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Q9CSH3

- RRP44_MOUSE

UniProt

Q9CSH3 - RRP44_MOUSE

Protein

Exosome complex exonuclease RRP44

Gene

Dis3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 4 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Putative 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. DIS3 has both 3'-5' exonuclease and endonuclease activities By similarity.By similarity

    Cofactori

    Magnesium or manganese.By similarity

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. endonuclease activity Source: UniProtKB
    3. guanyl-nucleotide exchange factor activity Source: Ensembl
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. CUT catabolic process Source: Ensembl
    2. nucleic acid phosphodiester bond hydrolysis Source: GOC
    3. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    4. rRNA catabolic process Source: Ensembl
    5. rRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    Magnesium, Manganese, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198696. KSRP destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex exonuclease RRP44 (EC:3.1.13.-, EC:3.1.26.-)
    Alternative name(s):
    Protein DIS3 homolog
    Ribosomal RNA-processing protein 44
    Gene namesi
    Name:Dis3
    Synonyms:Kiaa1008, Rrp44
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1919912. Dis3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear exosome (RNase complex) Source: UniProtKB
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 958958Exosome complex exonuclease RRP44PRO_0000314757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei18 – 181N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9CSH3.
    PaxDbiQ9CSH3.
    PRIDEiQ9CSH3.

    PTM databases

    PhosphoSiteiQ9CSH3.

    Expressioni

    Gene expression databases

    BgeeiQ9CSH3.
    CleanExiMM_DIS3.
    GenevestigatoriQ9CSH3.

    Interactioni

    Subunit structurei

    Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms By similarity.By similarity

    Protein-protein interaction databases

    BioGridi215499. 1 interaction.
    IntActiQ9CSH3. 1 interaction.
    MINTiMINT-8178486.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CSH3.
    SMRiQ9CSH3. Positions 10-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 182119PINcAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RNR ribonuclease family.Curated
    Contains 1 PINc domain.Curated

    Phylogenomic databases

    eggNOGiCOG0557.
    GeneTreeiENSGT00530000063106.
    HOGENOMiHOG000191945.
    HOVERGENiHBG059397.
    InParanoidiQ9CSH3.
    KOiK12585.
    OMAiENANDRN.
    OrthoDBiEOG7KH9J1.
    PhylomeDBiQ9CSH3.
    TreeFamiTF105755.

    Family and domain databases

    Gene3Di3.40.50.1010. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR022966. RNase_II/R_CS.
    [Graphical view]
    PfamiPF13638. PIN_4. 1 hit.
    [Graphical view]
    SMARTiSM00670. PINc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 4 hits.
    SSF88723. SSF88723. 1 hit.
    PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9CSH3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSKTFLKK TRAGGVVKIV REHYLRDDIG CGAPACSACG GAHAGPALEL    50
    QPRDQASSLC PWPHYLLPDT NVLLHQIDVL EHPAIRNVIV LQTVMQEVRN 100
    RSAPIYKRIR DVTNNQEKHF YTFTNEHHKE TYIEQEQGEN ANDRNDRAIR 150
    VAAKWYNEHL KRVAADSQLQ VILITNDRKN KEKAVQEGIP AFTCEEYVKS 200
    LTANPELIDR LAYLSDEMNE IESGKIIFSE HLPLSKLQQG IKSGSYLQGT 250
    FRASRENYLE ATVWIHGDKE EEKEILIQGI KHLNRAVHED IVAVELLPRS 300
    QWVAPSSVVL DDEGQNEDDV EKDEERELLL KTAVSEKMLR PTGRVVGIIK 350
    RNWRPYCGML SKSDIKESRR HLFTPADKRI PRIRIETRQA SALEGRRIIV 400
    AIDGWPRNSR YPNGHFVKNL GDVGEKETET EVLLLEHDVP HQPFSQAVLS 450
    FLPRMPWSIT EEDMKNREDL RHLCVCSVDP PGCTDIDDAL HCRELSNGNL 500
    EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV PELLSSNLCS 550
    LRSNVDRLAF SCIWEMNHNA EILKTRFTKS VINSKASLTY AEAQMRIDSA 600
    AMNDDITTSL RGLNQLAKIL KKGRIEKGAL TLSSPEIRFH MDSETHDPID 650
    LQTKELRETN SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYD 700
    ILVKAAKSKN LQIKTDTAKS LADSLDRAES PDFPYLNTLL RILATRCMMQ 750
    AVYFCSGMDN DFHHYGLASP IYTHFTSPIR RYADIIVHRL LAVAIGADCT 800
    YPELTDKHKL SDICKNLNFR HKMAQYAQRA SVAFHTQLFF KSKGIVSEEA 850
    YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PKPRLAYDDE IPSLRIEGTV 900
    FHVFDKVKVK ITLDSSNLQH QKIRMALVEP QIPGINIPPN VADKALTAPG 950
    GKKRKLEK 958
    Length:958
    Mass (Da):108,838
    Last modified:January 15, 2008 - v4
    Checksum:i31045737557AB4AE
    GO

