AT5F1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AT5F1_MOUSE
• UniProt AC: Q9CQQ7
• Protein Name: ATP synthase F(0) complex subunit B1, mitochondrial
• Gene Name: Atp5f1
• Organism: Mus musculus (Mouse).
• Sequence Length: 256
• 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: MLSRVVLSAAATAAPCLKNAAALGPGVLQATRAFHTGQPRLAPLPPLPEYGGKVRLGLIPEEFFQFLYPKTGVTGPYVLGTGLSLYFLSKEIYVITPETFSTISVVGLIVYVIKKYGASFGEFIDKLNEEKIAQLEEVKQSSMKQIQDAIDMEKAQQALVQKRHYLFDVQRNNIALALEVTYRERLHKAYKEVKNRLDYHISVQNMMRRKEEEHMIDWVEKHVVKSISVQQEKETIAKCIEDLKLLAKKAQAQPIM

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
53	Acetylation	PLPEYGGKVRLGLIP CCCCCCCEEEEECCC	21.59	23576753
53	Succinylation	PLPEYGGKVRLGLIP CCCCCCCEEEEECCC	21.59	24315375
53	Ubiquitination	PLPEYGGKVRLGLIP CCCCCCCEEEEECCC	21.59	-
115	Acetylation	LIVYVIKKYGASFGE HHHHHHHHHCCCHHH	37.48	16916647
126	Acetylation	SFGEFIDKLNEEKIA CHHHHHHHHCHHHHH	48.69	23864654
131	Ubiquitination	IDKLNEEKIAQLEEV HHHHCHHHHHHHHHH	36.84	-
131	Acetylation	IDKLNEEKIAQLEEV HHHHCHHHHHHHHHH	36.84	23864654
131	Succinylation	IDKLNEEKIAQLEEV HHHHCHHHHHHHHHH	36.84	23806337
131	Succinylation	IDKLNEEKIAQLEEV HHHHCHHHHHHHHHH	36.84	-
139	Acetylation	IAQLEEVKQSSMKQI HHHHHHHHHHHHHHH	47.98	23576753
139	Ubiquitination	IAQLEEVKQSSMKQI HHHHHHHHHHHHHHH	47.98	-
139	Succinylation	IAQLEEVKQSSMKQI HHHHHHHHHHHHHHH	47.98	26388266
144	Acetylation	EVKQSSMKQIQDAID HHHHHHHHHHHHHHH	46.31	23864654
144	Ubiquitination	EVKQSSMKQIQDAID HHHHHHHHHHHHHHH	46.31	-
144	Succinylation	EVKQSSMKQIQDAID HHHHHHHHHHHHHHH	46.31	23806337
154	Succinylation	QDAIDMEKAQQALVQ HHHHHHHHHHHHHHH	44.87	24315375
154	Acetylation	QDAIDMEKAQQALVQ HHHHHHHHHHHHHHH	44.87	23576753
162	Malonylation	AQQALVQKRHYLFDV HHHHHHHHHHHCHHH	33.39	26320211
162	Acetylation	AQQALVQKRHYLFDV HHHHHHHHHHHCHHH	33.39	23576753
162	Succinylation	AQQALVQKRHYLFDV HHHHHHHHHHHCHHH	33.39	26388266
165	Phosphorylation	ALVQKRHYLFDVQRN HHHHHHHHCHHHHCC	17.07	25195567
188	Acetylation	TYRERLHKAYKEVKN HHHHHHHHHHHHHHH	58.99	23201123
191	Acetylation	ERLHKAYKEVKNRLD HHHHHHHHHHHHHHH	61.97	23864654
191	Succinylation	ERLHKAYKEVKNRLD HHHHHHHHHHHHHHH	61.97	26388266
194	Acetylation	HKAYKEVKNRLDYHI HHHHHHHHHHHHHHH	37.12	23201123
221	Acetylation	HMIDWVEKHVVKSIS HHHHHHHHHHHHCCC	31.89	23576753
221	Succinylation	HMIDWVEKHVVKSIS HHHHHHHHHHHHCCC	31.89	24315375
225	Succinylation	WVEKHVVKSISVQQE HHHHHHHHCCCHHHC	40.77	23806337
225	Malonylation	WVEKHVVKSISVQQE HHHHHHHHCCCHHHC	40.77	26320211
225	Ubiquitination	WVEKHVVKSISVQQE HHHHHHHHCCCHHHC	40.77	-
225	Acetylation	WVEKHVVKSISVQQE HHHHHHHHCCCHHHC	40.77	23576753
226	Phosphorylation	VEKHVVKSISVQQEK HHHHHHHCCCHHHCH	14.42	29895711
228	Phosphorylation	KHVVKSISVQQEKET HHHHHCCCHHHCHHH	22.44	29895711
233	Malonylation	SISVQQEKETIAKCI CCCHHHCHHHHHHHH	56.68	26320211
233	Ubiquitination	SISVQQEKETIAKCI CCCHHHCHHHHHHHH	56.68	-
233	Succinylation	SISVQQEKETIAKCI CCCHHHCHHHHHHHH	56.68	23806337
233	Acetylation	SISVQQEKETIAKCI CCCHHHCHHHHHHHH	56.68	23576753
238	Ubiquitination	QEKETIAKCIEDLKL HCHHHHHHHHHHHHH	31.71	-
238	Acetylation	QEKETIAKCIEDLKL HCHHHHHHHHHHHHH	31.71	23864654
239	S-nitrosocysteine	EKETIAKCIEDLKLL CHHHHHHHHHHHHHH	2.81	-
239	S-nitrosylation	EKETIAKCIEDLKLL CHHHHHHHHHHHHHH	2.81	21278135
244	Acetylation	AKCIEDLKLLAKKAQ HHHHHHHHHHHHHHH	54.50	23576753
244	Succinylation	AKCIEDLKLLAKKAQ HHHHHHHHHHHHHHH	54.50	24315375
248	Acetylation	EDLKLLAKKAQAQPI HHHHHHHHHHHCCCC	48.92	23201123

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

Oops, there are no upstream regulatory protein records of AT5F1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AT5F1_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 AT5F1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of AT5F1_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-115; LYS-131; LYS-162;LYS-188; LYS-221; LYS-225 AND LYS-233, AND MASS SPECTROMETRY.
PubMed: 16916647