RL19A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL19A_YEAST
• UniProt AC: P0CX82
• Protein Name: 60S ribosomal protein L19-A {ECO:0000303|PubMed:9559554}
• Gene Name: RPL19A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 189
• 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. eL19 may play a role in the last stages of translation initiation, in particular sububit joining and shedding/releasing factors..
• Protein Sequence: MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA

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	TQKRLAASVVGVGKR HHHHHHHHHHCCCCC	16.24	21440633
19	Acetylation	ASVVGVGKRKVWLDP HHHHCCCCCEEECCC	46.79	24489116
19	Ubiquitination	ASVVGVGKRKVWLDP HHHHCCCCCEEECCC	46.79	-
21	Ubiquitination	VVGVGKRKVWLDPNE HHCCCCCEEECCCCC	41.05	22106047
29	Phosphorylation	VWLDPNETSEIAQAN EECCCCCHHHHHHHH	38.00	22369663
30	Phosphorylation	WLDPNETSEIAQANS ECCCCCHHHHHHHHH	22.34	22369663
37	Phosphorylation	SEIAQANSRNAIRKL HHHHHHHHHHHHHHH	29.90	21440633
46	Ubiquitination	NAIRKLVKNGTIVKK HHHHHHHHCCCEEEE	61.16	-
52	Succinylation	VKNGTIVKKAVTVHS HHCCCEEEEEEEECC	31.03	23954790
53	Ubiquitination	KNGTIVKKAVTVHSK HCCCEEEEEEEECCH	36.88	22106047
56	Phosphorylation	TIVKKAVTVHSKSRT CEEEEEEEECCHHHC	19.84	27717283
59	Phosphorylation	KKAVTVHSKSRTRAH EEEEEECCHHHCCHH	28.17	27214570
60	Ubiquitination	KAVTVHSKSRTRAHA EEEEECCHHHCCHHH	29.13	22106047
60	Acetylation	KAVTVHSKSRTRAHA EEEEECCHHHCCHHH	29.13	24489116
61	Phosphorylation	AVTVHSKSRTRAHAQ EEEECCHHHCCHHHH	41.73	23749301
63	Phosphorylation	TVHSKSRTRAHAQSK EECCHHHCCHHHHHH	39.02	19823750
69	Phosphorylation	RTRAHAQSKREGRHS HCCHHHHHHCCCCCC	34.17	27717283
80	Succinylation	GRHSGYGKRKGTREA CCCCCCCCCCCCCCC	42.31	23954790
80	Acetylation	GRHSGYGKRKGTREA CCCCCCCCCCCCCCC	42.31	24489116
91	Phosphorylation	TREARLPSQVVWIRR CCCCCCCHHHHHHHH	39.95	21082442
117	Acetylation	RDAGKIDKHLYHVLY HHCCCCCHHHHHHHH	38.70	24489116
117	Ubiquitination	RDAGKIDKHLYHVLY HHCCCCCHHHHHHHH	38.70	-
125	Acetylation	HLYHVLYKESKGNAF HHHHHHHHCCCCCHH	51.88	24489116
125	Ubiquitination	HLYHVLYKESKGNAF HHHHHHHHCCCCCHH	51.88	-
128	Succinylation	HVLYKESKGNAFKHK HHHHHCCCCCHHHHH	58.22	23954790
146	Acetylation	VEHIIQAKADAQREK HHHHHHHHHHHHHHH	30.35	24489116
146	Ubiquitination	VEHIIQAKADAQREK HHHHHHHHHHHHHHH	30.35	22106047
153	Ubiquitination	KADAQREKALNEEAE HHHHHHHHHHHHHHH	61.43	-
153	Acetylation	KADAQREKALNEEAE HHHHHHHHHHHHHHH	61.43	24489116
186	Ubiquitination	EKRDALLKEDA---- HHHHHHHHCCC----	55.16	22106047
186	Acetylation	EKRDALLKEDA---- HHHHHHHHCCC----	55.16	25381059

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

Oops, there are no upstream regulatory protein records of RL19A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL19A_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 RL19A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RQC2_YEAST	TAE2	genetic	20691087
ELO3_YEAST	ELO3	genetic	22808036

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 THR-29 AND SER-30, AND MASSSPECTROMETRY.
PubMed: 18407956

"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-30 AND SER-91, AND MASSSPECTROMETRY.
PubMed: 15665377