VATF1_DROME - dbPTM
VATF1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATF1_DROME
UniProt AC Q24583
Protein Name V-type proton ATPase subunit F 1
Gene Name Vha14-1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 124
Subcellular Localization
Protein Description Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells..
Protein Sequence MALHSAIKGKLISVIGDEDTCVGFLLGGVGEINKNRHPNFMVVDKNTAVSELEDCFKRFLKRDDIDIILINQNCAELIRHVIDAHTSPVPAVLEIPSKDHPYDASKDSILRRARGMFNPEDLVR
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
86PhosphorylationRHVIDAHTSPVPAVL
HHHHHCCCCCCCCEE
36.1219429919
87PhosphorylationHVIDAHTSPVPAVLE
HHHHCCCCCCCCEEE
17.6519429919

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 VATF1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATF1_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 VATF1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATE_DROMEVha26physical
22036573
VATD1_DROMEVha36-1physical
22036573
VA0D1_DROMEVhaAC39-1physical
22036573
VATC_DROMEVha44physical
22036573
VATA2_DROMEVha68-2physical
22036573
VATA1_DROMEVha68-1physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VATF1_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-87, AND MASSSPECTROMETRY.

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