RS23_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS23_MOUSE
• UniProt AC: P62267
• Protein Name: 40S ribosomal protein S23
• Gene Name: Rps23
• Organism: Mus musculus (Mouse).
• Sequence Length: 143
• Subcellular Localization: Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
• 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. Plays an important role in translational accuracy..
• Protein Sequence: MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS

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
27	Phosphorylation	QKWHDKQYKKAHLGT CCCCHHHHHHHHHHH	21.87	29895711
29	Ubiquitination	WHDKQYKKAHLGTAL CCHHHHHHHHHHHHH	35.78	27667366
34	Phosphorylation	YKKAHLGTALKANPF HHHHHHHHHHHCCCC	34.87	29895711
45	Phosphorylation	ANPFGGASHAKGIVL CCCCCCCCCCCCEEE	27.53	29514104
48	Ubiquitination	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	-
54	Succinylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	-
54	Ubiquitination	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	-
54	Acetylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	23806337
54	Succinylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	23806337
62	Hydroxylation	VGVEAKQPNSAIRKC ECCCCCCCCHHHHHH	35.72	-
90	Glutathionylation	AFVPNDGCLNFIEEN EEECCCCCCCHHHCC	2.90	24333276
90	S-palmitoylation	AFVPNDGCLNFIEEN EEECCCCCCCHHHCC	2.90	28526873
108	Ubiquitination	LVAGFGRKGHAVGDI EEEECCCCCCCCCCC	56.26	-
129	Phosphorylation	VVKVANVSLLALYKG EEEEECHHHHHHHCC	19.92	26643407
135	Acetylation	VSLLALYKGKKERPR HHHHHHHCCCCCCCC	66.17	23236377

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

Oops, there are no upstream regulatory protein records of RS23_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
62	P	Hydroxylation	Hydroxylation at Pro-62 affects translation termination efficiency.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RS23_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RS23_MOUSE !!

Drug and Disease Associations

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