RL30_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL30_YEAST
• UniProt AC: P14120
• Protein Name: 60S ribosomal protein L30 {ECO:0000303|PubMed:9559554}
• Gene Name: RPL30 {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 105
• 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: MAPVKSQESINQKLALVIKSGKYTLGYKSTVKSLRQGKSKLIIIAANTPVLRKSELEYYAMLSKTKVYYFQGGNNELGTAVGKLFRVGVVSILEAGDSDILTTLA

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
5	2-Hydroxyisobutyrylation	---MAPVKSQESINQ ---CCCCCCHHHHHH	45.41	-
5	Succinylation	---MAPVKSQESINQ ---CCCCCCHHHHHH	45.41	23954790
6	Phosphorylation	--MAPVKSQESINQK --CCCCCCHHHHHHH	39.14	22369663
9	Phosphorylation	APVKSQESINQKLAL CCCCCHHHHHHHEEE	21.14	22369663
13	Acetylation	SQESINQKLALVIKS CHHHHHHHEEEEECC	31.10	24489116
19	Ubiquitination	QKLALVIKSGKYTLG HHEEEEECCCCEEEC	45.75	23749301
19	2-Hydroxyisobutyrylation	QKLALVIKSGKYTLG HHEEEEECCCCEEEC	45.75	-
19	Acetylation	QKLALVIKSGKYTLG HHEEEEECCCCEEEC	45.75	22865919
22	Ubiquitination	ALVIKSGKYTLGYKS EEEECCCCEEECCHH	42.00	23749301
22	Acetylation	ALVIKSGKYTLGYKS EEEECCCCEEECCHH	42.00	24489116
24	Phosphorylation	VIKSGKYTLGYKSTV EECCCCEEECCHHHH	19.72	21440633
28	Succinylation	GKYTLGYKSTVKSLR CCEEECCHHHHHHHH	37.54	23954790
28	Acetylation	GKYTLGYKSTVKSLR CCEEECCHHHHHHHH	37.54	24489116
32	Succinylation	LGYKSTVKSLRQGKS ECCHHHHHHHHCCCC	43.81	23954790
32	2-Hydroxyisobutyrylation	LGYKSTVKSLRQGKS ECCHHHHHHHHCCCC	43.81	-
38	Ubiquitination	VKSLRQGKSKLIIIA HHHHHCCCCEEEEEE	35.76	22817900
40	Ubiquitination	SLRQGKSKLIIIAAN HHHCCCCEEEEEECC	47.38	23749301
40	Acetylation	SLRQGKSKLIIIAAN HHHCCCCEEEEEECC	47.38	24489116
48	Phosphorylation	LIIIAANTPVLRKSE EEEEECCCCCCCHHH	15.28	24961812
53	Ubiquitination	ANTPVLRKSELEYYA CCCCCCCHHHHHHHH	44.09	23749301
64	Acetylation	EYYAMLSKTKVYYFQ HHHHHHHCCEEEEEE	48.69	24489116
64	Ubiquitination	EYYAMLSKTKVYYFQ HHHHHHHCCEEEEEE	48.69	22817900
66	Acetylation	YAMLSKTKVYYFQGG HHHHHCCEEEEEECC	31.79	24489116
66	2-Hydroxyisobutyrylation	YAMLSKTKVYYFQGG HHHHHCCEEEEEECC	31.79	-
66	Ubiquitination	YAMLSKTKVYYFQGG HHHHHCCEEEEEECC	31.79	23749301
66	Succinylation	YAMLSKTKVYYFQGG HHHHHCCEEEEEECC	31.79	23954790
68	Phosphorylation	MLSKTKVYYFQGGNN HHHCCEEEEEECCCC	10.50	24909858
69	Phosphorylation	LSKTKVYYFQGGNNE HHCCEEEEEECCCCH	7.75	28132839
79	Phosphorylation	GGNNELGTAVGKLFR CCCCHHHHHHHHHHH	30.69	22369663
83	Acetylation	ELGTAVGKLFRVGVV HHHHHHHHHHHHEEE	37.54	24489116
83	Ubiquitination	ELGTAVGKLFRVGVV HHHHHHHHHHHHEEE	37.54	23749301
83	Succinylation	ELGTAVGKLFRVGVV HHHHHHHHHHHHEEE	37.54	23954790

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

Oops, there are no upstream regulatory protein records of RL30_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL30_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 RL30_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL30_YEAST	RPL30	physical	14970382
NCBP1_YEAST	STO1	genetic	20801768

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-6, AND MASSSPECTROMETRY.
PubMed: 18407956