dbPTM

PPX1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPX1_ARATH
UniProt AC	P48529
Protein Name	Serine/threonine-protein phosphatase PP-X isozyme 1
Gene Name	PPX1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	305
Subcellular Localization	Plastid stroma .
Protein Description
Protein Sequence	MSDLDRQIGQLKRCEPLSESEVKALCLKAMEILVEESNVQRVDAPVTLCGDIHGQFYDMMELFKVGGDCPKTNYLFMGDFVDRGYYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSSNVWRYCTDIFDYMSLSAVVENKIFCVHGGLSPAIMTLDQIRTIDRKQEVPHDGAMCDLLWSDPEDIVDGWGLSPRGAGFLFGGSVVTSFNHSNNIDYIARAHQLVMEGYKWMFDSQIVTVWSAPNYCYRCGNVASILELDENLNKEFRVFDAAQQDSRGPPAKKPAPDYFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
Oops, there are no PTM records of PPX1_ARATH !!

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 PPX1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPX1_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 PPX1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PPX1_ARATH !!

Drug and Disease Associations

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

Regulatory Network of PPX1_ARATH

Related Literatures of Post-Translational Modification