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Protein

Exosome complex component RRP43

Gene

EXOSC8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • AU-rich element binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120699-MONOMER.
ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-429958. mRNA decay by 3' to 5' exoribonuclease.
R-HSA-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17035. EXOSC8.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Nucleusnucleolus By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic exosome (RNase complex) Source: GO_Central
  • cytosol Source: Reactome
  • exosome (RNase complex) Source: UniProtKB
  • nuclear exosome (RNase complex) Source: GO_Central
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pontocerebellar hypoplasia 1C (PCH1C)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. EXOSC8 dysfunction causes myelin disruption through an imbalanced supply of myelin proteins due to dysregulation of their ARE-containing mRNAs (PubMed:24989451).1 Publication
Disease descriptionA severe autosomal recessive neurodegenerative disease characterized by cerebellar and corpus callosum hypoplasia, abnormal myelination of the central nervous system, and spinal motor neuron disease. Affected individuals manifest failure to thrive, severe muscle weakness, spasticity and psychomotor retardation. Vision and hearing are impaired.
See also OMIM:616081
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0725582A → V in PCH1C. 1 PublicationCorresponds to variant rs606231285dbSNPEnsembl.1
Natural variantiVAR_072559272S → T in PCH1C. 1 PublicationCorresponds to variant rs36027220dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi11340.
MalaCardsiEXOSC8.
MIMi616081. phenotype.
OpenTargetsiENSG00000120699.
Orphaneti2254. Pontocerebellar hypoplasia type 1.
PharmGKBiPA134922251.

Polymorphism and mutation databases

BioMutaiEXOSC8.
DMDMi21759409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001399672 – 276Exosome complex component RRP43Add BLAST275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96B26.
MaxQBiQ96B26.
PaxDbiQ96B26.
PeptideAtlasiQ96B26.
PRIDEiQ96B26.
TopDownProteomicsiQ96B26.

2D gel databases

SWISS-2DPAGEQ96B26.

PTM databases

iPTMnetiQ96B26.
PhosphoSitePlusiQ96B26.

Expressioni

Gene expression databases

BgeeiENSG00000120699.
CleanExiHS_EXOSC8.
ExpressionAtlasiQ96B26. baseline and differential.
GenevisibleiQ96B26. HS.

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
itself4EBI-371922,EBI-371922
AENQ8WTP83EBI-371922,EBI-8637627
ATF2P153363EBI-371922,EBI-1170906
COL23A1Q86Y223EBI-371922,EBI-373279
COX5AP206743EBI-371922,EBI-715032
DUSP23Q9BVJ75EBI-371922,EBI-724940
EXOSC1Q9Y3B24EBI-371922,EBI-371892
EXOSC3Q9NQT53EBI-371922,EBI-371866
EXOSC5Q9NQT414EBI-371922,EBI-371876
FAM90A1Q86YD75EBI-371922,EBI-6658203
FRG1Q143313EBI-371922,EBI-2515248
MORN4Q8WVZ33EBI-371922,EBI-10277137
OTUD4Q018043EBI-371922,EBI-1054396
RELQ048643EBI-371922,EBI-307352
SNRPCQ5TAL43EBI-371922,EBI-10246938
TCEA2Q155603EBI-371922,EBI-710310
TCEA2Q86VL03EBI-371922,EBI-10259904
TFAP4Q016645EBI-371922,EBI-2514218
TXNDC17Q9BRA25EBI-371922,EBI-1055906
TXNDC9O145305EBI-371922,EBI-707554

