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Protein

Exosome complex component CSL4

Gene

EXOSC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.

GO - Molecular functioni

  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processrRNA processing

Enzyme and pathway databases

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 CSL4
Alternative name(s):
Exosome component 1
Gene namesi
Name:EXOSC1
Synonyms:CSL4
ORF Names:CGI-108
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000171311.12
HGNCiHGNC:17286 EXOSC1
MIMi606493 gene
neXtProtiNX_Q9Y3B2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi51013
OpenTargetsiENSG00000171311
PharmGKBiPA134900737

Polymorphism and mutation databases

BioMutaiEXOSC1
DMDMi14285410

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871271 – 195Exosome complex component CSL4Add BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21PhosphoserineCombined sources1
Modified residuei98PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y3B2
MaxQBiQ9Y3B2
PaxDbiQ9Y3B2
PeptideAtlasiQ9Y3B2
PRIDEiQ9Y3B2
ProteomicsDBi86000

PTM databases

iPTMnetiQ9Y3B2
PhosphoSitePlusiQ9Y3B2

Expressioni

Gene expression databases

BgeeiENSG00000171311
CleanExiHS_EXOSC1
ExpressionAtlasiQ9Y3B2 baseline and differential
GenevisibleiQ9Y3B2 HS

Organism-specific databases

HPAiHPA038370

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 EXOSC5, EXOSC7 and EXOSC10. Interacts with DDX60.4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi119220, 62 interactors
ComplexPortaliCPX-476 Nuclear exosome complex, DIS3-EXOSC10 variant
CPX-591 Nucleolar exosome complex, EXOSC10 variant
CPX-592 Cytoplasmic exosome complex, DIS3L variant
CPX-593 Exosome complex, DIS3 variant
CPX-600 Cytoplasmic exosome complex, DIS3L-EXOSC10 variant
CORUMiQ9Y3B2
DIPiDIP-31261N
IntActiQ9Y3B2, 59 interactors
MINTiQ9Y3B2
STRINGi9606.ENSP00000359939

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 16Combined sources4
Turni17 – 19Combined sources3
Beta strandi23 – 25Combined sources3
Beta strandi27 – 29Combined sources3
Beta strandi32 – 34Combined sources3
Beta strandi41 – 45Combined sources5
Beta strandi49 – 52Combined sources4
Beta strandi70 – 78Combined sources9
Beta strandi80 – 93Combined sources14
Beta strandi103 – 106Combined sources4
Helixi107 – 109Combined sources3
Helixi118 – 120Combined sources3
Beta strandi124 – 135Combined sources12
Beta strandi142 – 145Combined sources4
Beta strandi148 – 150Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi165 – 168Combined sources4
Beta strandi171 – 173Combined sources3
Turni175 – 178Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35I1-195[»]
ProteinModelPortaliQ9Y3B2
SMRiQ9Y3B2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3B2

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 147S1 motifAdd BLAST82

Sequence similaritiesi

Belongs to the CSL4 family.Curated

Phylogenomic databases

eggNOGiKOG3409 Eukaryota
COG1096 LUCA
GeneTreeiENSGT00390000015287
HOGENOMiHOG000177330
HOVERGENiHBG051516
InParanoidiQ9Y3B2
KOiK07573
OMAiKPGFHLT
OrthoDBiEOG091G0NLQ
PhylomeDBiQ9Y3B2
TreeFamiTF316607

Family and domain databases

InterProiView protein in InterPro
IPR019495 EXOSC1
IPR025721 Exosome_cplx_N_dom
IPR012340 NA-bd_OB-fold
IPR022967 S1_dom
PfamiView protein in Pfam
PF14382 ECR1_N, 1 hit
PF10447 EXOSC1, 1 hit
SMARTiView protein in SMART
SM00316 S1, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit

Sequencei

Sequence statusi: Complete.

Q9Y3B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKSSENGAL
60 70 80 90 100
PVVSVVRETE SQLLPDVGAI VTCKVSSINS RFAKVHILYV GSMPLKNSFR
110 120 130 140 150
GTIRKEDVRA TEKDKVEIYK SFRPGDIVLA KVISLGDAQS NYLLTTAENE
160 170 180 190
LGVVVAHSES GIQMVPISWC EMQCPKTHTK EFRKVARVQP EFLQT
Length:195
Mass (Da):21,452
Last modified:November 1, 1999 - v1
Checksum:iE9C3B0A66F911195
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151866 mRNA Translation: AAD34103.1
AK313717 mRNA Translation: BAG36460.1
AL355490 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49936.1
BC022067 mRNA Translation: AAH22067.1
CCDSiCCDS7459.1
RefSeqiNP_001305291.1, NM_001318362.1
NP_001305292.1, NM_001318363.1
NP_001305293.1, NM_001318364.1
NP_001305294.1, NM_001318365.1
NP_001305295.1, NM_001318366.1
NP_057130.1, NM_016046.4
UniGeneiHs.632089

Genome annotation databases

EnsembliENST00000370902; ENSP00000359939; ENSG00000171311
GeneIDi51013
KEGGihsa:51013
UCSCiuc001kni.4 human

Similar proteinsi

Entry informationi

Entry nameiEXOS1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3B2
Secondary accession number(s): B2R9B3, Q5JTH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1999
Last modified: June 20, 2018
This is version 163 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

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