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Protein

Exosome complex component RRP45

Gene

Exosc9

Organism
Mus musculus (Mouse)
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. EXOSC9 binds to ARE-containing RNAs (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease, RNA-binding
Biological processrRNA processing

Enzyme and pathway databases

ReactomeiR-MMU-429958 mRNA decay by 3' to 5' exoribonuclease
R-MMU-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-MMU-450604 KSRP (KHSRP) binds and destabilizes mRNA
R-MMU-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP45
Alternative name(s):
Autoantigen PM/Scl 1
Exosome component 9
P75 polymyositis-scleroderma overlap syndrome-associated autoantigen
Polymyositis/scleroderma autoantigen 1
Polymyositis/scleroderma autoantigen 75 kDa
Short name:
PM/Scl-75
Gene namesi
Name:Exosc9
Synonyms:Pmscl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1355319 Exosc9

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001399721 – 438Exosome complex component RRP45Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei65PhosphoserineBy similarity1
Modified residuei297N6-acetyllysine; alternateBy similarity1
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei306PhosphoserineBy similarity1
Modified residuei346PhosphoserineBy similarity1
Modified residuei393PhosphoserineCombined sources1
Modified residuei395PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9JHI7
MaxQBiQ9JHI7
PaxDbiQ9JHI7
PeptideAtlasiQ9JHI7
PRIDEiQ9JHI7

PTM databases

iPTMnetiQ9JHI7
PhosphoSitePlusiQ9JHI7

Expressioni

Gene expression databases

BgeeiENSMUSG00000027714
CleanExiMM_EXOSC9
ExpressionAtlasiQ9JHI7 baseline and differential
GenevisibleiQ9JHI7 MM

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 (via C-terminus region) with SETX (via N-terminus domain); the interaction enhances SETX sumoylation (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9JHI7, 1 interactor
STRINGi10090.ENSMUSP00000029269

Structurei

3D structure databases

ProteinModelPortaliQ9JHI7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiKOG1614 Eukaryota
COG2123 LUCA
GeneTreeiENSGT00530000063093
HOGENOMiHOG000229504
HOVERGENiHBG051523
InParanoidiQ9JHI7
KOiK03678
OMAiMFMNSNL
OrthoDBiEOG091G08FZ
PhylomeDBiQ9JHI7
TreeFamiTF300092

Family and domain databases

CDDicd11368 RNase_PH_RRP45, 1 hit
Gene3Di3.30.230.70, 1 hit
InterProiView protein in InterPro
IPR001247 ExoRNase_PH_dom1
IPR015847 ExoRNase_PH_dom2
IPR036345 ExoRNase_PH_dom2_sf
IPR027408 PNPase/RNase_PH_dom_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR033100 Rrp45
PfamiView protein in Pfam
PF01138 RNase_PH, 1 hit
PF03725 RNase_PH_C, 1 hit
SUPFAMiSSF54211 SSF54211, 2 hits
SSF55666 SSF55666, 1 hit

Sequencei

Sequence statusi: Complete.

Q9JHI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL
60 70 80 90 100
GKTRVLGQVS CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV
110 120 130 140 150
KLNRLLERCL RNSKCIDTES LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS
160 170 180 190 200
IAAIVALCHF RRPDVSVQGE EVTLYTPEER DPVPLSIHHM PICVSFAFFQ
210 220 230 240 250
QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI MLLKDQVFRC
260 270 280 290 300
SKIAGVKVAE ITELIQKALE NDQRVRKEGG KFGFAESIAN QRITAFKMET
310 320 330 340 350
APIDTSNIEE RAEEIIAEAE PPPEVVSQPV LWTPGTAQIG DGIENSWGDL
360 370 380 390 400
EDSEKEEEEE EGGIDEAVIL DDTKMDTGEV SDIGSQGAPI VLSDSEEEEM
410 420 430
IILEPEKNPK KIRAQTSANQ KAPSKGQGKR KKKKRTAN
Length:438
Mass (Da):48,937
Last modified:October 1, 2000 - v1
Checksum:i7AAE63DBF12F5149
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152841 mRNA Translation: AAF73218.1
AF152842 mRNA Translation: AAF73219.1
BC005622 mRNA Translation: AAH05622.1
BC052156 mRNA Translation: AAH52156.1
AK011636 mRNA Translation: BAB27749.1
CCDSiCCDS17312.1
RefSeqiNP_062266.1, NM_019393.2
UniGeneiMm.116711

Genome annotation databases

EnsembliENSMUST00000029269; ENSMUSP00000029269; ENSMUSG00000027714
GeneIDi50911
KEGGimmu:50911
UCSCiuc008ozm.1 mouse

Similar proteinsi

Entry informationi

Entry nameiEXOS9_MOUSE
AccessioniPrimary (citable) accession number: Q9JHI7
Secondary accession number(s): Q9CSZ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: March 28, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health