CPLM-006648

Genbank Nucleotide ID

ATP synthase subunit gamma, mitochondrial

Protein Synonyms/Alias

F-ATPase gamma subunit

Homo sapiens (Human)

Position	Peptide	Type	References
49	QKITKSMKMVAAAKY	ubiquitination	[1, 2]
55	MKMVAAAKYARAERE	acetylation	[3]
55	MKMVAAAKYARAERE	ubiquitination	[1, 2, 4]
112	AIHSSIAKQMKSEVA	ubiquitination	[1, 2, 4]
115	SSIAKQMKSEVATLT	ubiquitination	[4]
136	MLVGIGDKIRGILYR	ubiquitination	[1, 2, 4]
154	DQFLVAFKEVGRKPP	acetylation	[3]
197	FRSVISYKTEEKPIF	acetylation	[3]
262	TAMDNASKNASEMID	ubiquitination	[4, 5]
270	NASEMIDKLTLTFNR	ubiquitination	[1, 2, 4, 5]

[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.

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.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR000131; ATPase_F1-cplx_gsu.
IPR023632; ATPase_F1_gsu_CS.
IPR023633; ATPase_F1_gsu_dom.

PS00153; ATPASE_GAMMA

PR00126; ATPASEGAMMA.