VATA2_DROME - dbPTM
VATA2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATA2_DROME
UniProt AC Q27331
Protein Name V-type proton ATPase catalytic subunit A isoform 2
Gene Name Vha68-2
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 614
Subcellular Localization
Protein Description Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells..
Protein Sequence MSNLKRFDDEERESKYGRVFAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKDINELTESIYIPKGVNVPSLSRVASWEFNPLNVKVGSHITGGDLYGLVHENTLVKHKMIVNPRAKGTVRYIAPSGNYKVDDVVLETEFDGEITKHTMLQVWPVRQPRPVTEKLPANHPLLTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELSVEIDGVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDDFYDKNFPEFVPLRTKVKEILQEEEDLSEIVQLVGKASLAETDKITLEVAKLLKDDFLQQNSYSSYDRFCPFYKTVGMLRNIIDFYDMARHSVESTAQSENKITWNVIREAMGNIMYQLSSMKFKDPVKDGEAKIKADFEQLHEDLQQAFRNLED
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 Orthologous
Protein Cluster
126PhosphorylationGVNVPSLSRVASWEF
CCCCCCHHHCEEEEC
29.1021082442
130PhosphorylationPSLSRVASWEFNPLN
CCHHHCEEEECCCCC
25.0419429919
142PhosphorylationPLNVKVGSHITGGDL
CCCEEECCEECCCCC
18.0719429919
145PhosphorylationVKVGSHITGGDLYGL
EEECCEECCCCCHHH
29.6819429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of VATA2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATA2_DROME !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of VATA2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATD1_DROMEVha36-1physical
22036573
VATC_DROMEVha44physical
22036573
ACADM_DROMECG12262physical
22036573
VATH_DROMEVhaSFDphysical
22036573
COQ6_DROMECG7277physical
22036573
VATA1_DROMEVha68-1physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VATA2_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.

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