ATPA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPA_DROME
• UniProt AC: P35381
• Protein Name: ATP synthase subunit alpha, mitochondrial
• Gene Name: blw
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 552
• Subcellular Localization: Mitochondrion inner membrane. Peripheral 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. Subunits alpha and beta form the catalytic core in F(1). 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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)..
• Protein Sequence: MSIFSARLASSVARNLPKAANQVACKAAYPAASLAARKLHVASTQRSAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEAQDESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTIAKDGAISEASDAKLKDIVAKFMSTFQG

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
47	Phosphorylation	HVASTQRSAEISNIL HHHCCCCCHHHHHHH	22.04	19429919
64	Acetylation	RILGVAPKADLEETG HHHCCCCCCCHHHHC	44.81	21791702
160	Acetylation	LGNAIDGKGAINTKD HHHHHCCCCCCCCCC	41.23	21791702
160	Ubiquitination	LGNAIDGKGAINTKD HHHHHCCCCCCCCCC	41.23	31113955
183	Phosphorylation	PGIIPRVSVREPMQT CCCCCCEECCCCCCC	19.41	22817900
239	Acetylation	NEAQDESKKLYCIYV HCCCHHHCCEEEEEE	44.76	21791702
423	Acetylation	VGSAAQTKAMKQVAG CCHHHHHHHHHHHHH	34.11	21791702
497	Acetylation	GVRGHLDKMDPAKIT ECCCCHHHCCHHHCH	52.11	21791702
505	Acetylation	MDPAKITKFEKEFLQ CCHHHCHHHHHHHHH	55.81	21791702
508	Acetylation	AKITKFEKEFLQHIK HHCHHHHHHHHHHHH	57.82	21791702
540	Acetylation	EASDAKLKDIVAKFM HHCHHHHHHHHHHHH	44.71	21791702

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATPG_DROME	ATPsyn-gamma	physical	22036573
ATPO_DROME	Oscp	physical	22036573
ATP5J_DROME	ATPsyn-Cf6	physical	22036573
AT5F1_DROME	ATPsyn-b	physical	22036573
ATP5H_DROME	ATPsyn-d	physical	22036573
ATPK_DROME	CG4692	physical	22036573
FAXC_DROME	fax	physical	22036573
TFDP_DROME	Dp	genetic	10225996
E2F1_DROME	E2f	genetic	10225996
ATPK_DROME	CG4692	physical	25023514
ATPB_DROME	ATPsyn-beta	physical	25023514

Drug and Disease Associations

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