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Q9CRA8

- EXOS5_MOUSE

UniProt

Q9CRA8 - EXOS5_MOUSE

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Protein
Exosome complex component RRP46
Gene
Exosc5, D7Wsu180e, Rrp46
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 By similarity.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA deamination Source: Ensembl
  2. RNA catabolic process Source: MGI
  3. defense response to virus Source: Ensembl
  4. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Ensembl
  5. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP46
Alternative name(s):
Exosome component 5
Ribosomal RNA-processing protein 46
Gene namesi
Name:Exosc5
Synonyms:D7Wsu180e, Rrp46
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:107889. Exosc5.

Subcellular locationi

Nucleusnucleolus By similarity. Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. exosome (RNase complex) Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
  4. transcriptionally active chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Exosome complex component RRP46
PRO_0000139976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9CRA8.
PRIDEiQ9CRA8.

PTM databases

PhosphoSiteiQ9CRA8.

Expressioni

Gene expression databases

BgeeiQ9CRA8.
CleanExiMM_EXOSC5.
GenevestigatoriQ9CRA8.

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 EXOSC1. Interacts with GTPBP1 By similarity. Interacts with ZC3HAV1 By similarity. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner By similarity.

Protein-protein interaction databases

BioGridi205707. 1 interaction.
IntActiQ9CRA8. 3 interactions.
MINTiMINT-1765755.

Structurei

3D structure databases

ProteinModelPortaliQ9CRA8.
SMRiQ9CRA8. Positions 26-234.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.

Phylogenomic databases

eggNOGiCOG0689.
GeneTreeiENSGT00550000075002.
HOGENOMiHOG000229515.
HOVERGENiHBG051520.
InParanoidiQ9CRA8.
KOiK12590.
OMAiTCEASLL.
OrthoDBiEOG7P8P90.
PhylomeDBiQ9CRA8.
TreeFamiTF315920.

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. 1 hit.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CRA8-1 [UniParc]FASTAAdd to Basket

« Hide

MEGAKRADAN LLTDTGTESS PRSPVCSLRH FACEQNLLSR PDGSASFLQG    50
DTSVLAGVYG PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLVRN 100
TCEAVVLGAL HPRTSITVVL QVVSDAGSLL ACCLNAACMA LVDAGVPMRA 150
LFCGVTCALD SDGNLVLDPT TKQEKEARAI LTFALDSAEQ KLLMSTTKGL 200
YSDAELQQCL AAAQAASQHI FRFYRESLQR RYSKS 235
Length:235
Mass (Da):25,194
Last modified:June 1, 2001 - v1
Checksum:i08752915141CF65D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → V in AAH34358. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK007372 mRNA. Translation: BAB24993.1.
AK006475 mRNA. Translation: BAB24607.1.
BC034358 mRNA. Translation: AAH34358.1.
CCDSiCCDS20990.1.
RefSeqiNP_613052.1. NM_138586.3.
UniGeneiMm.207484.
Mm.27853.

Genome annotation databases

EnsembliENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286.
GeneIDi27998.
KEGGimmu:27998.
UCSCiuc009fti.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK007372 mRNA. Translation: BAB24993.1 .
AK006475 mRNA. Translation: BAB24607.1 .
BC034358 mRNA. Translation: AAH34358.1 .
CCDSi CCDS20990.1.
RefSeqi NP_613052.1. NM_138586.3.
UniGenei Mm.207484.
Mm.27853.

3D structure databases

ProteinModelPortali Q9CRA8.
SMRi Q9CRA8. Positions 26-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205707. 1 interaction.
IntActi Q9CRA8. 3 interactions.
MINTi MINT-1765755.

PTM databases

PhosphoSitei Q9CRA8.

Proteomic databases

PaxDbi Q9CRA8.
PRIDEi Q9CRA8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079634 ; ENSMUSP00000078580 ; ENSMUSG00000061286 .
GeneIDi 27998.
KEGGi mmu:27998.
UCSCi uc009fti.2. mouse.

Organism-specific databases

CTDi 56915.
MGIi MGI:107889. Exosc5.

Phylogenomic databases

eggNOGi COG0689.
GeneTreei ENSGT00550000075002.
HOGENOMi HOG000229515.
HOVERGENi HBG051520.
InParanoidi Q9CRA8.
KOi K12590.
OMAi TCEASLL.
OrthoDBi EOG7P8P90.
PhylomeDBi Q9CRA8.
TreeFami TF315920.

Enzyme and pathway databases

Reactomei REACT_198696. KSRP destabilizes mRNA.

Miscellaneous databases

NextBioi 306496.
PROi Q9CRA8.
SOURCEi Search...

Gene expression databases

Bgeei Q9CRA8.
CleanExi MM_EXOSC5.
Genevestigatori Q9CRA8.

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. 1 hit.
SSF55666. SSF55666. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas and Testis.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEXOS5_MOUSE
AccessioniPrimary (citable) accession number: Q9CRA8
Secondary accession number(s): Q8K1J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 104 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

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