RLA4_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RLA4_SCHPO
• UniProt AC: P17478
• Protein Name: 60S acidic ribosomal protein P2-beta
• Gene Name: rpp202
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 110
• Protein Description: Plays an important role in the elongation step of protein synthesis..
• Protein Sequence: MKYLAAYLLLTVGGKQSPSASDIESVLSTVGIEAEAERVESLISELNGKNIEELIAAGNEKLSTVPSAGAVATPAAGGAAGAEATSAAEEAKEEEAAEESDEDMGFGLFD

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
67	Phosphorylation	EKLSTVPSAGAVATP CCCCCCCCCCCCCCC	34.69	29996109
73	Phosphorylation	PSAGAVATPAAGGAA CCCCCCCCCCCCCHH	13.58	29996109
85	Phosphorylation	GAAGAEATSAAEEAK CHHHHHHHHHHHHHH	15.48	21712547
86	Phosphorylation	AAGAEATSAAEEAKE HHHHHHHHHHHHHHH	32.31	21712547
100	Phosphorylation	EEEAAEESDEDMGFG HHHHHHHCCCCCCCC	37.49	28889911

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

Oops, there are no upstream regulatory protein records of RLA4_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RLA4_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RLA4_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of RLA4_SCHPO !!

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 fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
PubMed: 18257517