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Q8VBV3

- EXOS2_MOUSE

UniProt

Q8VBV3 - EXOS2_MOUSE

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Protein
Exosome complex component RRP4
Gene
Exosc2, Rrp4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. positive regulation of cell growth Source: Ensembl
  2. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP4
Alternative name(s):
Exosome component 2
Ribosomal RNA-processing protein 4
Gene namesi
Name:Exosc2
Synonyms:Rrp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2385133. Exosc2.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. exosome (RNase complex) Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Exosome complex component RRP4
PRO_0000087130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VBV3.
PaxDbiQ8VBV3.
PRIDEiQ8VBV3.

PTM databases

PhosphoSiteiQ8VBV3.

Expressioni

Gene expression databases

ArrayExpressiQ8VBV3.
BgeeiQ8VBV3.
CleanExiMM_EXOSC2.
GenevestigatoriQ8VBV3.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ8VBV3.
SMRiQ8VBV3. Positions 25-293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 15981S1 motif
Add
BLAST

Sequence similaritiesi

Belongs to the RRP4 family.
Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1097.
GeneTreeiENSGT00440000033656.
HOGENOMiHOG000193685.
HOVERGENiHBG051517.
InParanoidiQ8VBV3.
KOiK03679.
OMAiSRLRNCV.
OrthoDBiEOG7JX34R.
PhylomeDBiQ8VBV3.
TreeFamiTF105623.

Family and domain databases

InterProiIPR025721. Exosome_cplx_N_dom.
IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PANTHERiPTHR21321. PTHR21321. 1 hit.
PfamiPF14382. ECR1_N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8VBV3-1 [UniParc]FASTAAdd to Basket

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MALEMRLPKA RKPLSESLGR DSKKHLVVPG DTITTDTGFM RGHGTYMGEE    50
KLIASVAGSV ERVNKLICVK ALKTRYNGEV GDIVVGRITE VQQKRWKVET 100
NSRLDSVLLL SSMNLPGGEL RRRSAEDELA MRGFLQEGDL ISAEVQAVFS 150
DGAVSLHTRS LKYGKLGQGV LVQVSPSLVK RQKTHFHDLP CGASVILGNN 200
GFIWIYPTPE HKDEDAGGFI ANLEPVALSD REVISRLRNC VVLLVTQRMM 250
LFDTSILYCY EASLAHQIKD ILKPEVMEEI MLETRQRLLD QEG 293
Length:293
Mass (Da):32,632
Last modified:March 1, 2002 - v1
Checksum:i832C75F57980DDF8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC021485 mRNA. Translation: AAH21485.1.
BC021807 mRNA. Translation: AAH21807.1.
CCDSiCCDS15900.1.
RefSeqiNP_659135.1. NM_144886.2.
UniGeneiMm.150972.

Genome annotation databases

EnsembliENSMUST00000038474; ENSMUSP00000043519; ENSMUSG00000039356.
GeneIDi227715.
KEGGimmu:227715.
UCSCiuc008jdy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC021485 mRNA. Translation: AAH21485.1 .
BC021807 mRNA. Translation: AAH21807.1 .
CCDSi CCDS15900.1.
RefSeqi NP_659135.1. NM_144886.2.
UniGenei Mm.150972.

3D structure databases

ProteinModelPortali Q8VBV3.
SMRi Q8VBV3. Positions 25-293.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8VBV3.

Proteomic databases

MaxQBi Q8VBV3.
PaxDbi Q8VBV3.
PRIDEi Q8VBV3.

Protocols and materials databases

DNASUi 227715.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038474 ; ENSMUSP00000043519 ; ENSMUSG00000039356 .
GeneIDi 227715.
KEGGi mmu:227715.
UCSCi uc008jdy.1. mouse.

Organism-specific databases

CTDi 23404.
MGIi MGI:2385133. Exosc2.

Phylogenomic databases

eggNOGi COG1097.
GeneTreei ENSGT00440000033656.
HOGENOMi HOG000193685.
HOVERGENi HBG051517.
InParanoidi Q8VBV3.
KOi K03679.
OMAi SRLRNCV.
OrthoDBi EOG7JX34R.
PhylomeDBi Q8VBV3.
TreeFami TF105623.

Enzyme and pathway databases

Reactomei REACT_198696. KSRP destabilizes mRNA.

Miscellaneous databases

NextBioi 378776.
PROi Q8VBV3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VBV3.
Bgeei Q8VBV3.
CleanExi MM_EXOSC2.
Genevestigatori Q8VBV3.

Family and domain databases

InterProi IPR025721. Exosome_cplx_N_dom.
IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR022967. RNA-binding_domain_S1.
[Graphical view ]
PANTHERi PTHR21321. PTHR21321. 1 hit.
Pfami PF14382. ECR1_N. 1 hit.
[Graphical view ]
SMARTi SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiEXOS2_MOUSE
AccessioniPrimary (citable) accession number: Q8VBV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi