dbPTM

RL5A_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL5A_SCHPO
UniProt AC	P52822
Protein Name	60S ribosomal protein L5-A
Gene Name	rpl501
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	294
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel..
Protein Sequence	MPFIKAVKSSPYFSRYQTKYRRRREGKTDYYARKRLIAQAKNKYNAPKYRLVVRFSNRFVTCQIVSSRVNGDYVLAHAHSSELPRYGIKWGLANWTAAYATGLLVARRALAKVGLADKYEGVTEPEGEFELTEAIEDGPRPFKVFLDVGLKRTSTGSRVFGAMKGASDGGLFIPHSPNRFPGFDIETEELDDETLRKYIYGGHVAEYMEMLIDDDEERYQKQFSGLIADGIESDQLEDIYAEAYAKIREDPSFQKSGKDAAAFKAESLKHTQRKLTAEERKERFNAKVIEAGRA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	PFIKAVKSSPYFSRY CCCHHHHCCCCCHHH	29.91	28889911
10	Phosphorylation	FIKAVKSSPYFSRYQ CCHHHHCCCCCHHHH	20.22	28889911
12	Phosphorylation	KAVKSSPYFSRYQTK HHHHCCCCCHHHHHH	19.01	28889911
67	Phosphorylation	VTCQIVSSRVNGDYV EEEEEEECCCCCCEE	29.38	25720772
73	Phosphorylation	SSRVNGDYVLAHAHS ECCCCCCEEEEEEEC	9.96	25720772
81	Phosphorylation	VLAHAHSSELPRYGI EEEEEECCCCCCCCH	33.03	28889911
123	Phosphorylation	ADKYEGVTEPEGEFE CCCCCCCCCCCCEEE	57.59	21712547
132	Phosphorylation	PEGEFELTEAIEDGP CCCEEEEEHHHCCCC	19.04	24763107
153	Phosphorylation	LDVGLKRTSTGSRVF EEECEEECCCCCHHH	29.11	24763107
157	Phosphorylation	LKRTSTGSRVFGAMK EEECCCCCHHHCCCC	25.92	27738172
167	Phosphorylation	FGAMKGASDGGLFIP HCCCCCCCCCCEECC	45.52	28889911
176	Phosphorylation	GGLFIPHSPNRFPGF CCEECCCCCCCCCCC	20.65	28889911
187	Phosphorylation	FPGFDIETEELDDET CCCCCCCCCCCCHHH	34.78	29996109
256	Phosphorylation	EDPSFQKSGKDAAAF CCHHHHHCCCHHHHH	40.05	25720772

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of RL5A_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL5A_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RL5A_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RL5A_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of RL5A_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-10; TYR-12 AND SER-81,AND MASS SPECTROMETRY.	18257517 [Abstract]