CPLM-007991

Genbank Nucleotide ID

ATP synthase subunit O, mitochondrial

Protein Synonyms/Alias

Oligomycin sensitivity conferral protein; OSCP

Homo sapiens (Human)

Position	Peptide	Type	References
51	ALYSAASKQNKLEQV	ubiquitination	[1, 2]
54	SAASKQNKLEQVEKE	acetylation	[3]
54	SAASKQNKLEQVEKE	ubiquitination	[1, 2]
60	NKLEQVEKELLRVAQ	acetylation	[3, 4]
60	NKLEQVEKELLRVAQ	ubiquitination	[1, 2, 5]
70	LRVAQILKEPKVAAS	acetylation	[3]
70	LRVAQILKEPKVAAS	ubiquitination	[1, 2]
73	AQILKEPKVAASVLN	ubiquitination	[1, 2, 5]
84	SVLNPYVKRSIKVKS	ubiquitination	[1, 2, 6]
88	PYVKRSIKVKSLNDI	ubiquitination	[1, 2]
90	VKRSIKVKSLNDITA	ubiquitination	[1, 2]
98	SLNDITAKERFSPLT	ubiquitination	[1, 2]
158	EATLSELKTVLKSFL	ubiquitination	[1, 2]
162	SELKTVLKSFLSQGQ	acetylation	[3]
162	SELKTVLKSFLSQGQ	ubiquitination	[1, 2, 5]
172	LSQGQVLKLEAKTDP	acetylation	[3]
172	LSQGQVLKLEAKTDP	ubiquitination	[1, 2]
176	QVLKLEAKTDPSILG	ubiquitination	[1, 2]
192	MIVRIGEKYVDMSVK	acetylation	[3, 7, 8, 9]
192	MIVRIGEKYVDMSVK	ubiquitination	[1, 2]
199	KYVDMSVKTKIQKLG	ubiquitination	[1, 2]

[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] 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]
[5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[6] 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]
[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] 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]
[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 54 54 N6-acetyllysine.
MOD_RES 60 60 N6-acetyllysine (By similarity).
MOD_RES 70 70 N6-acetyllysine (By similarity).
MOD_RES 158 158 N6-acetyllysine (By similarity).
MOD_RES 162 162 N6-acetyllysine.
MOD_RES 172 172 N6-acetyllysine.
MOD_RES 176 176 N6-acetyllysine (By similarity).
MOD_RES 192 192 N6-acetyllysine.

Acetylation; ATP synthesis; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Polymorphism; Reference proteome; Transit peptide; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:Compara.
GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO:0008144; F:drug binding; IDA:UniProtKB.
GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
GO:0005496; F:steroid binding; IEA:Compara.
GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
GO:0006200; P:ATP catabolic process; IDA:UniProtKB.
GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
GO:0022904; P:respiratory electron transport chain; TAS:Reactome.

IPR000711; ATPase_F1-cplx_OSCP/dsu.
IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
IPR026015; ATPase_OSCP/delta_N.

PS00389; ATPASE_DELTA

PR00125; ATPASEDELTA.