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P56960 (EXOSX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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 component 10

EC=3.1.13.-
Alternative name(s):
Autoantigen PM/Scl 2 homolog
Polymyositis/scleroderma autoantigen 2 homolog
Gene names
Name:Exosc10
Synonyms:Pmscl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative 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. EXOSC10 has 3'-5' exonuclease activity By similarity. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of SKIV2L2, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA By similarity.

Subunit structure

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Interacts with C1D and MPHOSPH6 By similarity. Interacts with ALYREF/THOC4 By similarity.

Subcellular location

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

Sequence similarities

Contains 1 HRDC domain.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
rRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   LigandRNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCUT catabolic process

Inferred from electronic annotation. Source: Ensembl

dosage compensation by inactivation of X chromosome

Inferred from mutant phenotype PubMed 16789828. Source: MGI

histone mRNA catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

maturation of 5.8S rRNA

Inferred from electronic annotation. Source: Ensembl

nuclear polyadenylation-dependent rRNA catabolic process

Inferred from electronic annotation. Source: Ensembl

nuclear retention of unspliced pre-mRNA at the site of transcription

Inferred from electronic annotation. Source: Ensembl

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

exosome (RNase complex)

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear exosome (RNase complex)

Inferred from electronic annotation. Source: InterPro

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

transcriptionally active chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3'-5' exonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

exoribonuclease activity

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887Exosome component 10
PRO_0000087134

Regions

Domain503 – 58381HRDC

Experimental info

Sequence conflict7921I → V in AAF01779. Ref.1
Sequence conflict7921I → V in AAF01781. Ref.1
Sequence conflict8601C → F in AAF01779. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P56960 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 173164944163620C

FASTA887100,942
        10         20         30         40         50         60 
MAPPSPREHQ SAPATSATKP DAEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY 

        70         80         90        100        110        120 
DFYRSFPAFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDTNDVI 

       130        140        150        160        170        180 
LERVGMLLDE ASGVNKHQQP VLPAGLQVPK TIVSSWNRKA GEYGKKAKSE TFRLLHAKNI 

       190        200        210        220        230        240 
VRPQLRFREK IDNSNTPFLP KIFVKPNARK PLPLALSKER RERPQDRPED LDVPPALADF 

       250        260        270        280        290        300 
IHQQRTQQVE QDMFAHPYQY ELDHFTPPQS VLQRPKPQLY RAVGETPCHL VSSLDELVEL 

       310        320        330        340        350        360 
NEKLLGCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFIV DTLELRSDMY ILNESLTDPA 

       370        380        390        400        410        420 
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLAR HSLDHLLRLY CGVESNKQYQ 

       430        440        450        460        470        480 
LADWRIRPLP EEMLSYARDD THYLLYIYDR MRLELWERGN HQPVQLQVVW QRSRDICLKK 

       490        500        510        520        530        540 
FVKPIFTDES YLELYRKQKK HLNSQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI 

       550        560        570        580        590        600 
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSENAAGV RKSGPLPSAE 

       610        620        630        640        650        660 
RLENDLFGPH DCSHAPPDNY QNTSTDGTLP LQKQPSLFTE GKEETSVDAG CLLATAVITL 

       670        680        690        700        710        720 
FSEPNTEEGG KTPLTVAQKK AQNIMQSFEN PFRMFLPSLE HKAHISQAAK FDPSSKIYEI 

       730        740        750        760        770        780 
SNRWKLASQV QVQKEPKEAT KKKVAEQTAA REEAKEEAAA GVLEQAIPVR QQAALENATK 

       790        800        810        820        830        840 
KRERATSDLR TIEQKQEKKR LKSSKKAKDP DPPGKDFSPY DYSQSDFRAF AGDSKSKPSS 

       850        860        870        880 
QFDPNKLAPS GKKGVGAKKC KQSVGNKSMS FAVGKSDRGF RHNWPKR 

« Hide

References

« Hide 'large scale' references
[1]"Structure and localization of mouse Pmscl1 and Pmscl2 genes."
Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.
Genomics 64:106-110(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ and BALB/c.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 395-400, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091392 mRNA. Translation: AAF01779.1.
AF091505 expand/collapse EMBL AC list , AF091506, AF092074, AF092075, AF092076, AF092077, AF092078, AF092079, AF092080, AF092081, AF092082, AF092083 Genomic DNA. Translation: AAF01781.1.
AL606969, AL713995 Genomic DNA. Translation: CAM21195.1.
AL713995, AL606969 Genomic DNA. Translation: CAM23945.1.
RefSeqNP_057908.2. NM_016699.2.
UniGeneMm.266635.

3D structure databases

ProteinModelPortalP56960.
SMRP56960. Positions 179-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP56960. 1 interaction.
MINTMINT-4094804.

PTM databases

PhosphoSiteP56960.

Proteomic databases

PaxDbP56960.
PRIDEP56960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017408; ENSMUSP00000017408; ENSMUSG00000017264.
GeneID50912.
KEGGmmu:50912.
UCSCuc008vut.2. mouse.

Organism-specific databases

CTD5394.
MGIMGI:1355322. Exosc10.

Phylogenomic databases

eggNOGCOG0349.
GeneTreeENSGT00390000015408.
HOGENOMHOG000001579.
HOVERGENHBG051524.
InParanoidB1ARY9.
KOK12591.
OMAGNKSMSF.
OrthoDBEOG7Z3F3S.
TreeFamTF105991.

Gene expression databases

ArrayExpressP56960.
BgeeP56960.
CleanExMM_EXOSC10.
GenevestigatorP56960.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view]
SMARTSM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]
SUPFAMSSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEPS50967. HRDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEXOSC10. mouse.
NextBio307899.
PROP56960.
SOURCESearch...

Entry information

Entry nameEXOSX_MOUSE
AccessionPrimary (citable) accession number: P56960
Secondary accession number(s): B1ARY9, Q9QYS8, Q9R0B1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 102 of the entry and version 2 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