VAP11_ARATH - dbPTM
VAP11_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAP11_ARATH
UniProt AC Q8VZ95
Protein Name Vesicle-associated protein 1-1
Gene Name PVA11
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 256
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type IV membrane protein . Protein storage vacuole membrane
Single-pass type IV membrane protein
Cytoplasmic side . Localizes to immobile punctate structures reminiscent of the ER-plasma membrane conta
Protein Description Part of a membrane-cytoskeletal adapter complex that forms a bridge between the endoplasmic reticulum and the plasma membrane. Associates with microtubules..
Protein Sequence MSNIDLIGMSNRDLIGMSNSELLTVEPLDLQFPFELKKQISCSLYLTNKTDNNVAFKVKTTNPKKYCVRPNTGVVLPRSTCEVLVTMQAQKEAPSDMQCKDKFLLQGVIASPGVTAKEVTPEMFSKEAGHRVEETKLRVTYVAPPRPPSPVHEGSEEGSSPRASVSDNGHGSEFSFERFIVDNKAGHQENTSEARALITKLTEEKQSAIQLNNRLQRELDQLRRESKKSQSGGIPFMYVLLVGLIGLILGYIMKRT
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
1Acetylation-------MSNIDLIG
-------CCCCCEEE
6.63-
2Acetylation------MSNIDLIGM
------CCCCCEEEC
42.3622223895
2Phosphorylation------MSNIDLIGM
------CCCCCEEEC
42.3627288362
111PhosphorylationLLQGVIASPGVTAKE
HHHHECCCCCCCHHH
15.8630291188
140PhosphorylationEETKLRVTYVAPPRP
EEEEEEEEEECCCCC
13.0723776212
141PhosphorylationETKLRVTYVAPPRPP
EEEEEEEEECCCCCC
7.5523776212
149PhosphorylationVAPPRPPSPVHEGSE
ECCCCCCCCCCCCCC
42.0927532006
155PhosphorylationPSPVHEGSEEGSSPR
CCCCCCCCCCCCCCC
29.5024601666
159PhosphorylationHEGSEEGSSPRASVS
CCCCCCCCCCCEECC
40.2127532006
160PhosphorylationEGSEEGSSPRASVSD
CCCCCCCCCCEECCC
29.3024601666
164PhosphorylationEGSSPRASVSDNGHG
CCCCCCEECCCCCCC
24.3519376835
166PhosphorylationSSPRASVSDNGHGSE
CCCCEECCCCCCCCC
23.9019688752
172PhosphorylationVSDNGHGSEFSFERF
CCCCCCCCCEEEEEE
29.7819376835
175PhosphorylationNGHGSEFSFERFIVD
CCCCCCEEEEEEEEE
23.3419376835

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 VAP11_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAP11_ARATH !!

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 VAP11_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NIP11_ARATHNLM1physical
21798944
TPT_ARATHAPE2physical
21798944
PLST4_ARATHPGLCTphysical
21798944
VAP11_ARATHVAPphysical
21798944
MEB2_ARATHAT5G24290physical
21798944
Y4645_ARATHAT4G26450physical
21798944
PLP9_ARATHPLP9physical
21798944
CYB5E_ARATHCB5-Ephysical
21798944
TIP22_ARATHTIP2;2physical
21798944
SYP31_ARATHSYP31physical
21798944
PIP27_ARATHPIP3physical
21798944
Y4958_ARATHAT4G09580physical
21798944
SY132_ARATHSYP132physical
21798944
NAC89_ARATHNAC089physical
21798944
ORP2A_ARATHORP2Aphysical
21798944
BAM8_ARATHBMY2physical
21798944
KMS1_ARATHAT4G14950physical
21798944
DME_ARATHDMEphysical
21952135
SUI11_ARATHAT4G27130physical
21952135
SODF1_ARATHFSD1physical
21952135
ACT2_ARATHACT2physical
21952135
SYP71_ARATHSYP71physical
23696741

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VAP11_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-155 ANDSER-160, AND MASS SPECTROMETRY.
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-155, ANDMASS SPECTROMETRY.

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