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Protein

Exosome complex component RRP45

Gene

Exosc9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

  1. AU-rich element binding Source: MGI
  2. exonuclease activity Source: UniProtKB-KW
  3. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: MGI
  2. nuclear mRNA surveillance Source: MGI
  3. nuclear polyadenylation-dependent rRNA catabolic process Source: MGI
  4. nuclear-transcribed mRNA catabolic process Source: MGI
  5. positive regulation of cell growth Source: MGI
  6. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1355319. Exosc9.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity
Note: Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. exosome (RNase complex) Source: UniProtKB
  3. extracellular vesicular exosome Source: MGI
  4. intermediate filament cytoskeleton Source: MGI
  5. nuclear chromosome Source: UniProtKB
  6. nuclear exosome (RNase complex) Source: MGI
  7. nucleolus Source: UniProtKB
  8. nucleoplasm Source: UniProtKB
  9. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Exosome complex component RRP45PRO_0000139972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei297 – 2971N6-acetyllysineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9JHI7.
PaxDbiQ9JHI7.
PRIDEiQ9JHI7.

PTM databases

PhosphoSiteiQ9JHI7.

Expressioni

Gene expression databases

BgeeiQ9JHI7.
CleanExiMM_EXOSC9.
ExpressionAtlasiQ9JHI7. baseline and differential.
GenevestigatoriQ9JHI7.

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

Structurei

3D structure databases

ProteinModelPortaliQ9JHI7.
SMRiQ9JHI7. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051523.
InParanoidiQ9JHI7.
KOiK03678.
OMAiKMDTGVE.
OrthoDBiEOG7X9G70.
PhylomeDBiQ9JHI7.
TreeFamiTF300092.

Family and domain databases

InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
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.

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:September 30, 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9JHI7.
SMRiQ9JHI7. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9JHI7.

Proteomic databases

MaxQBiQ9JHI7.
PaxDbiQ9JHI7.
PRIDEiQ9JHI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5393.
MGIiMGI:1355319. Exosc9.

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051523.
InParanoidiQ9JHI7.
KOiK03678.
OMAiKMDTGVE.
OrthoDBiEOG7X9G70.
PhylomeDBiQ9JHI7.
TreeFamiTF300092.

Enzyme and pathway databases

ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.
REACT_300665. KSRP destabilizes mRNA.

Miscellaneous databases

NextBioi307895.
PROiQ9JHI7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHI7.
CleanExiMM_EXOSC9.
ExpressionAtlasiQ9JHI7. baseline and differential.
GenevestigatoriQ9JHI7.

Family and domain databases

InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and localization of mouse Pmscl1 and Pmscl2 genes."
    Bliskovski V., Liddell R., Ramsay E.S., Miller M.J., Mock B.A.
    Genomics 64:106-110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain and Spleen.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo and Mammary gland.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395.
    Strain: C57BL/6J.
    Tissue: Embryo.

Entry informationi

Entry nameiEXOS9_MOUSE
AccessioniPrimary (citable) accession number: Q9JHI7
Secondary accession number(s): Q9CSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2001
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.