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Q96B26 (EXOS8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome complex component RRP43
Alternative name(s):
Exosome component 8
Opa-interacting protein 2
Short name=OIP-2
Ribosomal RNA-processing protein 43
p9
Gene names
Name:EXOSC8
Synonyms:OIP2, RRP43
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. EXOSC8 binds to ARE-containing RNAs. Ref.8 Ref.9

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. Binds outer membrane protein opap from Neisseria gonorrhoeae. Ref.5 Ref.10

Subcellular location

Cytoplasm. Nucleus. Nucleusnucleolus By similarity Ref.9.

Sequence similarities

Belongs to the RNase PH family.

Caution

The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.

Sequence caution

The sequence CAI14013.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAX08581.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EXOSC3Q9NQT53EBI-371922,EBI-371866
EXOSC5Q9NQT44EBI-371922,EBI-371876

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 276275Exosome complex component RRP43
PRO_0000139967

Amino acid modifications

Modified residue21N-acetylalanine Ref.12

Experimental info

Sequence conflict265 – 27612LMDEV…SMKPK → TDG in AAC39558. Ref.4

Secondary structure

............................................ 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96B26 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: FC8F5BAE74A1FF55

FASTA27630,040
        10         20         30         40         50         60 
MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL VKLGNTTVIC 

        70         80         90        100        110        120 
GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE EAQVASQFIA DVIENSQIIQ 

       130        140        150        160        170        180 
KEDLCISPGK LVWVLYCDLI CLDYDGNILD ACTFALLAAL KNVQLPEVTI NEETALAEVN 

       190        200        210        220        230        240 
LKKKSYLNIR THPVATSFAV FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG 

       250        260        270 
SGLTGAKLQD CMSRAVTRHK EVKKLMDEVI KSMKPK 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Uterus.
[4]"Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth."
Williams J.M., Chen G.-C., Zhu L., Rest R.F.
Mol. Microbiol. 27:171-186(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-276.
[5]"AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
[6]"Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
J. Mol. Biol. 323:653-663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN INTERACTION.
[7]"A protein interaction framework for human mRNA degradation."
Lehner B., Sanderson C.M.
Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN INTERACTION.
[8]"Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome."
Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., Wilusz J.
RNA 12:1810-1816(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ARE-CONTAINING MRNA-BINDING.
[9]"Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways."
van Dijk E.L., Schilders G., Pruijn G.J.
RNA 13:1027-1035(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
[10]"Dis3-like 1: a novel exoribonuclease associated with the human exosome."
Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"Reconstitution, activities, and structure of the eukaryotic RNA exosome."
Liu Q., Greimann J.C., Lima C.D.
Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
[14]Erratum
Liu Q., Greimann J.C., Lima C.D.
Cell 131:188-189(2007)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL138706 Genomic DNA. Translation: CAI14013.1. Sequence problems.
CH471075 Genomic DNA. Translation: EAX08581.1. Sequence problems.
BC020773 mRNA. Translation: AAH20773.1.
AF025438 mRNA. Translation: AAC39558.1.
RefSeqNP_852480.1. NM_181503.2.
UniGeneHs.294041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35C1-276[»]
ProteinModelPortalQ96B26.
SMRQ96B26. Positions 7-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116468. 26 interactions.
IntActQ96B26. 24 interactions.
MINTMINT-4536555.
STRING9606.ENSP00000374354.

PTM databases

PhosphoSiteQ96B26.

Polymorphism databases

DMDM21759409.

2D gel databases

SWISS-2DPAGEQ96B26.

Proteomic databases

PaxDbQ96B26.
PeptideAtlasQ96B26.
PRIDEQ96B26.

Protocols and materials databases

DNASU11340.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389704; ENSP00000374354; ENSG00000120699.
GeneID11340.
KEGGhsa:11340.
UCSCuc001uwa.3. human.

Organism-specific databases

CTD11340.
GeneCardsGC13P037572.
HGNCHGNC:17035. EXOSC8.
HPACAB034240.
HPA039702.
HPA043942.
MIM606019. gene.
neXtProtNX_Q96B26.
PharmGKBPA134922251.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2123.
HOGENOMHOG000229504.
HOVERGENHBG051522.
InParanoidQ96B26.
KOK12586.
OMAYVDATCI.
OrthoDBEOG7D59PC.
PhylomeDBQ96B26.
TreeFamTF320415.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96B26.
BgeeQ96B26.
CleanExHS_EXOSC8.
GenevestigatorQ96B26.

Family and domain databases

Gene3D3.30.230.70. 1 hit.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ96B26.
GeneWikiExosome_component_8.
GenomeRNAi11340.
NextBio43089.
PROQ96B26.
SOURCESearch...

Entry information

Entry nameEXOS8_HUMAN
AccessionPrimary (citable) accession number: Q96B26
Secondary accession number(s): O43480, Q5TBA5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM