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Protein

Exosome complex exonuclease RRP44

Gene

DIS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications

Cofactori

Mg2+1 Publication, Mn2+1 Publication

GO - Molecular functioni

  • 3'-5'-exoribonuclease activity Source: UniProtKB
  • endonuclease activity Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • CUT catabolic process Source: UniProtKB
  • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  • gene expression Source: Reactome
  • mRNA catabolic process Source: GO_Central
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • positive regulation of GTPase activity Source: GOC
  • RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  • rRNA catabolic process Source: UniProtKB
  • rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

Magnesium, Manganese, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20604. DIS3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic exosome (RNase complex) Source: GO_Central
  • cytosol Source: Reactome
  • exosome (RNase complex) Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear exosome (RNase complex) Source: UniProtKB
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi146 – 1461D → N: Loss of endonuclease activity; when associated with N-487. 1 Publication
Mutagenesisi487 – 4871D → N: Loss of exonuclease activity. Loss of endonuclease activity; when associated with N-146. 1 Publication

Organism-specific databases

PharmGKBiPA162383628.

Polymorphism and mutation databases

BioMutaiDIS3.
DMDMi73620993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 958958Exosome complex exonuclease RRP44PRO_0000166419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei18 – 181N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y2L1.
PaxDbiQ9Y2L1.
PRIDEiQ9Y2L1.

2D gel databases

SWISS-2DPAGEQ9Y2L1.

PTM databases

PhosphoSiteiQ9Y2L1.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9Y2L1.
CleanExiHS_DIS3.
ExpressionAtlasiQ9Y2L1. baseline and differential.
GenevisibleiQ9Y2L1. HS.

Organism-specific databases

HPAiHPA039281.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC10Q017804EBI-373539,EBI-358236
EXOSC3Q9NQT53EBI-373539,EBI-371866

Protein-protein interaction databases

BioGridi116559. 31 interactions.
IntActiQ9Y2L1. 15 interactions.
MINTiMINT-3034163.
STRINGi9606.ENSP00000366997.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2L1.
SMRiQ9Y2L1. 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.
HOVERGENiHBG059397.
InParanoidiQ9Y2L1.
KOiK12585.
OMAiPWSITEK.
OrthoDBiEOG7KH9J1.
PhylomeDBiQ9Y2L1.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2L1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLKSKTFLKK TRAGGVMKIV REHYLRDDIG CGAPGCAACG GAHEGPALEP
60 70 80 90 100
QPQDPASSVC PQPHYLLPDT NVLLHQIDVL EDPAIRNVIV LQTVLQEVRN
110 120 130 140 150
RSAPVYKRIR DVTNNQEKHF YTFTNEHHRE TYVEQEQGEN ANDRNDRAIR
160 170 180 190 200
VAAKWYNEHL KKMSADNQLQ VIFITNDRRN KEKAIEEGIP AFTCEEYVKS
210 220 230 240 250
LTANPELIDR LACLSEEGNE IESGKIIFSE HLPLSKLQQG IKSGTYLQGT
260 270 280 290 300
FRASRENYLE ATVWIHGDNE ENKEIILQGL KHLNRAVHED IVAVELLPKS
310 320 330 340 350
QWVAPSSVVL HDEGQNEEDV EKEEETERML KTAVSEKMLK PTGRVVGIIK
360 370 380 390 400
RNWRPYCGML SKSDIKESRR HLFTPADKRI PRIRIETRQA STLEGRRIIV
410 420 430 440 450
AIDGWPRNSR YPNGHFVRNL GDVGEKETET EVLLLEHDVP HQPFSQAVLS
460 470 480 490 500
FLPKMPWSIT EKDMKNREDL RHLCICSVDP PGCTDIDDAL HCRELENGNL
510 520 530 540 550
EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV PELLSSNLCS
560 570 580 590 600
LKCDVDRLAF SCIWEMNHNA EILKTKFTKS VINSKASLTY AEAQLRIDSA
610 620 630 640 650
NMNDDITTSL RGLNKLAKIL KKRRIEKGAL TLSSPEVRFH MDSETHDPID
660 670 680 690 700
LQTKELRETN SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYE
710 720 730 740 750
ILVKAARSRN LEIKTDTAKS LAESLDQAES PTFPYLNTLL RILATRCMMQ
760 770 780 790 800
AVYFCSGMDN DFHHYGLASP IYTHFTSPIR RYADVIVHRL LAVAIGADCT
810 820 830 840 850
YPELTDKHKL ADICKNLNFR HKMAQYAQRA SVAFHTQLFF KSKGIVSEEA
860 870 880 890 900
YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PNPQLIYDDE IPSLKIEDTV
910 920 930 940 950
FHVFDKVKVK IMLDSSNLQH QKIRMSLVEP QIPGISIPTD TSNMDLNGPK

