dbPTM

VAP12_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VAP12_ARATH
UniProt AC	Q9SHC8
Protein Name	Vesicle-associated protein 1-2
Gene Name	PVA12
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	239
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type IV membrane protein Cytoplasmic side .
Protein Description	Vesicle-associated protein that binds the oxysterol-binding protein ORP3A and allows its targeting to the ER..
Protein Sequence	MSNELLTIDPVDLQFPFELKKQISCSLYLGNKTDNYVAFKVKTTNPKKYCVRPNTGVVHPRSSSEVLVTMQAQKEAPADLQCKDKFLLQCVVASPGATPKDVTHEMFSKEAGHRVEETKLRVVYVAPPRPPSPVREGSEEGSSPRASVSDNGNASDFTAAPRFSADRVDAQDNSSEARALVTKLTEEKNSAVQLNNRLQQELDQLRRESKRSKSGGIPFMYVLLVGLIGLILGYIMKRT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MSNELLTI -------CCCCCEEE	9.78	-
2	Acetylation	------MSNELLTID ------CCCCCEEEC	38.72	22223895
94	Phosphorylation	LLQCVVASPGATPKD EHHHHCCCCCCCCCH	16.56	26811356
124	Phosphorylation	ETKLRVVYVAPPRPP EEEEEEEEECCCCCC	6.50	23776212
132	Phosphorylation	VAPPRPPSPVREGSE ECCCCCCCCCCCCCC	38.42	27532006
138	Phosphorylation	PSPVREGSEEGSSPR CCCCCCCCCCCCCCC	27.93	27532006
142	Phosphorylation	REGSEEGSSPRASVS CCCCCCCCCCCCCCC	40.21	27532006
143	Phosphorylation	EGSEEGSSPRASVSD CCCCCCCCCCCCCCC	29.30	27532006
147	Phosphorylation	EGSSPRASVSDNGNA CCCCCCCCCCCCCCH	24.35	15308754
149	Phosphorylation	SSPRASVSDNGNASD CCCCCCCCCCCCHHH	23.90	30291188
155	Phosphorylation	VSDNGNASDFTAAPR CCCCCCHHHCCCCCC	36.94	30291188
158	Phosphorylation	NGNASDFTAAPRFSA CCCHHHCCCCCCCCC	27.22	19376835
164	Phosphorylation	FTAAPRFSADRVDAQ CCCCCCCCCCCCCCC	30.46	30291188
174	Phosphorylation	RVDAQDNSSEARALV CCCCCCCHHHHHHHH	37.53	25561503
175	Phosphorylation	VDAQDNSSEARALVT CCCCCCHHHHHHHHH	41.34	25561503

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 VAP12_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VAP12_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 VAP12_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ORP3A_ARATH	UNE18	physical	19207211

Drug and Disease Associations

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

Regulatory Network of VAP12_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-132; SER-138; SER-143;SER-147 AND SER-164, AND MASS SPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-149 ANDSER-164, AND MASS SPECTROMETRY.	19245862 [Abstract]
"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-132 AND SER-138, ANDMASS SPECTROMETRY.	18433157 [Abstract]
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.	15308754 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.	14506206 [Abstract]