RLA1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RLA1_DROME
• UniProt AC: P08570
• Protein Name: 60S acidic ribosomal protein P1
• Gene Name: RpLP1
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 112
• Protein Description: Plays an important role in the elongation step of protein synthesis..
• Protein Sequence: MSTKAELACVYASLILVDDDVAVTGEKINTILKAANVEVEPYWPGLFAKALEGINVKDLITNIGSGVGAAPAGGAAPAAAAAAPAAESKKEEKKKEEESDQSDDDMGFGLFD

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
65	Phosphorylation	DLITNIGSGVGAAPA HHHHHCCCCCCCCCC	26.89	22817900
88	Phosphorylation	AAAPAAESKKEEKKK HHCHHHHHHHHHHHH	44.28	22817900
99	Phosphorylation	EKKKEEESDQSDDDM HHHHHHHCCCCCCCC	44.20	21082442
102	Phosphorylation	KEEESDQSDDDMGFG HHHHCCCCCCCCCCC	48.25	21082442

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

Oops, there are no upstream regulatory protein records of RLA1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RLA1_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RLA1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RLA0_DROME	RpLP0	physical	14605208
DEI_DROME	tx	physical	14605208
ESM7_DROME	E(spl)m7-HLH	physical	14605208
TCPG_DROME	Cctgamma	physical	14605208

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-102, AND MASSSPECTROMETRY.
PubMed: 18327897