dbPTM

RLA02_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RLA02_ARATH
UniProt AC	Q42112
Protein Name	60S acidic ribosomal protein P0-2
Gene Name	RPP0B
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	320
Subcellular Localization
Protein Description	Ribosomal protein P0 is the functional equivalent of E.coli protein L10..
Protein Sequence	MVKATKAEKKIAYDTKLCQLIDEYTQILVVAADNVGSTQLQNIRKGLRGDSVVLMGKNTMMKRSVRIHSENTGNTAILNLLPLLQGNVGLIFTKGDLKEVSEEVAKYKVGAPARVGLVAPIDVVVQPGNTGLDPSQTSFFQVLNIPTKINKGTVEIITPVELIKQGDKVGSSEAALLAKLGIRPFSYGLVVQSVYDNGSVFSPEVLDLTEDQLVEKFASGISMVTSLALAVSYPTLAAAPHMFINAYKNALAIAVATEYTFPQAEKVKEYLKDPSKFAVASVAAVSADAGGGAPAAAKVEEKEESDEEDYGGDFGLFDEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
259	Phosphorylation	AIAVATEYTFPQAEK HHHHHCCCCCCCHHH	14.88	19880383
260	Phosphorylation	IAVATEYTFPQAEKV HHHHCCCCCCCHHHH	23.70	19880383
281	Phosphorylation	PSKFAVASVAAVSAD HHHHHHEEEEEECCC	12.99	23111157
286	Phosphorylation	VASVAAVSADAGGGA HEEEEEECCCCCCCC	18.72	25368622
305	Phosphorylation	KVEEKEESDEEDYGG CHHHHHCCCCCCCCC	51.95	30291188
310	Phosphorylation	EESDEEDYGGDFGLF HCCCCCCCCCCCCCC	26.70	23776212

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 RLA02_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RLA02_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 RLA02_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RLA02_ARATH !!

Drug and Disease Associations

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

Regulatory Network of RLA02_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-305, AND MASSSPECTROMETRY.	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-305, AND MASSSPECTROMETRY.	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-305, AND MASSSPECTROMETRY.	18433157 [Abstract]
"Phosphoproteins analysis in plants: a proteomic approach."; Laugesen S., Messinese E., Hem S., Pichereaux C., Grat S., Ranjeva R.,Rossignol M., Bono J.-J.; Phytochemistry 67:2208-2214(2006). Cited for: PROTEIN SEQUENCE OF 299-320, AND PHOSPHORYLATION AT SER-305.	16962150 [Abstract]