ATPD_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPD_MOUSE
• UniProt AC: Q9D3D9
• Protein Name: ATP synthase subunit delta, mitochondrial {ECO:0000305}
• Gene Name: Atp5f1d {ECO:0000250|UniProtKB:P30049}
• Organism: Mus musculus (Mouse).
• Sequence Length: 168
• 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 turnover 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 of the central stalk which is part of the complex rotary element. 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: MLPASLLRHPGLRRLMLQARTYAEAAAAPAPAAGPGQMSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE

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
136	Acetylation	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	23576753
136	Succinylation	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	-
136	Ubiquitination	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	-
136	Succinylation	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	23806337
136	Malonylation	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	26320211
136	Glutarylation	AARANLEKAQSELSG HHHHHHHHHHHHHHH	55.69	24703693
139	Phosphorylation	ANLEKAQSELSGAAD HHHHHHHHHHHHHHH	45.42	23140645
142	Phosphorylation	EKAQSELSGAADEAA HHHHHHHHHHHHHHH	23.49	27742792
165	Acetylation	EANEALVKALE---- HHHHHHHHHHC----	48.37	23576753
165	Succinylation	EANEALVKALE---- HHHHHHHHHHC----	48.37	-
165	Succinylation	EANEALVKALE---- HHHHHHHHHHC----	48.37	23806337

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPD_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 ATPD_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ATPD_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"A proteomics approach to identify the ubiquitinated proteins in mouseheart.";
Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.;
Biochem. Biophys. Res. Commun. 357:731-736(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136, AND MASSSPECTROMETRY.
PubMed: 17451654