RRP40_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RRP40_YEAST
• UniProt AC: Q08285
• Protein Name: Exosome complex component RRP40
• Gene Name: RRP40
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 240
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus .
• Protein Description: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP40 as peripheral part of the Exo-9 complex is thought to stabilize the hexameric ring of RNase PH-domain subunits..
• Protein Sequence: MSTFIFPGDSFPVDPTTPVKLGPGIYCDPNTQEIRPVNTGVLHVSAKGKSGVQTAYIDYSSKRYIPSVNDFVIGVIIGTFSDSYKVSLQNFSSSVSLSYMAFPNASKKNRPTLQVGDLVYARVCTAEKELEAEIECFDSTTGRDAGFGILEDGMIIDVNLNFARQLLFNNDFPLLKVLAAHTKFEVAIGLNGKIWVKCEELSNTLACYRTIMECCQKNDTAAFKDIAKRQFKEILTVKEE

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	Phosphorylation	------MSTFIFPGD ------CCCEECCCC	31.83	30377154
3	Phosphorylation	-----MSTFIFPGDS -----CCCEECCCCC	21.32	27017623
10	Phosphorylation	TFIFPGDSFPVDPTT CEECCCCCCCCCCCC	37.05	30377154
16	Phosphorylation	DSFPVDPTTPVKLGP CCCCCCCCCCCCCCC	38.99	28889911
17	Phosphorylation	SFPVDPTTPVKLGPG CCCCCCCCCCCCCCC	31.32	28152593
176	Acetylation	NNDFPLLKVLAAHTK CCCCHHHHHHHHCCC	42.77	24489116
224	Acetylation	KNDTAAFKDIAKRQF HCCCHHHHHHHHHHH	43.42	24489116

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

Oops, there are no upstream regulatory protein records of RRP40_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RRP40_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 RRP40_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OLA1_YEAST	OLA1	physical	16554755
OSM1_YEAST	OSM1	physical	16554755
SKI7_YEAST	SKI7	physical	16554755
RRP44_YEAST	DIS3	physical	16429126
MTR3_YEAST	MTR3	physical	16429126
RRP4_YEAST	RRP4	physical	16429126
RRP42_YEAST	RRP42	physical	16429126
RRP43_YEAST	RRP43	physical	16429126
RRP45_YEAST	RRP45	physical	16429126
RRP46_YEAST	RRP46	physical	16429126
RRP6_YEAST	RRP6	physical	16429126
RRP41_YEAST	SKI6	physical	16429126
SKI7_YEAST	SKI7	physical	16429126

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND MASSSPECTROMETRY.
PubMed: 18407956