ATPG_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPG_MOUSE
• UniProt AC: Q91VR2
• Protein Name: ATP synthase subunit gamma, mitochondrial {ECO:0000305}
• Gene Name: Atp5f1c {ECO:0000250|UniProtKB:P36542}
• Organism: Mus musculus (Mouse).
• Sequence Length: 298
• Subcellular Localization: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side .
• 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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..
• Protein Sequence: MFSRASVVGLSACAVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGTGSLALYEKADIKAPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKNEVAALTAAGKEVMIVGVGEKIKGILYRTHSDQFLVSFKDVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNQFKSVISYKTEEKPIFSLNTIATAETMSIYDDIDADVLQNYQEYNLANLIYYSLKESTTSEQSARMTAMDNASKNASDMIDKLTLTFNRTRQAVITKELIEIISGAAALD

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
29	Succinylation	VRNMATLKDITRRLK ECCCHHHHHHHHHHH	42.61	24315375
29	Ubiquitination	VRNMATLKDITRRLK ECCCHHHHHHHHHHH	42.61	-
39	Acetylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	23576753
39	Succinylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	26388266
39	Malonylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	26320211
49	Succinylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	-
49	Succinylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	23806337
49	Acetylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	24062335
55	Ubiquitination	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	-
55	Succinylation	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	26388266
55	Acetylation	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	24062335
64	Acetylation	ARAERELKPARVYGT HHHHHHCCCCEEECC	31.70	51083871
79	Acetylation	GSLALYEKADIKAPE CCEEEHHHCCCCCCC	37.49	89839
83	Succinylation	LYEKADIKAPEDKKK EHHHCCCCCCCCCCC	59.44	26388266
88	Acetylation	DIKAPEDKKKHLIIG CCCCCCCCCCCEEEE	63.16	6566835
89	Acetylation	IKAPEDKKKHLIIGV CCCCCCCCCCEEEEE	58.72	24062335
90	Acetylation	KAPEDKKKHLIIGVS CCCCCCCCCEEEEEC	49.75	24062335
103	S-palmitoylation	VSSDRGLCGAIHSSV ECCCCCHHHHHHHHH	3.73	28526873
103	S-nitrosylation	VSSDRGLCGAIHSSV ECCCCCHHHHHHHHH	3.73	22178444
103	S-nitrosocysteine	VSSDRGLCGAIHSSV ECCCCCHHHHHHHHH	3.73	-
103	Glutathionylation	VSSDRGLCGAIHSSV ECCCCCHHHHHHHHH	3.73	24333276
108	Phosphorylation	GLCGAIHSSVAKQMK CHHHHHHHHHHHHHH	22.01	22817900
115	Succinylation	SSVAKQMKNEVAALT HHHHHHHHHHHHHHH	47.68	23806337
115	Acetylation	SSVAKQMKNEVAALT HHHHHHHHHHHHHHH	47.68	23576753
115	Succinylation	SSVAKQMKNEVAALT HHHHHHHHHHHHHHH	47.68	-
138	Malonylation	VGVGEKIKGILYRTH EECCHHCCEEEEECC	51.47	26320211
138	Succinylation	VGVGEKIKGILYRTH EECCHHCCEEEEECC	51.47	26388266
138	Acetylation	VGVGEKIKGILYRTH EECCHHCCEEEEECC	51.47	23576753
142	Phosphorylation	EKIKGILYRTHSDQF HHCCEEEEECCCCCE	16.14	26745281
144	Phosphorylation	IKGILYRTHSDQFLV CCEEEEECCCCCEEE	16.51	22324799
146	Phosphorylation	GILYRTHSDQFLVSF EEEEECCCCCEEEEE	32.28	26824392
152	Phosphorylation	HSDQFLVSFKDVGRK CCCCEEEEEHHCCCC	28.82	22324799
154	Succinylation	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	-
154	Succinylation	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	23806337
154	Malonylation	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	26320211
154	Glutarylation	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	24703693
154	Acetylation	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	23576753
154	Ubiquitination	DQFLVSFKDVGRKPP CCEEEEEHHCCCCCC	43.95	-
197	Acetylation	FKSVISYKTEEKPIF CCHHHEEECCCCCCE	42.54	22645573
255	Phosphorylation	SEQSARMTAMDNASK CHHHHHHHHHHHHHH	17.18	28576409
262	Ubiquitination	TAMDNASKNASDMID HHHHHHHHCHHHHHH	54.87	-
265	Phosphorylation	DNASKNASDMIDKLT HHHHHCHHHHHHHHH	36.79	23737553
270	Succinylation	NASDMIDKLTLTFNR CHHHHHHHHHHCCCC	32.23	-
270	Succinylation	NASDMIDKLTLTFNR CHHHHHHHHHHCCCC	32.23	23806337
270	Acetylation	NASDMIDKLTLTFNR CHHHHHHHHHHCCCC	32.23	66692537
270	Ubiquitination	NASDMIDKLTLTFNR CHHHHHHHHHHCCCC	32.23	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPG_MOUSE !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of ATPG_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-79; LYS-90 AND LYS-115, ANDMASS SPECTROMETRY.
PubMed: 16916647

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.
PubMed: 19367708