RT51_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RT51_YEAST
• UniProt AC: Q02950
• Protein Name: 37S ribosomal protein MRP51, mitochondrial
• Gene Name: MRP51
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 344
• 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. bS1m functionally interacts with the 5'-UTR of mitochondrial mRNAs..
• Protein Sequence: MTLAELLGRSRIAQVANNHKPLTYTGKKFHPTHQIIETKPSTLYRQEWGLKSAIPSKIKSRYLVYNDLDTLERITTFEPRGGTQWNRLRFQEMGVPIVSNIGRQNPFFKYISRPEDESHAKLSLFKEMKGDTDISPAAMKKRLKKITALIRSFQDEFKEWLVENHPDELKLNSNKLEDYVVKFLNKKLETKTNKKFNTEIIGTGGLSYSLPGKLKNSPNGVIQRTVVPGRILNVVKENNDNKWLAAIGGFVADVVFFQSPPSSFNSMGDFIRMKTFLFEILEASMEKNGSVSMHARLLEPQNDKTREFFNKRPIYKPLTSRRARRPSVGNIQEANNLLNIIKGN

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
135	Phosphorylation	MKGDTDISPAAMKKR HCCCCCCCHHHHHHH	15.99	25704821
182	Acetylation	KLEDYVVKFLNKKLE HHHHHHHHHHHHHCC	33.81	24489116
195	Ubiquitination	LETKTNKKFNTEIIG CCHHCCCCCCCEEEE	46.01	23749301
198	Phosphorylation	KTNKKFNTEIIGTGG HCCCCCCCEEEECCC	31.52	23749301
207	Phosphorylation	IIGTGGLSYSLPGKL EEECCCCCCCCCCCC	18.89	23749301
242	Ubiquitination	VKENNDNKWLAAIGG EEECCCCCCHHHHHH	46.58	19722269
284	Phosphorylation	LFEILEASMEKNGSV HHHHHHHHHHHCCCC	20.35	29688323
327	Phosphorylation	SRRARRPSVGNIQEA CCCCCCCCCCCHHHH	40.62	22369663

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

Oops, there are no upstream regulatory protein records of RT51_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RT51_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 RT51_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GEM1_YEAST	GEM1	genetic	27708008
AGP2_YEAST	AGP2	genetic	27708008
QRI7_YEAST	QRI7	genetic	27708008
BCS1_YEAST	BCS1	genetic	27708008
AVL9_YEAST	AVL9	genetic	27708008
AEP2_YEAST	AEP2	genetic	27708008
HMI1_YEAST	HMI1	genetic	27708008
CY1_YEAST	CYT1	genetic	27708008

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASSSPECTROMETRY.
PubMed: 17563356