RL32A_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL32A_SCHPO
• UniProt AC: P79015
• Protein Name: 60S ribosomal protein L32-A
• Gene Name: rpl3202
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 127
• Protein Sequence: MAAVNIIKKRTKPFKRHQSDRFKRVGESWRKPRGIDSCVRRRFRGTISMPKIGYGNNKKTRYCMPNGLKAFLVRNVSDVELLLMHNKTYAAEIAGNVSARKRVEIVEKARALGVKVTNAGAKVRSQE

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
77	Phosphorylation	AFLVRNVSDVELLLM EEEEECCCHHHHHHH	39.22	28889911

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

Oops, there are no upstream regulatory protein records of RL32A_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL32A_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 RL32A_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DED1_SCHPO	sum3	physical	19682301
RL32B_SCHPO	rpl3201	genetic	23577148
YGNB_SCHPO	nap2	physical	23695164
YGNB_SCHPO	nap2	physical	26771498

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-77, AND MASSSPECTROMETRY.
PubMed: 18257517