ATPB_CAEEL - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPB_CAEEL
• UniProt AC: P46561
• Protein Name: ATP synthase subunit beta, mitochondrial
• Gene Name: atp-2
• Organism: Caenorhabditis elegans.
• Sequence Length: 538
• Subcellular Localization: Cell projection, cilium . Mitochondrion . Mitochondrion inner membrane . Peripheral membrane protein. Localizes to the cilium only in male-specific sensory neurons.
• 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. Required during male mating behavior for the response to hermaphrodite contact, acting with lov-1 and pkd-2. May be involved in polycystin signaling..
• Protein Sequence: MASRSLASISRSASRLLQSNVQKCALPAASIRLSSNNVESKKGIHTGVATQQAAAATKVSAKATAANASGRIVAVIGAVVDVQFDENLPPILNGLEVVGRSPRLILEVSQHLGDNVVRCIAMDGTEGLVRGQPVADTGDPIKIPVGPETLGRIMNVIGEPIDERGPIASKNFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIEGGVIDLKGKNSKVSLVYGQMNEPPGARARVCLTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRGIAELAIYPAVDPLDSTSRIMDPNVVGQNHYDIARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHQGKFVSLEETIRGFTMILKGELDHLPEVAFYMQGGIDDVFKKAEELAKQHGN

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
149	Phosphorylation	KIPVGPETLGRIMNV EECCCHHHHHHHHHH	37.33	28854356
239	Phosphorylation	VAKAHGGYSVFAGVG HHHHCCCEEEEECCC	13.27	27067626
474	Phosphorylation	RKIQRFLSQPFQVAE HHHHHHHCCCEEEEE	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_CAEEL !!

Functions of PTM Sites

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

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_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KLHL8_CAEEL	kel-8	physical	14992718
YUA6_CAEEL	F13D12.6	physical	14992718
RSSA_CAEEL	rps-0	physical	14992718

Drug and Disease Associations

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