dbPTM

P2C22_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P2C22_ARATH
UniProt AC	Q9SLA1
Protein Name	Probable protein phosphatase 2C 22
Gene Name	At2g25620
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	392
Subcellular Localization
Protein Description
Protein Sequence	MEETRGISDPENGSSSYGGKPPNPLSFSSSSAAAAVYRQTFDGERSLAPCNKRSLVRHSSLVKTMVSDISVENEFTIEKNKSEFVPATRSGAWSDIGSRSSMEDAYLCVDNFMDSFGLLNSEAGPSAFYGVFDGHGGKHAAEFACHHIPRYIVEDQEFPSEINKVLSSAFLQTDTAFLEACSLDGSLASGTTALAAILFGRSLVVANAGDCRAVLSRQGKAIEMSRDHKPMSSKERRRIEASGGHVFDGYLNGQLNVARALGDFHMEGMKKKKDGSDCGPLIAEPELMTTKLTEEDEFLIIGCDGVWDVFMSQNAVDFARRRLQEHNDPVMCSKELVEEALKRKSADNVTAVVVCLQPQPPPNLVAPRLRVHRSFSAEGLKDLQSYLDGLGN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
59	Phosphorylation	KRSLVRHSSLVKTMV CCHHHHHHHHHHHHH	18.14	28011693
60	Phosphorylation	RSLVRHSSLVKTMVS CHHHHHHHHHHHHHH	30.93	28011693
374	Phosphorylation	PRLRVHRSFSAEGLK CCEEEEECCCHHHHH	14.52	23776212
376	Phosphorylation	LRVHRSFSAEGLKDL EEEEECCCHHHHHHH	27.02	19880383

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 P2C22_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P2C22_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 P2C22_ARATH !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of P2C22_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-376, AND MASSSPECTROMETRY.	19376835 [Abstract]