    Sequence cautioni

    The sequence BAC98069.1 differs from that shown. Reason: Incompletely spliced mRNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti586 – 5883ASL → VSV in BAC98069. (PubMed:14621295)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012840 mRNA. Translation: BAB28503.3.
    AK032091 mRNA. Translation: BAC27692.1.
    AK129259 Transcribed RNA. Translation: BAC98069.1. Sequence problems.
    CCDSiCCDS49555.1.
    RefSeqiNP_082591.2. NM_028315.2.
    UniGeneiMm.163339.

    Genome annotation databases

    EnsembliENSMUST00000042471; ENSMUSP00000041906; ENSMUSG00000033166.
    GeneIDi72662.
    KEGGimmu:72662.
    UCSCiuc007uuw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012840 mRNA. Translation: BAB28503.3 .
    AK032091 mRNA. Translation: BAC27692.1 .
    AK129259 Transcribed RNA. Translation: BAC98069.1 . Sequence problems.
    CCDSi CCDS49555.1.
    RefSeqi NP_082591.2. NM_028315.2.
    UniGenei Mm.163339.

    3D structure databases

    ProteinModelPortali Q9CSH3.
    SMRi Q9CSH3. Positions 10-911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215499. 1 interaction.
    IntActi Q9CSH3. 1 interaction.
    MINTi MINT-8178486.

    PTM databases

    PhosphoSitei Q9CSH3.

    Proteomic databases

    MaxQBi Q9CSH3.
    PaxDbi Q9CSH3.
    PRIDEi Q9CSH3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042471 ; ENSMUSP00000041906 ; ENSMUSG00000033166 .
    GeneIDi 72662.
    KEGGi mmu:72662.
    UCSCi uc007uuw.1. mouse.

    Organism-specific databases

    CTDi 22894.
    MGIi MGI:1919912. Dis3.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0557.
    GeneTreei ENSGT00530000063106.
    HOGENOMi HOG000191945.
    HOVERGENi HBG059397.
    InParanoidi Q9CSH3.
    KOi K12585.
    OMAi ENANDRN.
    OrthoDBi EOG7KH9J1.
    PhylomeDBi Q9CSH3.
    TreeFami TF105755.

    Enzyme and pathway databases

    Reactomei REACT_198696. KSRP destabilizes mRNA.

    Miscellaneous databases

    NextBioi 336687.
    PROi Q9CSH3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CSH3.
    CleanExi MM_DIS3.
    Genevestigatori Q9CSH3.

    Family and domain databases

    Gene3Di 3.40.50.1010. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR022966. RNase_II/R_CS.
    [Graphical view ]
    Pfami PF13638. PIN_4. 1 hit.
    [Graphical view ]
    SMARTi SM00670. PINc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 4 hits.
    SSF88723. SSF88723. 1 hit.
    PROSITEi PS01175. RIBONUCLEASE_II. 1 hit.
    [Graphical view ]
    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] OF 1-267 AND 272-958.
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-588.
      Tissue: Embryonic tail.

    Entry informationi

    Entry nameiRRP44_MOUSE
    AccessioniPrimary (citable) accession number: Q9CSH3
    Secondary accession number(s): Q6ZQ07, Q8C074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 90 of the entry and version 4 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