RT23_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RT23_YEAST
• UniProt AC: Q01163
• Protein Name: 37S ribosomal protein S23, mitochondrial
• Gene Name: RSM23
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 450
• Subcellular Localization: Mitochondrion . Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner memb
• Protein Description: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS29 binds GTP and is probably an active GTPase. GTP hydrolysis may be linked to subunit association. [PubMed: 25609543]
• Protein Sequence: MLRMSTSRFIGQRLFTTARSLQAAKPAPKGKTQGFSKKSSSVSSYSSAKRVTPGSLYKNWTNTTHTAQLQQTAVPLALPIFNFDDISKTLNKVVSYSNKQYKSLHHLGSFKKSQFNELFQKPVCLVREDATNSFLKKLVSHPVKKFIITGEPGVGKTVLLSQAHAYAVDSKQIIINISYPELFLNGRNDFSYDDDLKLFIQPMYLKKLIRKILKANDPALLKSIELSKDYKFSNANPKNASVKPFVTLNKTKNTVLDLLSVMTHPHNRGKLMKAIIDELSVQSKVPIMFTVDNFSKVLTTAYSAYRNTENKQIYSLDLQMGKLMMDIISGETKFANGESSTILAISGVDRTNKTLPVALGKIPVDPYVTRYHYEPKFVELLQKGNVTEFEVPKLNKQEVNELIDYYKQSNVLLDKDITGKKWENLIDEKYFLSGNGNPRELLKSLVLSHR

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
32	Phosphorylation	KPAPKGKTQGFSKKS CCCCCCCCCCCCCCC	42.46	27017623
40	Phosphorylation	QGFSKKSSSVSSYSS CCCCCCCCCCCCCCC	43.57	27017623
41	Phosphorylation	GFSKKSSSVSSYSSA CCCCCCCCCCCCCCC	32.86	27017623
52	Phosphorylation	YSSAKRVTPGSLYKN CCCCCCCCCCCCCCC	26.43	21126336
222	Acetylation	ANDPALLKSIELSKD HCCHHHHHHHHHCCC	50.68	24489116
233	Phosphorylation	LSKDYKFSNANPKNA HCCCCCCCCCCCCCC	30.77	22369663
295	Phosphorylation	MFTVDNFSKVLTTAY EEEECCHHHHHHHHH	28.27	27017623
361	Ubiquitination	TLPVALGKIPVDPYV CCCEECCCCCCCCCC	44.69	19722269
376	Acetylation	TRYHYEPKFVELLQK CCCCCCHHHHHHHHC	50.53	24489116
433	Phosphorylation	IDEKYFLSGNGNPRE CCHHHCCCCCCCHHH	21.95	28889911

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

Oops, there are no upstream regulatory protein records of RT23_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RT23_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RT23_YEAST !!

Protein-Protein Interaction

Oops, there are no PPI records of RT23_YEAST !!

Drug and Disease Associations

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