CPLM-020540

Genbank Nucleotide ID

ATP synthase subunit b, mitochondrial

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
53	PLPEYGGKVRLGLIP	acetylation	[1]
53	PLPEYGGKVRLGLIP	ubiquitination	[2]
115	LIVYVIKKYGASFGE	acetylation	[3]
126	SFGEFIDKLNEEKIA	acetylation	[4, 5]
131	IDKLNEEKIAQLEEV	acetylation	[3, 4, 5, 6, 7, 8]
131	IDKLNEEKIAQLEEV	succinylation	[8]
131	IDKLNEEKIAQLEEV	ubiquitination	[2]
139	IAQLEEVKQSSMKQI	acetylation	[1, 4, 5, 9]
139	IAQLEEVKQSSMKQI	ubiquitination	[2]
144	EVKQSSMKQIQDAID	acetylation	[4, 5, 8, 9]
144	EVKQSSMKQIQDAID	succinylation	[8]
144	EVKQSSMKQIQDAID	ubiquitination	[2]
154	QDAIDMEKAQQALVQ	acetylation	[1, 4, 5, 6, 9]
162	AQQALVQKRHYLFDV	acetylation	[1, 3, 4, 5, 9]
188	TYRERLHKAYKEVKN	acetylation	[3, 4]
191	ERLHKAYKEVKNRLD	acetylation	[4, 5]
194	HKAYKEVKNRLDYHI	acetylation	[4]
221	HMIDWVEKHVVKSIS	acetylation	[1, 3, 4, 5, 9, 10]
225	WVEKHVVKSISVQQE	acetylation	[1, 3, 4, 5, 6, 7, 8, 9, 11]
225	WVEKHVVKSISVQQE	succinylation	[8]
225	WVEKHVVKSISVQQE	ubiquitination	[2]
233	SISVQQEKETIAKCI	acetylation	[1, 3, 4, 5, 6, 7, 8, 9, 10]
233	SISVQQEKETIAKCI	succinylation	[8]
233	SISVQQEKETIAKCI	ubiquitination	[2]
238	QEKETIAKCIEDLKL	acetylation	[1, 4, 5, 9]
238	QEKETIAKCIEDLKL	ubiquitination	[2]
244	AKCIEDLKLLAKKAQ	acetylation	[1, 4, 5, 9, 10]
248	EDLKLLAKKAQAQPI	acetylation	[4]

[1] 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]
[2] 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]
[3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[4] 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]
[5] 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]
[6] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
[7] 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]
[8] 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]
[9] 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]
[10] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
[11] 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]

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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.

MOD_RES 115 115 N6-acetyllysine.
MOD_RES 131 131 N6-acetyllysine.
MOD_RES 162 162 N6-acetyllysine.
MOD_RES 188 188 N6-acetyllysine.
MOD_RES 221 221 N6-acetyllysine.
MOD_RES 225 225 N6-acetyllysine.
MOD_RES 233 233 N6-acetyllysine.

Acetylation; CF(0); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:RefGenome.
GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:RefGenome.
GO:0015986; P:ATP synthesis coupled proton transport; IBA:RefGenome.

IPR008688; ATPase_B_chain/sub_B/MI25.
IPR013837; ATPase_F0_sub_B/B_chain.

PF05405; Mt_ATP-synt_B