RL11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL11_MOUSE
• UniProt AC: Q9CXW4
• Protein Name: 60S ribosomal protein L11
• Gene Name: Rpl11
• Organism: Mus musculus (Mouse).
• 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. [PubMed: 21804542 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	-
8	Acetylation	MAQDQGEKENPMREL CCCCCCCCCCHHHHH	70.39	12437759
19	Acetylation	MRELRIRKLCLNICV HHHHHHHHHHHHHHH	40.98	15297423
29	Phosphorylation	LNICVGESGDRLTRA HHHHHCCCCHHHHHH	39.81	26745281
34	Phosphorylation	GESGDRLTRAAKVLE CCCCHHHHHHHHHHH	21.11	23984901
38	Acetylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	22826441
38	Ubiquitination	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	-
38	Malonylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	26320211
44	Phosphorylation	AKVLEQLTGQTPVFS HHHHHHHHCCCCCCC	27.26	28066266
47	Phosphorylation	LEQLTGQTPVFSKAR HHHHHCCCCCCCCHH	23.82	26824392
51	Phosphorylation	TGQTPVFSKARYTVR HCCCCCCCCHHEEEH	26.16	26643407
52	Acetylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	22826441
52	Ubiquitination	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	27667366
52	Succinylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	23806337
52	Malonylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	26320211
55	Ubiquitination	PVFSKARYTVRSFGI CCCCCHHEEEHHCCC	17.91	27667366
67	Malonylation	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	26320211
67	Acetylation	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	23806337
72	S-nitrosylation	NEKIAVHCTVRGAKA CCEEEEEEEECCHHH	2.78	21278135
72	S-nitrosocysteine	NEKIAVHCTVRGAKA CCEEEEEEEECCHHH	2.78	-
72	Glutathionylation	NEKIAVHCTVRGAKA CCEEEEEEEECCHHH	2.78	24333276
85	Succinylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	23954790
85	Ubiquitination	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	-
85	Acetylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	23864654
85	Malonylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	26320211
140	Phosphorylation	VLGRPGFSIADKKRR EECCCCCCHHCHHHC	23.84	29176673
150	Glutathionylation	DKKRRTGCIGAKHRI CHHHCCCCCCCCCCC	2.28	24333276
154	Acetylation	RTGCIGAKHRISKEE CCCCCCCCCCCCHHH	28.36	23201123
159	Succinylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	23806337
159	Malonylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	26320211
159	Acetylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	23806337
159	Ubiquitination	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	27667366
162	Ubiquitination	HRISKEEAMRWFQQK CCCCHHHHHHHHHHH	8.24	27667366
169	Acetylation	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	22826441
178	Ubiquitination	DGIILPGK------- CCEEECCC-------	56.05	-

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

Oops, there are no upstream regulatory protein records of RL11_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL11_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_MOUSE	Mdm2	physical	15989966
P53_MOUSE	Trp53	physical	15989966

Drug and Disease Associations

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