ATP8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP8_MOUSE
• UniProt AC: P03930
• Protein Name: ATP synthase protein 8
• Gene Name: Mtatp8
• Organism: Mus musculus (Mouse).
• Sequence Length: 67
• Subcellular Localization: Mitochondrion membrane; Single-pass membrane protein.
• 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. Minor subunit located with subunit a in the membrane (By similarity)..
• Protein Sequence: MPQLDTSTWFITIISSMITLFILFQLKVSSQTFPLAPSPKSLTTMKVKTPWELKWTKIYLPHSLPQQ

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
41	Phosphorylation	PLAPSPKSLTTMKVK CCCCCCCCCCCCEEC	34.04	23737553
43	Phosphorylation	APSPKSLTTMKVKTP CCCCCCCCCCEECCC	31.75	23737553
44	Phosphorylation	PSPKSLTTMKVKTPW CCCCCCCCCEECCCC	21.93	23737553
46	Acetylation	PKSLTTMKVKTPWEL CCCCCCCEECCCCEE	38.19	23806337
46	Succinylation	PKSLTTMKVKTPWEL CCCCCCCEECCCCEE	38.19	23806337
46	Malonylation	PKSLTTMKVKTPWEL CCCCCCCEECCCCEE	38.19	26320211
48	Acetylation	SLTTMKVKTPWELKW CCCCCEECCCCEEEE	43.27	23864654
48	Succinylation	SLTTMKVKTPWELKW CCCCCEECCCCEEEE	43.27	23806337
48	Malonylation	SLTTMKVKTPWELKW CCCCCEECCCCEEEE	43.27	26320211
54	Acetylation	VKTPWELKWTKIYLP ECCCCEEEEEEEECC	41.10	23576753
54	Succinylation	VKTPWELKWTKIYLP ECCCCEEEEEEEECC	41.10	-
54	Succinylation	VKTPWELKWTKIYLP ECCCCEEEEEEEECC	41.10	23806337
57	Acetylation	PWELKWTKIYLPHSL CCEEEEEEEECCCCC	28.39	23576753
57	Ubiquitination	PWELKWTKIYLPHSL CCEEEEEEEECCCCC	28.39	-
57	Succinylation	PWELKWTKIYLPHSL CCEEEEEEEECCCCC	28.39	23954790
63	Phosphorylation	TKIYLPHSLPQQ--- EEEECCCCCCCC---	39.54	23737553

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

Oops, there are no upstream regulatory protein records of ATP8_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP8_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 ATP8_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ATP8_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-54, AND MASS SPECTROMETRY.
PubMed: 16916647