CPLM-009024

Genbank Nucleotide ID

ATP synthase subunit epsilon, mitochondrial

Protein Synonyms/Alias

ATPase subunit epsilon

Homo sapiens (Human)

Position	Peptide	Type	References
21	RYSQICAKAVRDALK	acetylation	[1, 2]
21	RYSQICAKAVRDALK	ubiquitination	[3, 4]
44	KTSGSNVKIVKVKKE	acetylation	[5]

[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] 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]
[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] 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]
[5] 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(1) domain and of the central stalk which is part of the complex rotary element. 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 (By similarity).

MOD_RES 21 21 N6-acetyllysine.

Acetylation; ATP synthesis; CF(1); Complete proteome; Disease mutation; Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro.
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:0022904; P:respiratory electron transport chain; TAS:Reactome.

IPR006721; ATPase_F1-cplx_esu_mt.

PF04627; ATP-synt_Eps