RL5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL5_MOUSE
• UniProt AC: P47962
• Protein Name: 60S ribosomal protein L5
• Gene Name: Rpl5
• Organism: Mus musculus (Mouse).
• Sequence Length: 297
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus .
• 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. Interacts with RRP1B..
• Protein Sequence: MGFVKVVKNKAYFKRYQVRFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVNGGEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNNVTPDMMEEMYKKAHAAIRENPVYEKKPKREVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES

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	------MGFVKVVKN ------CCCEEEECC	35.73	-
5	Acetylation	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	23864654
5	Ubiquitination	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	-
27	Acetylation	FRRRREGKTDYYARK EHHHCCCCCCCHHEE	33.21	23954790
27	Ubiquitination	FRRRREGKTDYYARK EHHHCCCCCCCHHEE	33.21	-
30	Phosphorylation	RREGKTDYYARKRLV HCCCCCCCHHEEEEE	12.31	29514104
41	Acetylation	KRLVIQDKNKYNTPK EEEEEECCCCCCCCC	38.68	23806337
43	Ubiquitination	LVIQDKNKYNTPKYR EEEECCCCCCCCCEE	45.69	-
43	Acetylation	LVIQDKNKYNTPKYR EEEECCCCCCCCCEE	45.69	23201123
48	Acetylation	KNKYNTPKYRMIVRV CCCCCCCCEEEEEEE	43.37	-
62	S-nitrosocysteine	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	-
62	S-palmitoylation	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	28526873
62	S-nitrosylation	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	20925432
62	Glutathionylation	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	24333276
66	Phosphorylation	DIICQIAYARIEGDM HHEEEEEEEEECCCE	9.68	22817900
76	S-nitrosocysteine	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	-
76	S-palmitoylation	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	28526873
76	S-nitrosylation	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	20925432
76	Glutathionylation	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	24333276
85	Acetylation	AYAHELPKYGVKVGL HHHHCCCCCCCCCCC	68.23	22826441
100	S-palmitoylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	28526873
100	Glutathionylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	24333276
100	S-nitrosylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	20925432
100	S-nitrosocysteine	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	-
158	Succinylation	ARTTTGNKVFGALKG EECCCCCHHHHCCCC	40.04	23806337
158	Acetylation	ARTTTGNKVFGALKG EECCCCCHHHHCCCC	40.04	23806337
164	Methylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	-
164	Ubiquitination	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	22790023
176	Phosphorylation	GGLSIPHSTKRFPGY CCCCCCCCCCCCCCC	30.21	30352176
177	Phosphorylation	GLSIPHSTKRFPGYD CCCCCCCCCCCCCCC	24.17	30352176
178	Acetylation	LSIPHSTKRFPGYDS CCCCCCCCCCCCCCC	55.87	2373027
183	Phosphorylation	STKRFPGYDSESKEF CCCCCCCCCCCCCCC	19.28	25195567
185	Phosphorylation	KRFPGYDSESKEFNA CCCCCCCCCCCCCCH	34.97	30352176
187	Phosphorylation	FPGYDSESKEFNAEV CCCCCCCCCCCCHHH	41.24	26745281
220	Succinylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	23806337
220	Acetylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	23806337
221	Ubiquitination	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	-
221	Acetylation	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	133649
228	Ubiquitination	KQFSQYIKNNVTPDM HHHHHHHHCCCCHHH	37.22	22790023
228	Acetylation	KQFSQYIKNNVTPDM HHHHHHHHCCCCHHH	37.22	23954790
232	Phosphorylation	QYIKNNVTPDMMEEM HHHHCCCCHHHHHHH	18.72	-
241	Acetylation	DMMEEMYKKAHAAIR HHHHHHHHHHHHHHH	42.02	23864654
241	Succinylation	DMMEEMYKKAHAAIR HHHHHHHHHHHHHHH	42.02	23954790
255	Acetylation	RENPVYEKKPKREVK HHCCCCCCCCCHHHH	57.60	23201123
272	Phosphorylation	RWNRPKMSLAQKKDR HCCCCCCCHHHHHHH	27.04	-
276	Malonylation	PKMSLAQKKDRVAQK CCCCHHHHHHHHHHH	51.54	26320211
283	Acetylation	KKDRVAQKKASFLRA HHHHHHHHHHHHHHH	40.34	23864654
286	Phosphorylation	RVAQKKASFLRAQER HHHHHHHHHHHHHHH	33.42	24704852

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

Oops, there are no upstream regulatory protein records of RL5_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL5_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 RL5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPM_MOUSE	Npm1	physical	16648475

Drug and Disease Associations

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