46IQKLFVDKIREYKSKubiquitination[3]
79ERELFKLKQMFGNADacetylation[2]
79ERELFKLKQMFGNADubiquitination[3, 5, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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
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 (By similarity). 
Sequence Annotation
  
Keyword
 Complete proteome; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 119 AA 
Protein Sequence
MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP 60
VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEEHFS QHLRSWQPSR DDDILILSS 119 
Gene Ontology
 GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. 
Interpro
 IPR008387; ATPase_F0-cplx_f6su_mt.
 IPR016349; ATPase_F0-cplx_f6su_mt_subgr. 
Pfam
 PF05511; ATP-synt_F6 
SMART
  
PROSITE
  
PRINTS