EXOS3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS3_MOUSE
• UniProt AC: Q7TQK4
• Protein Name: Exosome complex component RRP40
• Gene Name: Exosc3
• Organism: Mus musculus (Mouse).
• Sequence Length: 274
• 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. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5 (By similarity)..
• Protein Sequence: MAEVLSAGPESVAGCRARAVHKVLNQVVLPGEELVLPDHEDVDGLGGAGEQPLRLNAGARPRLRVVCGPGLRRCGDRLLVTKCGRLRHKEPSGGGGGVYWVDSQQKRYVPVKGDHVIGIVIAKSGDIFKVDVGGSEPASLSYLAFEGATKRNRPNVQVGDLIYGQCVVANKDMEPEMVCIDSCGRANGMGVIGQDGLLFKVTLGLIRKLLAPDCEIVQELGKLYPLEIVFGMNGRIWVKAKTIQQTLILANVLEACEHMTTEQRKQIFARLAES

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	Acetylation	------MAEVLSAGP ------CCCHHCCCH	18.66	-
6	Phosphorylation	--MAEVLSAGPESVA --CCCHHCCCHHHHC	36.03	30635358
92	Phosphorylation	RLRHKEPSGGGGGVY EEECCCCCCCCCCEE	51.68	26643407
124	Phosphorylation	IGIVIAKSGDIFKVD EEEEEECCCCEEEEE	32.45	29895711
135	Phosphorylation	FKVDVGGSEPASLSY EEEECCCCCCCCHHH	34.18	29895711
141	Phosphorylation	GSEPASLSYLAFEGA CCCCCCHHHHHHCCC	18.66	-
142	Phosphorylation	SEPASLSYLAFEGAT CCCCCHHHHHHCCCC	13.82	29895711
150	Ubiquitination	LAFEGATKRNRPNVQ HHHCCCCCCCCCCCC	47.33	-
208	Acetylation	VTLGLIRKLLAPDCE HHHHHHHHHHCCCCH	40.64	22826441

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

Oops, there are no upstream regulatory protein records of EXOS3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS3_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 EXOS3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EXOS3_MOUSE !!

Drug and Disease Associations

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