dbPTM

Y5566_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y5566_ARATH
UniProt AC	Q9LSK9
Protein Name	Uncharacterized protein At5g65660
Gene Name	At5g65660
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	136
Subcellular Localization	Membrane Single-pass membrane protein .
Protein Description
Protein Sequence	MENTQDFSPPHMDASRPSLGFPLGTALLLIIIFSLSGIFSCCYHWDKHRSLRRSLANGRPSADIESNPYKPKPPFPEMKKPQNLSVPVLMPGDNTPKFIALPCPCAPPRPEKLTVDVQTPPQSPPVKPARFPVPLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
119	Phosphorylation	KLTVDVQTPPQSPPV CCEEEECCCCCCCCC	36.46	30291188
123	Phosphorylation	DVQTPPQSPPVKPAR EECCCCCCCCCCCCC	36.62	30291188

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 Y5566_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y5566_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 Y5566_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Y5566_ARATH !!

Drug and Disease Associations

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

Regulatory Network of Y5566_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119 AND SER-123, ANDMASS SPECTROMETRY.	17317660 [Abstract]