VA0D1_MOUSE - dbPTM
VA0D1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VA0D1_MOUSE
UniProt AC P51863
Protein Name V-type proton ATPase subunit d 1
Gene Name Atp6v0d1
Organism Mus musculus (Mouse).
Sequence Length 351
Subcellular Localization Membrane
Peripheral membrane protein
Cytoplasmic side . Localizes to centrosome and the base of the cilium..
Protein Description Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity)..
Protein Sequence MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDKLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
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
24UbiquitinationEGLVRGLKAGVLSQA
HHHHHHHHHCCCCHH
46.01-
39GlutathionylationDYLNLVQCETLEDLK
HHHCCEECCCHHHHH
3.1724333276
39S-palmitoylationDYLNLVQCETLEDLK
HHHCCEECCCHHHHH
3.1728680068
51PhosphorylationDLKLHLQSTDYGNFL
HHHHHHHCCCHHHHH
29.6129899451
63PhosphorylationNFLANEASPLTVSVI
HHHCCCCCCCEEEEE
17.7929899451
66PhosphorylationANEASPLTVSVIDDK
CCCCCCCEEEEECHH
17.7029899451
68PhosphorylationEASPLTVSVIDDKLK
CCCCCEEEEECHHHH
14.2329899451
73UbiquitinationTVSVIDDKLKEKMVV
EEEEECHHHHHHHHE
58.6822790023
121PhosphorylationTGTLHQRSIAELVPK
HCCCCHHCHHHHCCC
21.4122817900
187UbiquitinationIIRNTLYKAYLESFY
HHHHHHHHHHHHHHH
33.4022790023
197S-palmitoylationLESFYKFCTLLGGTT
HHHHHHHHHHHCCCC
1.9928680068
248PhosphorylationFPHCGRLYPEGLAQL
CCCCCCCCHHHHHHH
9.6222324799
265UbiquitinationADDYEQVKNVADYYP
CCCHHHHHCHHHHCH
45.4522790023
270PhosphorylationQVKNVADYYPEYKLL
HHHCHHHHCHHHHHH
15.9322817900
275UbiquitinationADYYPEYKLLFEGAG
HHHCHHHHHHHCCCC
36.7322790023
283PhosphorylationLLFEGAGSNPGDKTL
HHHCCCCCCCCCCCH
39.0425521595
288UbiquitinationAGSNPGDKTLEDRFF
CCCCCCCCCHHHHHH
62.0122790023
335GlutathionylationNIVWIAECIAQRHRA
HHHHHHHHHHHHHHH
2.0024333276
335S-palmitoylationNIVWIAECIAQRHRA
HHHHHHHHHHHHHHH
2.0028526873
343UbiquitinationIAQRHRAKIDNYIPI
HHHHHHHHHHCCCCC
51.0222790023
347PhosphorylationHRAKIDNYIPIF---
HHHHHHCCCCCC---
12.3429514104

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 VA0D1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VA0D1_MOUSE !!

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 VA0D1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VA0D1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VA0D1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, AND MASSSPECTROMETRY.

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