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Q9Y2L1

- RRP44_HUMAN

UniProt

Q9Y2L1 - RRP44_HUMAN

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Protein

Exosome complex exonuclease RRP44

Gene

DIS3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

GO - Biological processi

  1. CUT catabolic process Source: UniProtKB
  2. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  6. nucleic acid phosphodiester bond hydrolysis Source: GOC
  7. positive regulation of GTPase activity Source: GOC
  8. RNA metabolic process Source: Reactome
  9. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  10. rRNA catabolic process Source: UniProtKB
  11. 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: Chromosome 13

Organism-specific databases

HGNCiHGNC:20604. DIS3.

Subcellular locationi

Cytoplasm. Nucleusnucleolus. Nucleusnucleoplasm. Nucleus
Note: Predominantly located in the nucleus. According to PubMed:12429849, found in the nucleolus and according to PubMed:20531386, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of DIS3.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. exosome (RNase complex) Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nuclear exosome (RNase complex) Source: UniProtKB
  6. nucleoplasm Source: UniProtKB
  7. nucleus Source: HPA
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.

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.
GenevestigatoriQ9Y2L1.

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.

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.
OMAiENANDRN.
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. Align

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

Polymorphism databases

DMDMi73620993.

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 .
CCDSi CCDS45057.1. [Q9Y2L1-2 ]
CCDS9447.1. [Q9Y2L1-1 ]
PIRi JE0110.
RefSeqi NP_001121698.1. NM_001128226.2. [Q9Y2L1-2 ]
NP_055768.3. NM_014953.4. [Q9Y2L1-1 ]
UniGenei Hs.744104.

3D structure databases

ProteinModelPortali Q9Y2L1.
SMRi Q9Y2L1. Positions 10-911.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116559. 31 interactions.
IntActi Q9Y2L1. 15 interactions.
MINTi MINT-3034163.

PTM databases

PhosphoSitei Q9Y2L1.

Polymorphism databases

DMDMi 73620993.

2D gel databases

SWISS-2DPAGE Q9Y2L1.

Proteomic databases

MaxQBi Q9Y2L1.
PaxDbi Q9Y2L1.
PRIDEi Q9Y2L1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377767 ; ENSP00000366997 ; ENSG00000083520 . [Q9Y2L1-1 ]
ENST00000377780 ; ENSP00000367011 ; ENSG00000083520 . [Q9Y2L1-2 ]
GeneIDi 22894.
KEGGi hsa:22894.
UCSCi uc001vix.4. human. [Q9Y2L1-1 ]
uc001viy.4. human. [Q9Y2L1-2 ]

Organism-specific databases

CTDi 22894.
GeneCardsi GC13M073329.
H-InvDB HIX0011365.
HGNCi HGNC:20604. DIS3.
HPAi HPA039281.
MIMi 607533. gene.
neXtProti NX_Q9Y2L1.
PharmGKBi PA162383628.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0557.
GeneTreei ENSGT00530000063106.
HOVERGENi HBG059397.
InParanoidi Q9Y2L1.
KOi K12585.
OMAi ENANDRN.
OrthoDBi EOG7KH9J1.
PhylomeDBi Q9Y2L1.
TreeFami TF105755.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi DIS3. human.
GeneWikii DIS3.
GenomeRNAii 22894.
NextBioi 43511.
PROi Q9Y2L1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2L1.
CleanExi HS_DIS3.
ExpressionAtlasi Q9Y2L1. baseline and differential.
Genevestigatori Q9Y2L1.

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

« 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: November 26, 2014
This is version 150 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