ATPA_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPA_SCHPO
• UniProt AC: P24487
• Protein Name: ATP synthase subunit alpha, mitochondrial
• Gene Name: atp1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 536
• Subcellular Localization: Mitochondrion. 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: MLRQAGTRLLKVPVCGLRPSITLKRGYAEKAAPTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKRWNNSSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEFLSSF

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
220	Phosphorylation	NHKRWNNSSDESKKL CCCCCCCCCHHHCEE	35.63	21712547
239	Phosphorylation	VAVGQKRSTVAQLVQ EEECCCHHHHHHHHH	33.98	25720772
240	Phosphorylation	AVGQKRSTVAQLVQK EECCCHHHHHHHHHH	24.72	25720772
534	Phosphorylation	AVIKEFLSSF----- HHHHHHHHCC-----	34.71	25720772

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

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

Functions of PTM Sites

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

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_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of ATPA_SCHPO !!

Drug and Disease Associations

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