CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006648
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit gamma, mitochondrial 
Protein Synonyms/Alias
 F-ATPase gamma subunit 
Gene Name
 ATP5C1 
Gene Synonyms/Alias
 ATP5C; ATP5CL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
49QKITKSMKMVAAAKYubiquitination[1, 2]
55MKMVAAAKYARAEREacetylation[3]
55MKMVAAAKYARAEREubiquitination[1, 2, 4]
112AIHSSIAKQMKSEVAubiquitination[1, 2, 4]
115SSIAKQMKSEVATLTubiquitination[4]
136MLVGIGDKIRGILYRubiquitination[1, 2, 4]
154DQFLVAFKEVGRKPPacetylation[3]
197FRSVISYKTEEKPIFacetylation[3]
262TAMDNASKNASEMIDubiquitination[4, 5]
270NASEMIDKLTLTFNRubiquitination[1, 2, 4, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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
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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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. 
Sequence Annotation
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 79 79 N6-acetyllysine (By similarity).
 MOD_RES 90 90 N6-acetyllysine (By similarity).
 MOD_RES 115 115 N6-acetyllysine (By similarity).
 MOD_RES 146 146 Phosphoserine (By similarity).
 MOD_RES 154 154 N6-acetyllysine.
 MOD_RES 197 197 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP synthesis; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 298 AA 
Protein Sequence
MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 60
RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR GLCGAIHSSI AKQMKSEVAT 120
LTAAGKEVML VGIGDKIRGI LYRTHSDQFL VAFKEVGRKP PTFGDASVIA LELLNSGYEF 180
DEGSIIFNKF RSVISYKTEE KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY 240
SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); NAS:UniProtKB.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; 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:0006119; P:oxidative phosphorylation; NAS:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; TAS:Reactome. 
Interpro
 IPR000131; ATPase_F1-cplx_gsu.
 IPR023632; ATPase_F1_gsu_CS.
 IPR023633; ATPase_F1_gsu_dom. 
Pfam
 PF00231; ATP-synt 
SMART
  
PROSITE
 PS00153; ATPASE_GAMMA 
PRINTS
 PR00126; ATPASEGAMMA.