dbPTM

RL19B_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL19B_YEAST
UniProt AC	P0CX83
Protein Name	60S ribosomal protein L19-B {ECO:0000303\|PubMed:9559554}
Gene Name	RPL19B {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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MANLRTQKRLAASVV CCCHHHHHHHHHHHH	49.09	17644757
13	Phosphorylation	TQKRLAASVVGVGKR HHHHHHHHHHCCCCC	16.24	21440633
19	Ubiquitination	ASVVGVGKRKVWLDP HHHHCCCCCEEECCC	46.79	23749301
21	Ubiquitination	VVGVGKRKVWLDPNE HHCCCCCEEECCCCC	41.05	23749301
29	Phosphorylation	VWLDPNETSEIAQAN EECCCCCHHHHHHHH	38.00	22369663
30	Phosphorylation	WLDPNETSEIAQANS ECCCCCHHHHHHHHH	22.34	22369663
37	Phosphorylation	SEIAQANSRNAIRKL HHHHHHHHHHHHHHH	29.90	21440633
43	Ubiquitination	NSRNAIRKLVKNGTI HHHHHHHHHHHCCCE	52.06	22817900
46	Ubiquitination	NAIRKLVKNGTIVKK HHHHHHHHCCCEEEE	61.16	23749301
52	Ubiquitination	VKNGTIVKKAVTVHS HHCCCEEEEEEEECC	31.03	22817900
53	Ubiquitination	KNGTIVKKAVTVHSK HCCCEEEEEEEECCH	36.88	22817900
56	Phosphorylation	TIVKKAVTVHSKSRT CEEEEEEEECCHHHC	19.84	27717283
59	Phosphorylation	KKAVTVHSKSRTRAH EEEEEECCHHHCCHH	28.17	27214570
60	Ubiquitination	KAVTVHSKSRTRAHA EEEEECCHHHCCHHH	29.13	23749301
61	Phosphorylation	AVTVHSKSRTRAHAQ EEEECCHHHCCHHHH	41.73	23749301
63	Phosphorylation	TVHSKSRTRAHAQSK EECCHHHCCHHHHHH	39.02	19823750
69	Phosphorylation	RTRAHAQSKREGRHS HCCHHHHHHCCCCCC	34.17	27717283
80	Ubiquitination	GRHSGYGKRKGTREA CCCCCCCCCCCCCCC	42.31	17644757
91	Phosphorylation	TREARLPSQVVWIRR CCCCCCCHHHHHHHH	39.95	15665377
108	Ubiquitination	VLRRLLAKYRDAGKI HHHHHHHHHHHCCCC	40.56	22817900
114	Ubiquitination	AKYRDAGKIDKHLYH HHHHHCCCCCHHHHH	49.83	22817900
117	Ubiquitination	RDAGKIDKHLYHVLY HHCCCCCHHHHHHHH	38.70	23749301
125	Ubiquitination	HLYHVLYKESKGNAF HHHHHHHHCCCCCHH	51.88	23749301
128	Ubiquitination	HVLYKESKGNAFKHK HHHHHCCCCCHHHHH	58.22	22817900
133	Ubiquitination	ESKGNAFKHKRALVE CCCCCHHHHHHHHHH	45.89	22817900
135	Ubiquitination	KGNAFKHKRALVEHI CCCHHHHHHHHHHHH	39.70	22817900
146	Ubiquitination	VEHIIQAKADAQREK HHHHHHHHHHHHHHH	30.35	23749301
153	Ubiquitination	KADAQREKALNEEAE HHHHHHHHHHHHHHH	61.43	23749301
180	Ubiquitination	RAQRVAEKRDALLKE HHHHHHHHHHHHHHC	45.93	22817900
186	Ubiquitination	EKRDALLKEDA---- HHHHHHHHCCC----	55.16	23749301

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of RL19B_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL19B_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RL19B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
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.

Regulatory Network of RL19B_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	18407956 [Abstract]
"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.	15665377 [Abstract]