RL35_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL35_SCHPO
• UniProt AC: O74904
• Protein Name: 60S ribosomal protein L35
• Gene Name: rpl35
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 122
• Protein Sequence: MALKTFELRKQSQENLAEQLQELRQELASLRVQKIAGGSGSKLSKIKTTRKDIARILTVINESNRLAAREAYKNKKYIPLDLRQKKTRAIRRALTPYEQSRKTLKQIKKERYFPLRKYALKA

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
12	Phosphorylation	TFELRKQSQENLAEQ HHHHHHHHHHHHHHH	42.36	28889911
39	Phosphorylation	VQKIAGGSGSKLSKI HHHHHCCCCHHHHHC	38.69	21712547
41	Phosphorylation	KIAGGSGSKLSKIKT HHHCCCCHHHHHCCC	31.92	21712547
44	Phosphorylation	GGSGSKLSKIKTTRK CCCCHHHHHCCCCHH	35.75	24763107

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

Oops, there are no upstream regulatory protein records of RL35_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL35_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 RL35_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of RL35_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-12, AND MASSSPECTROMETRY.
PubMed: 18257517