CPLM-005311

Genbank Nucleotide ID

ATP synthase subunit b, mitochondrial

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
18	ATAAPSLKNAAFLGP	ubiquitination	[1, 2]
53	PLPEYGGKVRYGLIP	ubiquitination	[2]
126	FVADFADKLNEQKLA	ubiquitination	[2, 3]
131	ADKLNEQKLAQLEEA	acetylation	[4]
131	ADKLNEQKLAQLEEA	ubiquitination	[2, 3]
139	LAQLEEAKQASIQHI	ubiquitination	[1, 2, 3]
154	QNAIDTEKSQQALVQ	acetylation	[4]
154	QNAIDTEKSQQALVQ	ubiquitination	[3]
162	SQQALVQKRHYLFDV	acetylation	[4]
162	SQQALVQKRHYLFDV	ubiquitination	[2, 3, 5]
210	VQNMMRRKEQEHMIN	ubiquitination	[2]
221	HMINWVEKHVVQSIS	acetylation	[4, 6, 7]
233	SISTQQEKETIAKCI	acetylation	[4, 6, 7, 8, 9]
233	SISTQQEKETIAKCI	ubiquitination	[1, 2, 3]
238	QEKETIAKCIADLKL	acetylation	[6]
244	AKCIADLKLLAKKAQ	ubiquitination	[5]

[1] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[9] 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(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 (By similarity).
MOD_RES 131 131 N6-acetyllysine (By similarity).
MOD_RES 162 162 N6-acetyllysine (By similarity).
MOD_RES 221 221 N6-acetyllysine.
MOD_RES 233 233 N6-acetyllysine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
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:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
GO:0022904; P:respiratory electron transport chain; TAS:Reactome.

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

PF05405; Mt_ATP-synt_B