RL11_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL11_RAT
• UniProt AC: P62914
• Protein Name: 60S ribosomal protein L11
• Gene Name: Rpl11
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 178
• Subcellular Localization: Nucleus, nucleolus . 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. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Promotes nucleolar location of PML..
• Protein Sequence: MAQDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK

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
2	Acetylation	------MAQDQGEKE ------CCCCCCCCC	22.96	1599472
38	Acetylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	22902405
44	Phosphorylation	AKVLEQLTGQTPVFS HHHHHHHHCCCCCCC	27.26	23984901
47	Phosphorylation	LEQLTGQTPVFSKAR HHHHHCCCCCCCCHH	23.82	23984901
51	Phosphorylation	TGQTPVFSKARYTVR HCCCCCCCCHHEEEH	26.16	23984901
52	Acetylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	22902405
59	Phosphorylation	KARYTVRSFGIRRNE CHHEEEHHCCCCCCC	24.40	23984901
67	Acetylation	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	25786129
73	Phosphorylation	EKIAVHCTVRGAKAE CEEEEEEEECCHHHH	9.81	23984901
78	Acetylation	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	22902405
85	Acetylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	22902405
88	Acetylation	EILEKGLKVREYELR HHHHHCCEEEEEEHH	48.17	22902405
140	Phosphorylation	VLGRPGFSIADKKRR EECCCCCCHHCHHHC	23.84	27097102
159	Acetylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	22902405

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

Oops, there are no upstream regulatory protein records of RL11_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL11_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RL11_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RL11_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"The primary structure of rat ribosomal protein L11.";
Chan Y.-L., Olvera J., Paz V., Wool I.G.;
Biochem. Biophys. Res. Commun. 185:356-362(1992).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OFINITIATOR METHIONINE, AND ACETYLATION AT ALA-2.
PubMed: 1599472