RL36B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL36B_YEAST
• UniProt AC: O14455
• Protein Name: 60S ribosomal protein L36-B {ECO:0000303|PubMed:9559554}
• Gene Name: RPL36B {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 100
• 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: MAVKTGIAIGLNKGKKVTQMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNSGEKRARKVAKKRLGSFTRAKAKVEEMNNIIAASRRH

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	Phosphorylation	---MAVKTGIAIGLN ---CCCCCCEEEECC	27.50	21440633
13	Acetylation	GIAIGLNKGKKVTQM CEEEECCCCCCCCEE	76.72	24489116
16	Ubiquitination	IGLNKGKKVTQMTPA EECCCCCCCCEECCC	60.22	23749301
18	Phosphorylation	LNKGKKVTQMTPAPK CCCCCCCCEECCCCC	22.85	21440633
21	Phosphorylation	GKKVTQMTPAPKISY CCCCCEECCCCCCCC	13.38	22369663
25	Ubiquitination	TQMTPAPKISYKKGA CEECCCCCCCCCCCC	46.52	23749301
25	Acetylation	TQMTPAPKISYKKGA CEECCCCCCCCCCCC	46.52	24489116
42	Phosphorylation	NRTKFVRSLVREIAG CHHHHHHHHHHHHCC	26.39	21440633
51	Phosphorylation	VREIAGLSPYERRLI HHHHCCCCHHHHHHH	25.23	27214570
64	Phosphorylation	LIDLIRNSGEKRARK HHHHHHHCHHHHHHH	38.18	28152593
79	Phosphorylation	VAKKRLGSFTRAKAK HHHHHHCCHHHHHHH	28.21	19823750
81	Phosphorylation	KKRLGSFTRAKAKVE HHHHCCHHHHHHHHH	31.26	24961812
84	Ubiquitination	LGSFTRAKAKVEEMN HCCHHHHHHHHHHHH	45.51	22817900
86	Ubiquitination	SFTRAKAKVEEMNNI CHHHHHHHHHHHHHH	49.85	23749301
86	Acetylation	SFTRAKAKVEEMNNI CHHHHHHHHHHHHHH	49.85	24489116
97	Phosphorylation	MNNIIAASRRH---- HHHHHHHHHCC----	22.33	22369663

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

Oops, there are no upstream regulatory protein records of RL36B_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL36B_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 RL36B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GYL1_YEAST	GYL1	physical	16429126
RL36A_YEAST	RPL36A	genetic	25119672
EBP2_YEAST	EBP2	physical	25119672
NOP12_YEAST	NOP12	physical	25119672

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-79, AND MASSSPECTROMETRY.
PubMed: 15665377