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Q96B26

- EXOS8_HUMAN

UniProt

Q96B26 - EXOS8_HUMAN

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Protein

Exosome complex component RRP43

Gene

EXOSC8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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. EXOSC8 binds to ARE-containing RNAs.2 Publications

GO - Molecular functioni

  1. AU-rich element binding Source: UniProtKB

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EXOSC8
Synonyms:OIP2, RRP43
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:17035. EXOSC8.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. exosome (RNase complex) Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134922251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 276275Exosome complex component RRP43PRO_0000139967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96B26.
PaxDbiQ96B26.
PeptideAtlasiQ96B26.
PRIDEiQ96B26.

2D gel databases

SWISS-2DPAGEQ96B26.

PTM databases

PhosphoSiteiQ96B26.

Expressioni

Gene expression databases

BgeeiQ96B26.
CleanExiHS_EXOSC8.
ExpressionAtlasiQ96B26. baseline and differential.
GenevestigatoriQ96B26.

Organism-specific databases

HPAiCAB034240.
HPA039702.
HPA043942.

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. Binds outer membrane protein opap from Neisseria gonorrhoeae.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC3Q9NQT53EBI-371922,EBI-371866
EXOSC5Q9NQT44EBI-371922,EBI-371876

Protein-protein interaction databases

BioGridi116468. 42 interactions.
DIPiDIP-31133N.
IntActiQ96B26. 24 interactions.
MINTiMINT-4536555.
STRINGi9606.ENSP00000374354.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 199Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi71 – 733Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 893Combined sources
Beta strandi95 – 973Combined sources
Helixi100 – 11617Combined sources
Helixi121 – 1244Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi133 – 14311Combined sources
Helixi150 – 16112Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi194 – 2007Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2093Combined sources
Turni212 – 2165Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi232 – 2387Combined sources
Helixi245 – 26723Combined sources
Turni268 – 2736Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35C1-276[»]
ProteinModelPortaliQ96B26.
SMRiQ96B26. Positions 7-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96B26.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051522.
InParanoidiQ96B26.
KOiK12586.
OMAiQAASQFI.
OrthoDBiEOG7D59PC.
PhylomeDBiQ96B26.
TreeFamiTF320415.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96B26-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL
60 70 80 90 100
VKLGNTTVIC GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE
110 120 130 140 150
EAQVASQFIA DVIENSQIIQ KEDLCISPGK LVWVLYCDLI CLDYDGNILD
160 170 180 190 200
ACTFALLAAL KNVQLPEVTI NEETALAEVN LKKKSYLNIR THPVATSFAV
210 220 230 240 250
FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG SGLTGAKLQD
260 270
CMSRAVTRHK EVKKLMDEVI KSMKPK
Length:276
Mass (Da):30,040
Last modified:December 1, 2001 - v1
Checksum:iFC8F5BAE74A1FF55
GO

Sequence cautioni

The sequence CAI14013.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAX08581.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 27612LMDEV…SMKPK → TDG in AAC39558. (PubMed:9466265)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31958.1.
RefSeqiNP_852480.1. NM_181503.2.
UniGeneiHs.294041.

Genome annotation databases

EnsembliENST00000389704; ENSP00000374354; ENSG00000120699.
GeneIDi11340.
KEGGihsa:11340.
UCSCiuc001uwa.3. human.

Polymorphism databases

DMDMi21759409.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS31958.1.
RefSeqi NP_852480.1. NM_181503.2.
UniGenei Hs.294041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NN6 X-ray 3.35 C 1-276 [» ]
ProteinModelPortali Q96B26.
SMRi Q96B26. Positions 7-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116468. 42 interactions.
DIPi DIP-31133N.
IntActi Q96B26. 24 interactions.
MINTi MINT-4536555.
STRINGi 9606.ENSP00000374354.

PTM databases

PhosphoSitei Q96B26.

Polymorphism databases

DMDMi 21759409.

2D gel databases

SWISS-2DPAGE Q96B26.

Proteomic databases

MaxQBi Q96B26.
PaxDbi Q96B26.
PeptideAtlasi Q96B26.
PRIDEi Q96B26.

Protocols and materials databases

DNASUi 11340.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389704 ; ENSP00000374354 ; ENSG00000120699 .
GeneIDi 11340.
KEGGi hsa:11340.
UCSCi uc001uwa.3. human.

Organism-specific databases

CTDi 11340.
GeneCardsi GC13P037572.
HGNCi HGNC:17035. EXOSC8.
HPAi CAB034240.
HPA039702.
HPA043942.
MIMi 606019. gene.
neXtProti NX_Q96B26.
PharmGKBi PA134922251.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2123.
GeneTreei ENSGT00530000063093.
HOGENOMi HOG000229504.
HOVERGENi HBG051522.
InParanoidi Q96B26.
KOi K12586.
OMAi QAASQFI.
OrthoDBi EOG7D59PC.
PhylomeDBi Q96B26.
TreeFami TF320415.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q96B26.
GeneWikii Exosome_component_8.
GenomeRNAii 11340.
NextBioi 43089.
PROi Q96B26.
SOURCEi Search...

Gene expression databases

Bgeei Q96B26.
CleanExi HS_EXOSC8.
ExpressionAtlasi Q96B26. baseline and differential.
Genevestigatori Q96B26.

Family and domain databases

Gene3Di 3.30.230.70. 1 hit.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
Pfami PF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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)

Entry informationi

Entry nameiEXOS8_HUMAN
AccessioniPrimary (citable) accession number: Q96B26
Secondary accession number(s): O43480, Q5TBA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3