RL131_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL131_ARATH
• UniProt AC: P41127
• Protein Name: 60S ribosomal protein L13-1
• Gene Name: RPL13B
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 206
• Subcellular Localization: Cytoplasm.
• Protein Sequence: MKHNNVIPNGHFKKHWQNYVKTWFNQPARKTRRRIARQKKAVKIFPRPTSGPLRPVVHGQTLKYNMKVRTGKGFTLEELKAAGIPKKLAPTIGIAVDHRRKNRSLEGLQTNVQRLKTYKTKLVIFPRRARKVKAGDSTPEELANATQVQGDYLPIVREKPTMELVKLTSEMKSFKAFDKIRLERTNKRHAGARAKRAAEAEKEEKK

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
49	Phosphorylation	VKIFPRPTSGPLRPV EEECCCCCCCCCCCE	47.82	25561503
50	Phosphorylation	KIFPRPTSGPLRPVV EECCCCCCCCCCCEE	40.89	25561503
104	Phosphorylation	DHRRKNRSLEGLQTN ECHHHCCCCHHHHHH	39.92	30291188
137	Phosphorylation	RKVKAGDSTPEELAN CCCCCCCCCHHHHHH	44.97	24601666
138	Phosphorylation	KVKAGDSTPEELANA CCCCCCCCHHHHHHH	39.19	24924143
146	Phosphorylation	PEELANATQVQGDYL HHHHHHHHCCCCCCC	29.13	23776212
152	Phosphorylation	ATQVQGDYLPIVREK HHCCCCCCCCCCCCC	22.62	19376835
173	Phosphorylation	KLTSEMKSFKAFDKI HHHHHHHHHHHHHHH	30.57	25561503

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

Oops, there are no upstream regulatory protein records of RL131_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL131_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 RL131_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of RL131_ARATH !!

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 THR-138, AND MASSSPECTROMETRY.
PubMed: 19376835