KKKMKLGK
Length:958
Mass (Da):109,003
Last modified:August 16, 2005 - v2
Checksum:i92336BA0D06247FE
GO
Isoform 2 (identifier: Q9Y2L1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-129: DVLEDPAIRNVIVLQTVLQEVRNRSAPVYKRIRDVTNNQEKHFYTFTNEHHR → VSAWRPGTWASVASSLRLPGSL

Show »
Length:928
Mass (Da):105,040
Checksum:iEDE527578627579A
GO

Sequence cautioni

The sequence BAA76852.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti635 – 6351P → S in CAH56266 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti269 – 2691N → S.3 Publications
Corresponds to variant rs4883918 [ dbSNP | Ensembl ].
VAR_023099
Natural varianti326 – 3261T → R.2 Publications
Corresponds to variant rs7332388 [ dbSNP | Ensembl ].
VAR_023100

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 12952DVLED…NEHHR → VSAWRPGTWASVASSLRLPG SL in isoform 2. 1 PublicationVSP_014971Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF330044 mRNA. Translation: AAL37479.1.
AB023225 mRNA. Translation: BAA76852.2. Different initiation.
AL832266 mRNA. Translation: CAH56266.1.
AK314715 mRNA. Translation: BAG37259.1.
AL080158 mRNA. Translation: CAB45749.1.
AL138695, AL391384 Genomic DNA. Translation: CAH72709.1.
AL138695, AL391384 Genomic DNA. Translation: CAH72708.1.
AL391384, AL138695 Genomic DNA. Translation: CAI15670.1.
AL391384, AL138695 Genomic DNA. Translation: CAI15671.1.
CH471093 Genomic DNA. Translation: EAW80517.1.
BC056143 mRNA. Translation: AAH56143.1.
CCDSiCCDS45057.1. [Q9Y2L1-2]
CCDS9447.1. [Q9Y2L1-1]
PIRiJE0110.
RefSeqiNP_001121698.1. NM_001128226.2. [Q9Y2L1-2]
NP_055768.3. NM_014953.4. [Q9Y2L1-1]
UniGeneiHs.744104.

Genome annotation databases

EnsembliENST00000377767; ENSP00000366997; ENSG00000083520.
ENST00000377780; ENSP00000367011; ENSG00000083520. [Q9Y2L1-2]
GeneIDi22894.
KEGGihsa:22894.
UCSCiuc001vix.4. human. [Q9Y2L1-1]
uc001viy.4. human. [Q9Y2L1-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF330044 mRNA. Translation: AAL37479.1.
AB023225 mRNA. Translation: BAA76852.2. Different initiation.
AL832266 mRNA. Translation: CAH56266.1.
AK314715 mRNA. Translation: BAG37259.1.
AL080158 mRNA. Translation: CAB45749.1.
AL138695, AL391384 Genomic DNA. Translation: CAH72709.1.
AL138695, AL391384 Genomic DNA. Translation: CAH72708.1.
AL391384, AL138695 Genomic DNA. Translation: CAI15670.1.
AL391384, AL138695 Genomic DNA. Translation: CAI15671.1.
CH471093 Genomic DNA. Translation: EAW80517.1.
BC056143 mRNA. Translation: AAH56143.1.
CCDSiCCDS45057.1. [Q9Y2L1-2]
CCDS9447.1. [Q9Y2L1-1]
PIRiJE0110.
RefSeqiNP_001121698.1. NM_001128226.2. [Q9Y2L1-2]
NP_055768.3. NM_014953.4. [Q9Y2L1-1]
UniGeneiHs.744104.

