ATPO_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPO_MOUSE
• UniProt AC: Q9DB20
• Protein Name: ATP synthase subunit O, mitochondrial
• Gene Name: Atp5o
• Organism: Mus musculus (Mouse).
• Sequence Length: 213
• Subcellular Localization: Mitochondrion. Mitochondrion inner membrane.
• Protein 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..
• Protein Sequence: MAAPAASGLSRQVRSFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKEKKLDQVEKELLRVGQLLKDPKVSLAVLNPYIKRTVKVKSLNDITKREKFSPLTANLMNLLAENGRLGNTQGIISAFSTIMSVHRGEVPCTVTTASPLDDAVLSELKTVLKSFLSPNQILKLEIKTDPSIMGGMIVRIGEKYVDMSAKSKIQKLSKAMREML

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MAAPAASGLSRQVR -CCCCCCCCCHHHHH	42.23	24759943
26	Succinylation	SVVRPFAKLVRPPVQ HHHHCHHHHHCCCEE	48.14	24315375
26	Acetylation	SVVRPFAKLVRPPVQ HHHHCHHHHHCCCEE	48.14	23576753
35	Nitration	VRPPVQVYGIEGRYA HCCCEEEEEECHHHH	8.69	-
35	Phosphorylation	VRPPVQVYGIEGRYA HCCCEEEEEECHHHH	8.69	17242355
51	Acetylation	ALYSAASKEKKLDQV HHHHHHHHHHCHHHH	69.68	24062335
51	Succinylation	ALYSAASKEKKLDQV HHHHHHHHHHCHHHH	69.68	26388266
51	Ubiquitination	ALYSAASKEKKLDQV HHHHHHHHHHCHHHH	69.68	-
53	Acetylation	YSAASKEKKLDQVEK HHHHHHHHCHHHHHH	63.47	24062335
54	Glutarylation	SAASKEKKLDQVEKE HHHHHHHCHHHHHHH	59.39	24703693
54	Malonylation	SAASKEKKLDQVEKE HHHHHHHCHHHHHHH	59.39	26320211
54	Acetylation	SAASKEKKLDQVEKE HHHHHHHCHHHHHHH	59.39	23576753
54	Succinylation	SAASKEKKLDQVEKE HHHHHHHCHHHHHHH	59.39	26388266
60	Ubiquitination	KKLDQVEKELLRVGQ HCHHHHHHHHHHHHH	55.60	-
60	Acetylation	KKLDQVEKELLRVGQ HCHHHHHHHHHHHHH	55.60	23576753
60	Malonylation	KKLDQVEKELLRVGQ HCHHHHHHHHHHHHH	55.60	26073543
60	Glutarylation	KKLDQVEKELLRVGQ HCHHHHHHHHHHHHH	55.60	24703693
70	Acetylation	LRVGQLLKDPKVSLA HHHHHHHHCCCCCHH	79.26	23576753
70	Succinylation	LRVGQLLKDPKVSLA HHHHHHHHCCCCCHH	79.26	23806337
70	Malonylation	LRVGQLLKDPKVSLA HHHHHHHHCCCCCHH	79.26	26320211
70	Glutarylation	LRVGQLLKDPKVSLA HHHHHHHHCCCCCHH	79.26	24703693
73	Acetylation	GQLLKDPKVSLAVLN HHHHHCCCCCHHHHC	55.37	23576753
73	Glutarylation	GQLLKDPKVSLAVLN HHHHHCCCCCHHHHC	55.37	24703693
73	Ubiquitination	GQLLKDPKVSLAVLN HHHHHCCCCCHHHHC	55.37	-
75	Phosphorylation	LLKDPKVSLAVLNPY HHHCCCCCHHHHCHH	19.41	23567750
82	Phosphorylation	SLAVLNPYIKRTVKV CHHHHCHHHHCEEEE	20.28	25195567
84	Succinylation	AVLNPYIKRTVKVKS HHHCHHHHCEEEECC	35.85	26388266
84	Ubiquitination	AVLNPYIKRTVKVKS HHHCHHHHCEEEECC	35.85	-
84	Acetylation	AVLNPYIKRTVKVKS HHHCHHHHCEEEECC	35.85	24062335
88	Acetylation	PYIKRTVKVKSLNDI HHHHCEEEECCHHHC	43.25	21728379
90	Succinylation	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	23806337
90	Glutarylation	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	24703693
90	Malonylation	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	26073543
90	Ubiquitination	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	-
90	Succinylation	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	-
90	Acetylation	IKRTVKVKSLNDITK HHCEEEECCHHHCCC	43.43	23201123
96	Phosphorylation	VKSLNDITKREKFSP ECCHHHCCCHHHCCH	27.23	-
97	Malonylation	KSLNDITKREKFSPL CCHHHCCCHHHCCHH	59.92	26073543
97	Ubiquitination	KSLNDITKREKFSPL CCHHHCCCHHHCCHH	59.92	27667366
97	Acetylation	KSLNDITKREKFSPL CCHHHCCCHHHCCHH	59.92	23864654
