RR31_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RR31_ARATH
• UniProt AC: O80439
• Protein Name: 30S ribosomal protein S31, chloroplastic
• Gene Name: RPS31
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 118
• Subcellular Localization: Plastid, chloroplast.
• Protein Sequence: MASLILGAPPRVTVALPSSRLSSSHSETAGVSLSCFTHQFSLSTSSSSSIPLVYCGRGDRKTAKGKRFNHSFGNARPRNKSKGRGPERVPVPPAPPRKDKFENDEKIKIDIDESLFSN

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
114	Phosphorylation	IKIDIDESLFSN--- CCCCCCHHHHCC---	30.85	19376835
117	Phosphorylation	DIDESLFSN------ CCCHHHHCC------	47.09	30291188

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RR31_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RR31_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RR31_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MBD2_ARATH	MBD02	physical	21798944
BOI_ARATH	RING	physical	21798944

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-117, AND MASSSPECTROMETRY.
PubMed: 19376835