RLA1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RLA1_YEAST
• UniProt AC: P05318
• Protein Name: 60S acidic ribosomal protein P1-alpha {ECO:0000303|PubMed:9559554}
• Gene Name: RPP1A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 106
• Subcellular Localization: Cytoplasm .
• 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: MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD

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
2	Acetylation	------MSTESALSY ------CCHHHHHHH	40.66	8476850
2	Phosphorylation	------MSTESALSY ------CCHHHHHHH	40.66	30377154
3	Phosphorylation	-----MSTESALSYA -----CCHHHHHHHH	32.43	30377154
5	Phosphorylation	---MSTESALSYAAL ---CCHHHHHHHHHH	34.30	30377154
62	Phosphorylation	KDLLVNFSAGAAAPA HHHHHHCCCCCCCCC	22.16	24909858
96	Phosphorylation	EEEAKEESDDDMGFG HHHHHHHCCCCCCCC	47.64	25521595

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

Oops, there are no upstream regulatory protein records of RLA1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RLA1_YEAST !!

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_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RLA4_YEAST	RPP2B	physical	20225338
RLA4_YEAST	RPP2B	physical	17040491
RLA1_YEAST	RPP1A	physical	17040491
RLA4_YEAST	RPP2B	genetic	21247875
RLA4_YEAST	RPP2B	physical	21247875
RLA4_YEAST	RPP2B	physical	12653543
RLA4_YEAST	RPP2B	physical	21907821
RLA0_YEAST	RPP0	genetic	22275522
RLA3_YEAST	RPP1B	genetic	22377630
RL36A_YEAST	RPL36A	genetic	29158977

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
PubMed: 10601260

"The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes.NH2-terminal acetylation is a conserved difference between P1 and P2proteins.";
Santos C., Ortiz-Reyes B., Naranda T., Remacha M., Ballesta J.P.G.;
Biochemistry 32:4231-4236(1993).
Cited for: PROTEIN SEQUENCE OF 2-5, ACETYLATION AT SER-2, AND PHOSPHORYLATION.
PubMed: 8476850

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
PubMed: 18407956

"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
PubMed: 17330950

"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASSSPECTROMETRY.
PubMed: 11875433