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Q8VBV3 (EXOS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome complex component RRP4
Alternative name(s):
Exosome component 2
Ribosomal RNA-processing protein 4
Gene names
Name:Exosc2
Synonyms:Rrp4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with GTPBP1 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the RRP4 family.

Contains 1 S1 motif domain.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

exosome (RNase complex)

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 293293Exosome complex component RRP4
PRO_0000087130

Regions

Domain79 – 15981S1 motif

Amino acid modifications

Modified residue1241Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VBV3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 832C75F57980DDF8

FASTA29332,632
        10         20         30         40         50         60 
MALEMRLPKA RKPLSESLGR DSKKHLVVPG DTITTDTGFM RGHGTYMGEE KLIASVAGSV 

        70         80         90        100        110        120 
ERVNKLICVK ALKTRYNGEV GDIVVGRITE VQQKRWKVET NSRLDSVLLL SSMNLPGGEL 

       130        140        150        160        170        180 
RRRSAEDELA MRGFLQEGDL ISAEVQAVFS DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK 

       190        200        210        220        230        240 
RQKTHFHDLP CGASVILGNN GFIWIYPTPE HKDEDAGGFI ANLEPVALSD REVISRLRNC 

       250        260        270        280        290 
VVLLVTQRMM LFDTSILYCY EASLAHQIKD ILKPEVMEEI MLETRQRLLD QEG 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC021485 mRNA. Translation: AAH21485.1.
BC021807 mRNA. Translation: AAH21807.1.
RefSeqNP_659135.1. NM_144886.2.
UniGeneMm.150972.

3D structure databases

ProteinModelPortalQ8VBV3.
SMRQ8VBV3. Positions 25-293.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8VBV3.

Proteomic databases

PaxDbQ8VBV3.
PRIDEQ8VBV3.

Protocols and materials databases

DNASU227715.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038474; ENSMUSP00000043519; ENSMUSG00000039356.
GeneID227715.
KEGGmmu:227715.
UCSCuc008jdy.1. mouse.

Organism-specific databases

CTD23404.
MGIMGI:2385133. Exosc2.

Phylogenomic databases

eggNOGCOG1097.
GeneTreeENSGT00440000033656.
HOGENOMHOG000193685.
HOVERGENHBG051517.
InParanoidQ8VBV3.
KOK03679.
OMAPLKTRYN.
OrthoDBEOG7JX34R.
TreeFamTF105623.

Gene expression databases

ArrayExpressQ8VBV3.
BgeeQ8VBV3.
CleanExMM_EXOSC2.
GenevestigatorQ8VBV3.

Family and domain databases

InterProIPR025721. Exosome_cplx_N_dom.
IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR012340. NA-bd_OB-fold.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PANTHERPTHR21321. PTHR21321. 1 hit.
PfamPF14382. ECR1_N. 1 hit.
[Graphical view]
SMARTSM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

NextBio378776.
PROQ8VBV3.
SOURCESearch...

Entry information

Entry nameEXOS2_MOUSE
AccessionPrimary (citable) accession number: Q8VBV3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot