RL35A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL35A_YEAST
• UniProt AC: P0CX84
• Protein Name: 60S ribosomal protein L35-A {ECO:0000303|PubMed:9559554}
• Gene Name: RPL35A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 120
• 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: MAGVKAYELRTKSKEQLASQLVDLKKELAELKVQKLSRPSLPKIKTVRKSIACVLTVINEQQREAVRQLYKGKKYQPKDLRAKKTRALRRALTKFEASQVTEKQRKKQIAFPQRKYAIKA

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	Acetylation	---MAGVKAYELRTK ---CCCCCHHHCCCC	44.31	23572591
11	Phosphorylation	VKAYELRTKSKEQLA CCHHHCCCCCHHHHH	52.90	30377154
13	Phosphorylation	AYELRTKSKEQLASQ HHHCCCCCHHHHHHH	40.59	21440633
14	Ubiquitination	YELRTKSKEQLASQL HHCCCCCHHHHHHHH	51.54	-
14	Acetylation	YELRTKSKEQLASQL HHCCCCCHHHHHHHH	51.54	24489116
19	Phosphorylation	KSKEQLASQLVDLKK CCHHHHHHHHHHHHH	32.41	22369663
25	Ubiquitination	ASQLVDLKKELAELK HHHHHHHHHHHHHHH	39.47	-
25	Succinylation	ASQLVDLKKELAELK HHHHHHHHHHHHHHH	39.47	23954790
25	Acetylation	ASQLVDLKKELAELK HHHHHHHHHHHHHHH	39.47	24489116
26	Acetylation	SQLVDLKKELAELKV HHHHHHHHHHHHHHH	66.32	24489116
26	Ubiquitination	SQLVDLKKELAELKV HHHHHHHHHHHHHHH	66.32	-
32	Acetylation	KKELAELKVQKLSRP HHHHHHHHHHHHCCC	33.84	24489116
32	Ubiquitination	KKELAELKVQKLSRP HHHHHHHHHHHHCCC	33.84	-
32	Succinylation	KKELAELKVQKLSRP HHHHHHHHHHHHCCC	33.84	23954790
35	Acetylation	LAELKVQKLSRPSLP HHHHHHHHHCCCCCC	51.95	24489116
37	Phosphorylation	ELKVQKLSRPSLPKI HHHHHHHCCCCCCCC	49.53	21440633
40	Phosphorylation	VQKLSRPSLPKIKTV HHHHCCCCCCCCHHH	57.08	22369663
43	Acetylation	LSRPSLPKIKTVRKS HCCCCCCCCHHHHHH	63.23	24489116
49	Ubiquitination	PKIKTVRKSIACVLT CCCHHHHHHHHHHHH	41.71	-
50	Phosphorylation	KIKTVRKSIACVLTV CCHHHHHHHHHHHHH	12.59	21440633
56	Phosphorylation	KSIACVLTVINEQQR HHHHHHHHHCCHHHH	10.03	30377154
78	Succinylation	KGKKYQPKDLRAKKT CCCCCCCHHHHHHHH	54.60	23954790
78	Acetylation	KGKKYQPKDLRAKKT CCCCCCCHHHHHHHH	54.60	24489116
93	Phosphorylation	RALRRALTKFEASQV HHHHHHHHHHHHHHC	32.47	23749301
94	Ubiquitination	ALRRALTKFEASQVT HHHHHHHHHHHHHCC	41.90	-
94	Acetylation	ALRRALTKFEASQVT HHHHHHHHHHHHHCC	41.90	24489116
98	Phosphorylation	ALTKFEASQVTEKQR HHHHHHHHHCCHHHH	20.27	23749301
101	Phosphorylation	KFEASQVTEKQRKKQ HHHHHHCCHHHHHHH	29.81	28889911
103	Succinylation	EASQVTEKQRKKQIA HHHHCCHHHHHHHCC	46.14	23954790
103	Acetylation	EASQVTEKQRKKQIA HHHHCCHHHHHHHCC	46.14	24489116
103	Ubiquitination	EASQVTEKQRKKQIA HHHHCCHHHHHHHCC	46.14	-

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

Oops, there are no upstream regulatory protein records of RL35A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL35A_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 RL35A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARD1_YEAST	ARD1	physical	17541948
NACA_YEAST	EGD2	physical	26195668
RL13A_YEAST	RPL13A	physical	26195668

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-98, AND MASSSPECTROMETRY.
PubMed: 18407956