RS21B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS21B_YEAST
• UniProt AC: Q3E754
• Protein Name: 40S ribosomal protein S21-B {ECO:0000303|PubMed:9559554}
• Gene Name: RPS21B {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 87
• 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. [PubMed: 22096102 eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability]
• Protein Sequence: MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYITYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR

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
1	Acetylation	-------MENDKGQL -------CCCCCCCE	11.09	10601260
5	Acetylation	---MENDKGQLVELY ---CCCCCCCEEEEE	61.20	-
5	Ubiquitination	---MENDKGQLVELY ---CCCCCCCEEEEE	61.20	24961812
12	Phosphorylation	KGQLVELYVPRKCSA CCCEEEEECCCCCCC	8.56	19823750
18	Phosphorylation	LYVPRKCSATNRIIK EECCCCCCCCCCEEE	40.96	21551504
20	Phosphorylation	VPRKCSATNRIIKAD CCCCCCCCCCEEECC	14.56	21440633
25	2-Hydroxyisobutyrylation	SATNRIIKADDHASV CCCCCEEECCCCCEE	43.31	-
25	Ubiquitination	SATNRIIKADDHASV CCCCCEEECCCCCEE	43.31	24961812
31	Phosphorylation	IKADDHASVQINVAK EECCCCCEEEEEEEE	15.90	24961812
38	Ubiquitination	SVQINVAKVDEEGRA EEEEEEEEECCCCCC	46.03	23749301
61	Phosphorylation	ALSGYVRSRGESDDS HHHHHHHCCCCCHHH	34.29	22369663
65	Phosphorylation	YVRSRGESDDSLNRL HHHCCCCCHHHHHHH	49.93	22369663
68	Phosphorylation	SRGESDDSLNRLAQN CCCCCHHHHHHHHHH	32.31	22369663
80	Ubiquitination	AQNDGLLKNVWSYSR HHHCCHHHHHHHHCC	55.27	23749301
84	Phosphorylation	GLLKNVWSYSR---- CHHHHHHHHCC----	14.67	19823750
85	Phosphorylation	LLKNVWSYSR----- HHHHHHHHCC-----	7.86	20377248
86	Phosphorylation	LKNVWSYSR------ HHHHHHHCC------	26.46	25521595

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

Oops, there are no upstream regulatory protein records of RS21B_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS21B_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 RS21B_YEAST !!

Protein-Protein Interaction

Oops, there are no PPI records of RS21B_YEAST !!

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: ACETYLATION AT MET-1 BY NATB.
PubMed: 10601260

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-65; SER-68; SER-84 ANDSER-86, AND MASS SPECTROMETRY.
PubMed: 18407956

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.
PubMed: 17563356

"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND MASSSPECTROMETRY.
PubMed: 15665377