RL44B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL44B_YEAST
• UniProt AC: P0CX28
• Protein Name: 60S ribosomal protein L42-B {ECO:0000303|PubMed:9559554}
• Gene Name: RPL42B {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 106
• 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: MVNVPKTRKTYCKGKTCRKHTQHKVTQYKAGKASLFAQGKRRYDRKQSGFGGQTKPVFHKKAKTTKKVVLRLECVKCKTRAQLTLKRCKHFELGGEKKQKGQALQF

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
19	Ubiquitination	CKGKTCRKHTQHKVT CCCCCCHHHCCCCCE	53.82	22817900
24	Ubiquitination	CRKHTQHKVTQYKAG CHHHCCCCCEEEHHH	36.84	23749301
29	Ubiquitination	QHKVTQYKAGKASLF CCCCEEEHHHHHHHH	40.62	23749301
40	Methylation	ASLFAQGKRRYDRKQ HHHHHCCCCCCCCCC	22.94	22522802
55	Methylation	SGFGGQTKPVFHKKA CCCCCCCCCCCCCCC	31.15	18957409
76	Ubiquitination	VLRLECVKCKTRAQL EEEEEECCCCCHHHH	41.49	23749301
78	Ubiquitination	RLECVKCKTRAQLTL EEEECCCCCHHHHHH	35.01	22817900
79	Phosphorylation	LECVKCKTRAQLTLK EEECCCCCHHHHHHH	40.48	28889911
97	Ubiquitination	HFELGGEKKQKGQAL CCCCCCCCCCCCCCC	64.87	22817900
98	Ubiquitination	FELGGEKKQKGQALQ CCCCCCCCCCCCCCC	53.60	22817900
100	Ubiquitination	LGGEKKQKGQALQF- CCCCCCCCCCCCCC-	62.97	23749301

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

Oops, there are no upstream regulatory protein records of RL44B_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
40	K	Methylation	In wild-type cells, 78% of L42 is monomethylated at both Lys-40 and Lys-55, and 22% are a mixture of species with either residue monomethylated.	18957409
55	K	Methylation	In wild-type cells, 78% of L42 is monomethylated at both Lys-40 and Lys-55, and 22% are a mixture of species with either residue monomethylated.	18957409

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RL44B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEO1_YEAST	SEO1	physical	16554755
SLI15_YEAST	SLI15	physical	16554755
SPT16_YEAST	SPT16	physical	16554755
MRS1_YEAST	MRS1	physical	16554755
NAP1_YEAST	NAP1	physical	16554755
HOG1_YEAST	HOG1	physical	16554755
NST1_YEAST	NST1	physical	16554755
SYWC_YEAST	WRS1	physical	16554755
NOC4_YEAST	NOC4	physical	16554755

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Methylation

"Identification of two SET domain proteins required for methylation oflysine residues in yeast ribosomal protein Rpl42ab.";
Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.;
J. Biol. Chem. 283:35561-35568(2008).
Cited for: METHYLATION AT LYS-40 AND LYS-55, AND MASS SPECTROMETRY.
PubMed: 18957409