RL18A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL18A_YEAST
• UniProt AC: P0CX49
• Protein Name: 60S ribosomal protein L18-A {ECO:0000303|PubMed:9559554}
• Gene Name: RPL18A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 186
• 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: MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRPPVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGECITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRRSKGFKV

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
13	Phosphorylation	TSKQHKRSGHRTAPK CCCCCCCCCCCCCCC	43.70	27717283
21	Phosphorylation	GHRTAPKSDNVYLKL CCCCCCCCCCHHHHH	33.10	28889911
27	Acetylation	KSDNVYLKLLVKLYT CCCCHHHHHHHHHHH	23.30	24489116
31	Acetylation	VYLKLLVKLYTFLAR HHHHHHHHHHHHHHH	35.43	24489116
31	Ubiquitination	VYLKLLVKLYTFLAR HHHHHHHHHHHHHHH	35.43	-
46	Acetylation	RTDAPFNKVVLKALF CCCCCHHHHHHHHHH	33.81	24489116
50	Acetylation	PFNKVVLKALFLSKI CHHHHHHHHHHHHHC	31.28	24489116
50	Methylation	PFNKVVLKALFLSKI CHHHHHHHHHHHHHC	31.28	22522802
50	Ubiquitination	PFNKVVLKALFLSKI CHHHHHHHHHHHHHC	31.28	-
50	"N6,N6,N6-trimethyllysine"	PFNKVVLKALFLSKI CHHHHHHHHHHHHHC	31.28	-
56	Acetylation	LKALFLSKINRPPVS HHHHHHHHCCCCCCC	46.26	24489116
63	Phosphorylation	KINRPPVSVSRIARA HCCCCCCCHHHHHHH	21.83	23749301
65	Phosphorylation	NRPPVSVSRIARALK CCCCCCHHHHHHHHH	15.51	23749301
72	Acetylation	SRIARALKQEGAANK HHHHHHHHHCCCCCC	45.37	25381059
72	Succinylation	SRIARALKQEGAANK HHHHHHHHHCCCCCC	45.37	23954790
72	Ubiquitination	SRIARALKQEGAANK HHHHHHHHHCCCCCC	45.37	-
86	Phosphorylation	KTVVVVGTVTDDARI CEEEEEEEECCCCEE	14.50	17287358
98	Ubiquitination	ARIFEFPKTTVAALR CEECCCCCCHHHHHH	63.25	-
98	Succinylation	ARIFEFPKTTVAALR CEECCCCCCHHHHHH	63.25	23954790
98	Acetylation	ARIFEFPKTTVAALR CEECCCCCCHHHHHH	63.25	24489116
116	Ubiquitination	GARAKIVKAGGECIT CCCEEEEEECCEEEE	44.80	22106047
133	Ubiquitination	QLAVRAPKGQNTLIL HEEEECCCCCCEEEE	72.62	-
133	Acetylation	QLAVRAPKGQNTLIL HEEEECCCCCCEEEE	72.62	24489116
137	Phosphorylation	RAPKGQNTLILRGPR ECCCCCCEEEEECCC	13.79	21126336
159	Acetylation	HFGMGPHKGKAPRIL HCCCCCCCCCCCCCC	66.30	24489116
167	Phosphorylation	GKAPRILSTGRKFER CCCCCCCCCCCHHHH	26.83	17287358
168	Phosphorylation	KAPRILSTGRKFERA CCCCCCCCCCHHHHH	37.24	19823750

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

Oops, there are no upstream regulatory protein records of RL18A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL18A_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 RL18A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYDC_YEAST	DPS1	physical	16429126
GFA1_YEAST	GFA1	physical	16429126
THDH_YEAST	ILV1	physical	16429126
MPG1_YEAST	PSA1	physical	16429126
TBA3_YEAST	TUB3	physical	16429126
RL36B_YEAST	RPL36B	physical	16429126
NOG1_YEAST	NOG1	physical	16429126
RL7A_YEAST	RPL7A	physical	16429126
RL2A_YEAST	RPL2A	physical	16429126
RL2B_YEAST	RPL2A	physical	16429126
RL10_YEAST	RPL10	physical	16429126
RL4B_YEAST	RPL4B	physical	16429126
RRP5_YEAST	RRP5	physical	16429126
RL13B_YEAST	RPL13B	physical	16429126
RS4A_YEAST	RPS4A	physical	16429126
RS4B_YEAST	RPS4A	physical	16429126
RL27A_YEAST	RPL27A	physical	16429126
RL4A_YEAST	RPL4A	physical	16429126
C1TM_YEAST	MIS1	physical	16429126
RLA0_YEAST	RPP0	physical	16429126
NSA2_YEAST	NSA2	physical	16429126
RPB4_YEAST	RPB4	physical	16429126
SYTC_YEAST	THS1	physical	16429126
IMB4_YEAST	KAP123	physical	16429126
RS3A2_YEAST	RPS1B	physical	16429126
TBB_YEAST	TUB2	physical	16429126
ARX1_YEAST	ARX1	physical	16429126
RL3_YEAST	RPL3	physical	16429126
NOG2_YEAST	NOG2	physical	16429126
NUG1_YEAST	NUG1	physical	16429126
RL5_YEAST	RPL5	physical	16429126
DED1_YEAST	DED1	physical	16429126
EIF3B_YEAST	PRT1	physical	16429126
RS3_YEAST	RPS3	physical	16429126
GBLP_YEAST	ASC1	physical	16429126
PYR1_YEAST	URA2	physical	16429126

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-86 AND SER-167, AND MASSSPECTROMETRY.
PubMed: 17287358

"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-167, AND MASSSPECTROMETRY.
PubMed: 15665377