EXOS5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS5_MOUSE
• UniProt AC: Q9CRA8
• Protein Name: Exosome complex component RRP46
• Gene Name: Exosc5
• Organism: Mus musculus (Mouse).
• Sequence Length: 235
• Subcellular Localization: Nucleus, nucleolus. Cytoplasm. Nucleus.
• 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 promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. 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 (By similarity)..
• Protein Sequence: MEGAKRADANLLTDTGTESSPRSPVCSLRHFACEQNLLSRPDGSASFLQGDTSVLAGVYGPAEVKVSKEIFNKATLEVILRPKIGLPGVAEKSRERLVRNTCEAVVLGALHPRTSITVVLQVVSDAGSLLACCLNAACMALVDAGVPMRALFCGVTCALDSDGNLVLDPTTKQEKEARAILTFALDSAEQKLLMSTTKGLYSDAELQQCLAAAQAASQHIFRFYRESLQRRYSKS

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
13	Phosphorylation	RADANLLTDTGTESS CCCCCCCCCCCCCCC	34.38	27742792
15	Phosphorylation	DANLLTDTGTESSPR CCCCCCCCCCCCCCC	40.54	27742792
17	Phosphorylation	NLLTDTGTESSPRSP CCCCCCCCCCCCCCC	34.48	27742792
19	Phosphorylation	LTDTGTESSPRSPVC CCCCCCCCCCCCCCH	45.54	25521595
20	Phosphorylation	TDTGTESSPRSPVCS CCCCCCCCCCCCCHH	20.35	25521595
23	Phosphorylation	GTESSPRSPVCSLRH CCCCCCCCCCHHHHH	25.68	25521595
27	Phosphorylation	SPRSPVCSLRHFACE CCCCCCHHHHHHHHH	28.77	27742792
92	Ubiquitination	GLPGVAEKSRERLVR CCCCCHHHHHHHHHH	45.11	-
198	Ubiquitination	KLLMSTTKGLYSDAE HHHHHCCCCCCCHHH	47.18	-

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

Oops, there are no upstream regulatory protein records of EXOS5_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS5_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 EXOS5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EXOS5_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.
PubMed: 17242355