97	Glutarylation	KSLNDITKREKFSPL CCHHHCCCHHHCCHH	59.92	24703693
100	Succinylation	NDITKREKFSPLTAN HHCCCHHHCCHHHHH	55.99	23806337
100	Ubiquitination	NDITKREKFSPLTAN HHCCCHHHCCHHHHH	55.99	-
100	Succinylation	NDITKREKFSPLTAN HHCCCHHHCCHHHHH	55.99	-
100	Acetylation	NDITKREKFSPLTAN HHCCCHHHCCHHHHH	55.99	23576753
121	Phosphorylation	ENGRLGNTQGIISAF HHCCCCCHHHHHHHH	26.78	23140645
126	Phosphorylation	GNTQGIISAFSTIMS CCHHHHHHHHHHHHH	22.72	23140645
129	Phosphorylation	QGIISAFSTIMSVHR HHHHHHHHHHHHHCC	19.42	23140645
130	Phosphorylation	GIISAFSTIMSVHRG HHHHHHHHHHHHCCC	17.78	23140645
133	Phosphorylation	SAFSTIMSVHRGEVP HHHHHHHHHCCCCCC	15.77	23140645
141	Glutathionylation	VHRGEVPCTVTTASP HCCCCCCCEEEECCC	6.04	24333276
141	S-nitrosylation	VHRGEVPCTVTTASP HCCCCCCCEEEECCC	6.04	22588120
141	S-nitrosocysteine	VHRGEVPCTVTTASP HCCCCCCCEEEECCC	6.04	-
141	S-palmitoylation	VHRGEVPCTVTTASP HCCCCCCCEEEECCC	6.04	28526873
147	Phosphorylation	PCTVTTASPLDDAVL CCEEEECCCCCHHHH	24.73	23140645
155	Phosphorylation	PLDDAVLSELKTVLK CCCHHHHHHHHHHHH	33.99	25521595
158	Succinylation	DAVLSELKTVLKSFL HHHHHHHHHHHHHCC	32.32	23806337
158	Acetylation	DAVLSELKTVLKSFL HHHHHHHHHHHHHCC	32.32	23576753
158	Succinylation	DAVLSELKTVLKSFL HHHHHHHHHHHHHCC	32.32	-
162	Glutarylation	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	24703693
162	Succinylation	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	-
162	Acetylation	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	23576753
162	Ubiquitination	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	-
162	Malonylation	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	26073543
162	Succinylation	SELKTVLKSFLSPNQ HHHHHHHHHCCCHHH	34.52	23806337
166	Phosphorylation	TVLKSFLSPNQILKL HHHHHCCCHHHEEEE	21.57	22817900
172	Acetylation	LSPNQILKLEIKTDP CCHHHEEEEEECCCH	45.78	23576753
172	Ubiquitination	LSPNQILKLEIKTDP CCHHHEEEEEECCCH	45.78	-
172	Succinylation	LSPNQILKLEIKTDP CCHHHEEEEEECCCH	45.78	26388266
176	Succinylation	QILKLEIKTDPSIMG HEEEEEECCCHHHHC	37.18	23806337
176	Acetylation	QILKLEIKTDPSIMG HEEEEEECCCHHHHC	37.18	23576753
192	Succinylation	MIVRIGEKYVDMSAK EEEEECHHHCCCCHH	45.41	23806337
192	Ubiquitination	MIVRIGEKYVDMSAK EEEEECHHHCCCCHH	45.41	27667366
192	Acetylation	MIVRIGEKYVDMSAK EEEEECHHHCCCCHH	45.41	23864654
199	Ubiquitination	KYVDMSAKSKIQKLS HHCCCCHHHHHHHHH	45.00	-
199	Glutarylation	KYVDMSAKSKIQKLS HHCCCCHHHHHHHHH	45.00	24703693
199	Acetylation	KYVDMSAKSKIQKLS HHCCCCHHHHHHHHH	45.00	23806337
199	Succinylation	KYVDMSAKSKIQKLS HHCCCCHHHHHHHHH	45.00	23806337
199	Succinylation	KYVDMSAKSKIQKLS HHCCCCHHHHHHHHH	45.00	-
204	Acetylation	SAKSKIQKLSKAMRE CHHHHHHHHHHHHHH	59.19	23201123

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ATPO_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
70	K	Acetylation	Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice.	23576753
158	K	Acetylation	Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice.	23806337
162	K	Acetylation	Acetylation at Lys-162 decreases ATP production.	23806337

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ATPO_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ATPO_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-70; LYS-158;LYS-162; LYS-172; LYS-176 AND LYS-192, AND MASS SPECTROMETRY.
PubMed: 16916647