ATPB_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPB_DROME
• UniProt AC: Q05825
• Protein Name: ATP synthase subunit beta, mitochondrial
• Gene Name: ATPsynbeta {ECO:0000312|FlyBase:FBgn0010217}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 505
• 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: MFALRAASKADKNLLPFLGQLSRSHAAKAAKAAAAANGKIVAVIGAVVDVQFDDNLPPILNALEVDNRSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRLAKEAA

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
101	Acetylation	EGLVRGQKVLDTGYP CCEECCEEEECCCCC	47.81	21791702
175	Acetylation	DLLAPYAKGGKIGLF HHHHCCCCCCEEEEE	63.45	21791702
403	Acetylation	NVARGVQKILQDYKS HHHHHHHHHHHHHHH	42.87	21791702
442	Phosphorylation	RKIQRFLSQPFQVAE HHHHHHHCCCCEEEE	32.85	21082442

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

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TLL_DROME	tll	physical	14605208
ACT5_DROME	Act87E	physical	14605208
CANB1_DROME	CanB	physical	14605208
NOC_DROME	noc	physical	14605208
ATPA_DROME	blw	physical	22036573
PDI_DROME	Pdi	physical	22036573
NLP_DROME	Nlp	physical	22036573
ATP5J_DROME	ATPsyn-Cf6	physical	22036573
SH3BG_DROME	Sh3beta	physical	22036573
ATPO_DROME	Oscp	physical	22036573
MYSA_DROME	Mhc	physical	22036573
NACA_DROME	Nacalpha	physical	22036573
FKB12_DROME	FK506-bp2	physical	22036573

Drug and Disease Associations

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