CPLM-009025

Genbank Nucleotide ID

ATP synthase subunit epsilon, mitochondrial

Protein Synonyms/Alias

ATPase subunit epsilon

Mus musculus (Mouse)

Position	Peptide	Type	References
21	RFSQICAKAVRDALK	acetylation	[1, 2, 3, 4, 5, 6]
21	RFSQICAKAVRDALK	succinylation	[5]
28	KAVRDALKTEFKANA	acetylation	[1, 3, 4, 5, 6]
28	KAVRDALKTEFKANA	succinylation	[5]
32	DALKTEFKANAEKTS	acetylation	[1, 3, 4, 5, 6]
32	DALKTEFKANAEKTS	succinylation	[5]
32	DALKTEFKANAEKTS	ubiquitination	[7]
37	EFKANAEKTSGSSIK	acetylation	[1, 3, 4, 5, 6]
37	EFKANAEKTSGSSIK	succinylation	[5]
44	KTSGSSIKIVKVSKK	acetylation	[2, 3, 4, 5, 6]
44	KTSGSSIKIVKVSKK	succinylation	[5]
47	GSSIKIVKVSKKE**	acetylation	[3]

[1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[7] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

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 (By similarity).

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro.
GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; ISA:MGI.
GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
GO:0015986; P:ATP synthesis coupled proton transport; ISA:MGI.

IPR006721; ATPase_F1-cplx_esu_mt.

PF04627; ATP-synt_Eps