ATP5E_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5E_YEAST
• UniProt AC: P21306
• Protein Name: ATP synthase subunit epsilon, mitochondrial
• Gene Name: ATP15
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 62
• 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(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: MSAWRKAGISYAAYLNVAAQAIRSSLKTELQTASVLNRSQTDAFYTQYKNGTAASEPTPITK

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
24	Phosphorylation	VAAQAIRSSLKTELQ HHHHHHHHHHHHHHH	33.63	22369663
25	Phosphorylation	AAQAIRSSLKTELQT HHHHHHHHHHHHHHH	24.84	22369663
27	Acetylation	QAIRSSLKTELQTAS HHHHHHHHHHHHHHH	41.73	24489116
28	Phosphorylation	AIRSSLKTELQTASV HHHHHHHHHHHHHHH	47.42	22369663
32	Phosphorylation	SLKTELQTASVLNRS HHHHHHHHHHHHCHH	33.26	22369663
34	Phosphorylation	KTELQTASVLNRSQT HHHHHHHHHHCHHHC	30.44	22369663
39	Phosphorylation	TASVLNRSQTDAFYT HHHHHCHHHCHHHHH	36.04	24961812
41	Phosphorylation	SVLNRSQTDAFYTQY HHHCHHHCHHHHHHH	30.46	28889911
46	Phosphorylation	SQTDAFYTQYKNGTA HHCHHHHHHHCCCCC	20.97	24961812
49	Acetylation	DAFYTQYKNGTAASE HHHHHHHCCCCCCCC	38.80	24489116
52	Phosphorylation	YTQYKNGTAASEPTP HHHHCCCCCCCCCCC	28.57	28889911

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

Oops, there are no upstream regulatory protein records of ATP5E_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5E_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ATP5E_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIN4_YEAST	CIN4	genetic	17322879
SRS2_YEAST	SRS2	genetic	21459050
ATPO_YEAST	ATP5	physical	22940862
ATPG_YEAST	ATP3	physical	22940862
ATPB_YEAST	ATP2	physical	22940862
ATP7_YEAST	ATP7	physical	22940862
ATPF_YEAST	ATP4	physical	22940862
ATPA_YEAST	ATP1	physical	22940862

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, AND MASSSPECTROMETRY.
PubMed: 17761666