ATPB_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPB_SCHPO
• UniProt AC: P22068
• Protein Name: ATP synthase subunit beta, mitochondrial
• Gene Name: atp2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 525
• 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..
• Protein Sequence: MLKKQALSGIRRFSLATKQSFVKTSYKLPRKSWLNTAKFNTIRYASTEAAKHNKGSIKQVIGAVVDCQFEDADSLPSILNALEVKLPDNKRLVLEVAQHVGENTVRTIAMDGTEGLVRGTAVIDTGSPISIPVGPGTLGRIMNVIGEPVDERGPIKAVKYSPIHADAPSFEEQSTTPEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGYSVFTGVGERTREGNDLYREMQETGVIKLEGESKAALVFGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGAMQERITTTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSISELGIYPAVDPLDSKSRMMDPRILGEEHYNLAGSVQQMLQEYKSLQDIIAILGMDELSEADKLTVERARKVQRFLSQPFAVAEVFTGIEGRLVSLKDTIRSFKEILEGKHDSLPESAFYMVGSIDDAVKKAEKIAQELAA

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
384	Phosphorylation	ATTVLSRSISELGIY HHHHHCCHHHHHCCC	27.39	25720772
386	Phosphorylation	TVLSRSISELGIYPA HHHCCHHHHHCCCCC	28.19	25720772
391	Phosphorylation	SISELGIYPAVDPLD HHHHHCCCCCCCCCC	5.37	25720772
401	Phosphorylation	VDPLDSKSRMMDPRI CCCCCCCCCCCCHHH	29.38	25720772

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPB_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 ATPB_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of ATPB_SCHPO !!

Drug and Disease Associations

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