3D structure databases

ProteinModelPortaliQ9Y2L1.
SMRiQ9Y2L1. Positions 10-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116559. 31 interactions.
IntActiQ9Y2L1. 15 interactions.
MINTiMINT-3034163.
STRINGi9606.ENSP00000366997.

PTM databases

PhosphoSiteiQ9Y2L1.

Polymorphism and mutation databases

BioMutaiDIS3.
DMDMi73620993.

2D gel databases

SWISS-2DPAGEQ9Y2L1.

Proteomic databases

MaxQBiQ9Y2L1.
PaxDbiQ9Y2L1.
PRIDEiQ9Y2L1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377767; ENSP00000366997; ENSG00000083520.
ENST00000377780; ENSP00000367011; ENSG00000083520. [Q9Y2L1-2]
GeneIDi22894.
KEGGihsa:22894.
UCSCiuc001vix.4. human. [Q9Y2L1-1]
uc001viy.4. human. [Q9Y2L1-2]

Organism-specific databases

CTDi22894.
GeneCardsiGC13M073329.
H-InvDBHIX0011365.
HGNCiHGNC:20604. DIS3.
HPAiHPA039281.
MIMi607533. gene.
neXtProtiNX_Q9Y2L1.
PharmGKBiPA162383628.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0557.
GeneTreeiENSGT00530000063106.
HOVERGENiHBG059397.
InParanoidiQ9Y2L1.
KOiK12585.
OMAiPWSITEK.
OrthoDBiEOG7KH9J1.
PhylomeDBiQ9Y2L1.
TreeFamiTF105755.

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_20619. mRNA decay by 3' to 5' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSiDIS3. human.
GeneWikiiDIS3.
GenomeRNAii22894.
NextBioi43511.
PROiQ9Y2L1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2L1.
CleanExiHS_DIS3.
ExpressionAtlasiQ9Y2L1. baseline and differential.
GenevisibleiQ9Y2L1. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3."
    Shiomi T., Fukushima K., Suzuki N., Nakashima N., Noguchi E., Nishimoto T.
    J. Biochem. 123:883-890(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  2. Erratum
    Shiomi T., Fukushima K., Suzuki N., Nakashima N., Noguchi E., Nishimoto T.
    J. Biochem. 124:250-250(1998)
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-269.
    Tissue: Brain and Peripheral blood leukocyte.
  4. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ARG-326.
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-269.
    Tissue: Trachea.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-269.
    Tissue: Lymph node and Testis.
  8. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 1), VARIANT ARG-326.
    Tissue: Lymph.
  11. "RNA exosome depletion reveals transcription upstream of active human promoters."
    Preker P., Nielsen J., Kammler S., Lykke-Andersen S., Christensen M.S., Mapendano C.K., Schierup M.H., Jensen T.H.
    Science 322:1851-1854(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROMPT DEGRADATION.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-146 AND ASP-487.
  15. "Dis3-like 1: a novel exoribonuclease associated with the human exosome."
    Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., Heck A.J., Raijmakers R., Pruijn G.J.
    EMBO J. 29:2358-2367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH EXOSC3.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRRP44_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2L1
Secondary accession number(s): A6NI21
, B2RBL2, Q5W0P7, Q5W0P8, Q658Z7, Q7Z481, Q8WWI2, Q9UG36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 16, 2005
Last modified: July 22, 2015
This is version 158 of the entry and version 2 of the sequence. [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

Miscellaneous

The association of DIS3 with the RNA exosome complex appears to be weak explaining its absence in some complex purifications.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.