RL31A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL31A_YEAST
• UniProt AC: P0C2H8
• Protein Name: 60S ribosomal protein L31-A {ECO:0000303|PubMed:9559554}
• Gene Name: RPL31A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 113
• 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: MAGLKDVVTREYTINLHKRLHGVSFKKRAPRAVKEIKKFAKLHMGTDDVRLAPELNQAIWKRGVKGVEYRLRLRISRKRNEEEDAKNPLFSYVEPVLVASAKGLQTVVVEEDA

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	Succinylation	---MAGLKDVVTREY ---CCCCCCCCCCEE	47.78	23954790
9	Phosphorylation	AGLKDVVTREYTINL CCCCCCCCCEEEEEH	20.03	21440633
13	Phosphorylation	DVVTREYTINLHKRL CCCCCEEEEEHHHHH	9.91	20377248
18	Succinylation	EYTINLHKRLHGVSF EEEEEHHHHHCCCCC	60.88	23954790
18	Acetylation	EYTINLHKRLHGVSF EEEEEHHHHHCCCCC	60.88	24489116
24	Phosphorylation	HKRLHGVSFKKRAPR HHHHCCCCCCCCCCH	35.62	17287358
26	Acetylation	RLHGVSFKKRAPRAV HHCCCCCCCCCCHHH	33.57	25381059
26	Ubiquitination	RLHGVSFKKRAPRAV HHCCCCCCCCCCHHH	33.57	17644757
27	Ubiquitination	LHGVSFKKRAPRAVK HCCCCCCCCCCHHHH	52.35	17644757
37	Ubiquitination	PRAVKEIKKFAKLHM CHHHHHHHHHHHHHC	42.82	22817900
38	Ubiquitination	RAVKEIKKFAKLHMG HHHHHHHHHHHHHCC	57.10	22817900
41	Ubiquitination	KEIKKFAKLHMGTDD HHHHHHHHHHCCCCC	41.90	22817900
41	2-Hydroxyisobutyrylation	KEIKKFAKLHMGTDD HHHHHHHHHHCCCCC	41.90	-
41	Acetylation	KEIKKFAKLHMGTDD HHHHHHHHHHCCCCC	41.90	24489116
61	Succinylation	ELNQAIWKRGVKGVE HHHHHHHHCCCCCHH	32.91	23954790
61	2-Hydroxyisobutyrylation	ELNQAIWKRGVKGVE HHHHHHHHCCCCCHH	32.91	-
61	Acetylation	ELNQAIWKRGVKGVE HHHHHHHHCCCCCHH	32.91	24489116
61	Ubiquitination	ELNQAIWKRGVKGVE HHHHHHHHCCCCCHH	32.91	23749301
65	Ubiquitination	AIWKRGVKGVEYRLR HHHHCCCCCHHHHHH	61.12	22817900
65	2-Hydroxyisobutyrylation	AIWKRGVKGVEYRLR HHHHCCCCCHHHHHH	61.12	-
86	Acetylation	RNEEEDAKNPLFSYV CCCCCCCCCCCHHCH	72.00	24489116
86	Ubiquitination	RNEEEDAKNPLFSYV CCCCCCCCCCCHHCH	72.00	17644757
91	Phosphorylation	DAKNPLFSYVEPVLV CCCCCCHHCHHHHHH	35.63	21551504
100	Phosphorylation	VEPVLVASAKGLQTV HHHHHHHCCCCCEEE	24.04	17563356
102	Acetylation	PVLVASAKGLQTVVV HHHHHCCCCCEEEEE	58.62	23572591
102	Ubiquitination	PVLVASAKGLQTVVV HHHHHCCCCCEEEEE	58.62	17644757

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

Oops, there are no upstream regulatory protein records of RL31A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL31A_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 RL31A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCN4_YEAST	GCN4	genetic	18423200
RL39_YEAST	RPL39	genetic	18829863
RTC6_YEAST	RTC6	genetic	20691087
RL31B_YEAST	RPL31B	genetic	22377630
GCN4_YEAST	GCN4	genetic	24217298

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
PubMed: 17563356