EXOS2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS2_MOUSE
• UniProt AC: Q8VBV3
• Protein Name: Exosome complex component RRP4
• Gene Name: Exosc2
• Organism: Mus musculus (Mouse).
• Sequence Length: 293
• Subcellular Localization: Cytoplasm. Nucleus, nucleolus. 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. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7 (By similarity)..
• Protein Sequence: MALEMRLPKARKPLSESLGRDSKKHLVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYNGEVGDIVVGRITEVQQKRWKVETNSRLDSVLLLSSMNLPGGELRRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRSLKYGKLGQGVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKDEDAGGFIANLEPVALSDREVISRLRNCVVLLVTQRMMLFDTSILYCYEASLAHQIKDILKPEVMEEIMLETRQRLLDQEG

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
15	Phosphorylation	PKARKPLSESLGRDS CCCCCCHHHHCCCCC	33.40	28066266
17	Phosphorylation	ARKPLSESLGRDSKK CCCCHHHHCCCCCCC	32.52	28066266
59	Phosphorylation	LIASVAGSVERVNKL HHHHHHCCHHHHHHH	15.86	29514104
65	Acetylation	GSVERVNKLICVKAL CCHHHHHHHHHHHHH	36.05	22826441
94	Malonylation	RITEVQQKRWKVETN EEHHHHHHCCCCCCC	43.04	26320211
102	Phosphorylation	RWKVETNSRLDSVLL CCCCCCCCCHHHHHH	41.46	-
106	Phosphorylation	ETNSRLDSVLLLSSM CCCCCHHHHHHHHHC	21.18	-
111	Phosphorylation	LDSVLLLSSMNLPGG HHHHHHHHHCCCCCC	27.75	-
124	Phosphorylation	GGELRRRSAEDELAM CCHHCCCCHHHHHHH	33.91	26824392
175	Phosphorylation	QGVLVQVSPSLVKRQ CCEEEEECHHHHHCC	7.53	26745281
177	Phosphorylation	VLVQVSPSLVKRQKT EEEEECHHHHHCCCC	37.98	23984901

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

Oops, there are no upstream regulatory protein records of EXOS2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS2_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 EXOS2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EXOS2_MOUSE !!

Drug and Disease Associations

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