Protein-protein interaction databases

BioGridi116468. 67 interactors.
DIPiDIP-31133N.
IntActiQ96B26. 73 interactors.
MINTiMINT-4536555.
STRINGi9606.ENSP00000374354.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 19Combined sources9
Beta strandi37 – 39Combined sources3
Beta strandi43 – 53Combined sources11
Beta strandi56 – 66Combined sources11
Beta strandi71 – 73Combined sources3
Beta strandi80 – 84Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi95 – 97Combined sources3
Helixi100 – 116Combined sources17
Helixi121 – 124Combined sources4
Beta strandi126 – 128Combined sources3
Beta strandi133 – 143Combined sources11
Helixi150 – 161Combined sources12
Beta strandi172 – 175Combined sources4
Beta strandi194 – 200Combined sources7
Turni202 – 204Combined sources3
Beta strandi207 – 209Combined sources3
Turni212 – 216Combined sources5
Beta strandi219 – 226Combined sources8
Beta strandi232 – 238Combined sources7
Helixi245 – 267Combined sources23
Turni268 – 273Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ96B26.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiKOG1613. Eukaryota.
COG2123. LUCA.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051522.
InParanoidiQ96B26.
KOiK12586.
OMAiITRHKEV.
OrthoDBiEOG091G0JEJ.
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.
IPR033196. Rrp43.
[Graphical view]
PANTHERiPTHR11097:SF9. PTHR11097:SF9. 1 hit.
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 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAX08581 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti265 – 276LMDEV…SMKPK → TDG in AAC39558 (PubMed:9466265).CuratedAdd BLAST12

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0725582A → V in PCH1C. 1 PublicationCorresponds to variant rs606231285dbSNPEnsembl.1
Natural variantiVAR_072559272S → T in PCH1C. 1 PublicationCorresponds to variant rs36027220dbSNPEnsembl.1

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.5. human.

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.
CCDSiCCDS31958.1.
RefSeqiNP_852480.1. NM_181503.2.
UniGeneiHs.294041.

3D structure databases

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

Protein-protein interaction databases

BioGridi116468. 67 interactors.
DIPiDIP-31133N.
IntActiQ96B26. 73 interactors.
MINTiMINT-4536555.
STRINGi9606.ENSP00000374354.

PTM databases

iPTMnetiQ96B26.
PhosphoSitePlusiQ96B26.

Polymorphism and mutation databases

BioMutaiEXOSC8.
DMDMi21759409.

2D gel databases

SWISS-2DPAGEQ96B26.

Proteomic databases

EPDiQ96B26.
MaxQBiQ96B26.
PaxDbiQ96B26.
PeptideAtlasiQ96B26.
PRIDEiQ96B26.
TopDownProteomicsiQ96B26.

Protocols and materials databases

DNASUi11340.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389704; ENSP00000374354; ENSG00000120699.
GeneIDi11340.
KEGGihsa:11340.
UCSCiuc001uwa.5. human.

Organism-specific databases

CTDi11340.
DisGeNETi11340.
GeneCardsiEXOSC8.
HGNCiHGNC:17035. EXOSC8.
HPAiCAB034240.
HPA039702.
HPA043942.
MalaCardsiEXOSC8.
MIMi606019. gene.
616081. phenotype.
neXtProtiNX_Q96B26.
OpenTargetsiENSG00000120699.
Orphaneti2254. Pontocerebellar hypoplasia type 1.
PharmGKBiPA134922251.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1613. Eukaryota.
COG2123. LUCA.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051522.
InParanoidiQ96B26.
KOiK12586.
OMAiITRHKEV.
OrthoDBiEOG091G0JEJ.
PhylomeDBiQ96B26.
TreeFamiTF320415.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120699-MONOMER.
ReactomeiR-HSA-380994. ATF4 activates genes.
R-HSA-429958. mRNA decay by 3' to 5' exoribonuclease.
R-HSA-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
R-HSA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Miscellaneous databases

EvolutionaryTraceiQ96B26.
GeneWikiiExosome_component_8.
GenomeRNAii11340.
PROiQ96B26.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120699.
CleanExiHS_EXOSC8.
ExpressionAtlasiQ96B26. baseline and differential.
GenevisibleiQ96B26. HS.

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.
IPR033196. Rrp43.
[Graphical view]
PANTHERiPTHR11097:SF9. PTHR11097:SF9. 1 hit.
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetiSearch...

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 30, 2016
This is version 149 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.