RS12_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS12_YEAST
• UniProt AC: P48589
• Protein Name: 40S ribosomal protein S12 {ECO:0000303|PubMed:9559554}
• Gene Name: RPS12 {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 143
• 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: MSDVEEVVEVQEETVVEQTAEVTIEDALKVVLRTALVHDGLARGLRESTKALTRGEALLVVLVSSVTEANIIKLVEGLANDPENKVPLIKVADAKQLGEWAGLGKIDREGNARKVVGASVVVVKNWGAETDELSMIMEHFSQQ

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	Phosphorylation	------MSDVEEVVE ------CCCHHHHEE	50.82	24909858
14	Phosphorylation	VVEVQEETVVEQTAE HEEECCCEEEEEEEE	29.15	28132839
34	Phosphorylation	ALKVVLRTALVHDGL HHHHHHHHHHHHHHH	21.85	24909858
50	Ubiquitination	RGLRESTKALTRGEA HHHHHHHHHCHHCCE	51.16	22817900
64	Phosphorylation	ALLVVLVSSVTEANI EEEEEECCCCCHHHH	18.22	17287358
65	Phosphorylation	LLVVLVSSVTEANII EEEEECCCCCHHHHH	26.11	17287358
73	Ubiquitination	VTEANIIKLVEGLAN CCHHHHHHHHHHHHC	42.56	15699485
85	2-Hydroxyisobutyrylation	LANDPENKVPLIKVA HHCCCCCCCCEEEEE	43.50	-
85	Ubiquitination	LANDPENKVPLIKVA HHCCCCCCCCEEEEE	43.50	23749301
85	Acetylation	LANDPENKVPLIKVA HHCCCCCCCCEEEEE	43.50	24489116
90	2-Hydroxyisobutyrylation	ENKVPLIKVADAKQL CCCCCEEEEECHHHH	38.77	-
90	Ubiquitination	ENKVPLIKVADAKQL CCCCCEEEEECHHHH	38.77	23749301
90	Acetylation	ENKVPLIKVADAKQL CCCCCEEEEECHHHH	38.77	24489116
95	2-Hydroxyisobutyrylation	LIKVADAKQLGEWAG EEEEECHHHHHCCCC	46.75	-
95	Ubiquitination	LIKVADAKQLGEWAG EEEEECHHHHHCCCC	46.75	23749301
95	Succinylation	LIKVADAKQLGEWAG EEEEECHHHHHCCCC	46.75	23954790
95	Acetylation	LIKVADAKQLGEWAG EEEEECHHHHHCCCC	46.75	24489116
105	Succinylation	GEWAGLGKIDREGNA HCCCCCCEECCCCCC	46.61	23954790
105	Ubiquitination	GEWAGLGKIDREGNA HCCCCCCEECCCCCC	46.61	23749301
105	Acetylation	GEWAGLGKIDREGNA HCCCCCCEECCCCCC	46.61	24489116
105	2-Hydroxyisobutyrylation	GEWAGLGKIDREGNA HCCCCCCEECCCCCC	46.61	-
114	Ubiquitination	DREGNARKVVGASVV CCCCCCEEEECEEEE	38.57	23749301
114	Acetylation	DREGNARKVVGASVV CCCCCCEEEECEEEE	38.57	23572591
114	2-Hydroxyisobutyrylation	DREGNARKVVGASVV CCCCCCEEEECEEEE	38.57	-
119	Phosphorylation	ARKVVGASVVVVKNW CEEEECEEEEEEECC	14.98	19684113
124	Acetylation	GASVVVVKNWGAETD CEEEEEEECCCCCHH	35.06	23572591
124	Ubiquitination	GASVVVVKNWGAETD CEEEEEEECCCCCHH	35.06	15699485
130	Phosphorylation	VKNWGAETDELSMIM EECCCCCHHHHHHHH	33.95	28889911
134	Phosphorylation	GAETDELSMIMEHFS CCCHHHHHHHHHHHH	12.29	21440633
141	Phosphorylation	SMIMEHFSQQ----- HHHHHHHHCC-----	29.58	30377154

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

Oops, there are no upstream regulatory protein records of RS12_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS12_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 RS12_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPT4_YEAST	SPT4	genetic	19325107
GGPPS_YEAST	BTS1	genetic	19325107
SSH1_YEAST	SSH1	genetic	19325107

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

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 AND SER-119, AND MASSSPECTROMETRY.
PubMed: 18407956

"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-65, AND MASSSPECTROMETRY.
PubMed: 17287358