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Q9Y2L1 (RRP44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DIS3
Synonyms:KIAA1008, RRP44
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length958 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.14

Cofactor

Magnesium or manganese. Ref.14

Subunit structure

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.

Subcellular location

Cytoplasm. Nucleusnucleolus. Nucleusnucleoplasm. Nucleus. Note: Predominantly located in the nucleus. According to Ref.12, found in the nucleolus and according to Ref.14, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of DIS3. Ref.12 Ref.14 Ref.15

Tissue specificity

Widely expressed.

Miscellaneous

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

Sequence similarities

Belongs to the RNR ribonuclease family.

Contains 1 PINc domain.

Sequence caution

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

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Manganese
RNA-binding
   Molecular functionEndonuclease
Exonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCUT catabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from mutant phenotype Ref.14. Source: GOC

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Inferred from mutant phenotype Ref.14. Source: GOC

rRNA catabolic process

Inferred from mutant phenotype PubMed 20368444. Source: UniProtKB

rRNA processing

Traceable author statement Ref.1. Source: UniProtKB

regulation of GTPase activity

Inferred from direct assay Ref.1. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

exosome (RNase complex)

Traceable author statement Ref.1. Source: UniProtKB

nuclear exosome (RNase complex)

Inferred from direct assay Ref.14. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_function3'-5'-exoribonuclease activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

endonuclease activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

guanyl-nucleotide exchange factor activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15231747Ref.14Ref.15PubMed 21255825PubMed 23756462. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EXOSC10Q017804EBI-373539,EBI-358236
EXOSC3Q9NQT53EBI-373539,EBI-371866

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2L1-1)

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.
Isoform 2 (identifier: Q9Y2L1-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 958958Exosome complex exonuclease RRP44
PRO_0000166419

Regions

Domain64 – 182119PINc

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17
Modified residue181N6-acetyllysine Ref.13

Natural variations

Alternative sequence78 – 12952DVLED…NEHHR → VSAWRPGTWASVASSLRLPG SL in isoform 2.
VSP_014971
Natural variant2691N → S. Ref.3 Ref.6 Ref.7
Corresponds to variant rs4883918 [ dbSNP | Ensembl ].
VAR_023099
Natural variant3261T → R. Ref.4 Ref.10
Corresponds to variant rs7332388 [ dbSNP | Ensembl ].
VAR_023100

Experimental info

Mutagenesis1461D → N: Loss of endonuclease activity; when associated with N-487. Ref.14
Mutagenesis4871D → N: Loss of exonuclease activity. Loss of endonuclease activity; when associated with N-146. Ref.14
Sequence conflict6351P → S in CAH56266. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 92336BA0D06247FE

FASTA958109,003
        10         20         30         40         50         60 
MLKSKTFLKK TRAGGVMKIV REHYLRDDIG CGAPGCAACG GAHEGPALEP QPQDPASSVC 

        70         80         90        100        110        120 
PQPHYLLPDT NVLLHQIDVL EDPAIRNVIV LQTVLQEVRN RSAPVYKRIR DVTNNQEKHF 

       130        140        150        160        170        180 
YTFTNEHHRE TYVEQEQGEN ANDRNDRAIR VAAKWYNEHL KKMSADNQLQ VIFITNDRRN 

       190        200        210        220        230        240 
KEKAIEEGIP AFTCEEYVKS LTANPELIDR LACLSEEGNE IESGKIIFSE HLPLSKLQQG 

       250        260        270        280        290        300 
IKSGTYLQGT FRASRENYLE ATVWIHGDNE ENKEIILQGL KHLNRAVHED IVAVELLPKS 

       310        320        330        340        350        360 
QWVAPSSVVL HDEGQNEEDV EKEEETERML KTAVSEKMLK PTGRVVGIIK RNWRPYCGML 

       370        380        390        400        410        420 
SKSDIKESRR HLFTPADKRI PRIRIETRQA STLEGRRIIV AIDGWPRNSR YPNGHFVRNL 

       430        440        450        460        470        480 
GDVGEKETET EVLLLEHDVP HQPFSQAVLS FLPKMPWSIT EKDMKNREDL RHLCICSVDP 

       490        500        510        520        530        540 
PGCTDIDDAL HCRELENGNL EVGVHIADVS HFIRPGNALD QESARRGTTV YLCEKRIDMV 

       550        560        570        580        590        600 
PELLSSNLCS LKCDVDRLAF SCIWEMNHNA EILKTKFTKS VINSKASLTY AEAQLRIDSA 

       610        620        630        640        650        660 
NMNDDITTSL RGLNKLAKIL KKRRIEKGAL TLSSPEVRFH MDSETHDPID LQTKELRETN 

       670        680        690        700        710        720 
SMVEEFMLLA NISVAKKIHE EFSEHALLRK HPAPPPSNYE ILVKAARSRN LEIKTDTAKS 

       730        740        750        760        770        780 
LAESLDQAES PTFPYLNTLL RILATRCMMQ AVYFCSGMDN DFHHYGLASP IYTHFTSPIR 

       790        800        810        820        830        840 
RYADVIVHRL LAVAIGADCT YPELTDKHKL ADICKNLNFR HKMAQYAQRA SVAFHTQLFF 

       850        860        870        880        890        900 
KSKGIVSEEA YILFVRKNAI VVLIPKYGLE GTVFFEEKDK PNPQLIYDDE IPSLKIEDTV 

       910        920        930        940        950 
FHVFDKVKVK IMLDSSNLQH QKIRMSLVEP QIPGISIPTD TSNMDLNGPK KKKMKLGK 

« Hide

Isoform 2 [UniParc].

Checksum: EDE527578627579A
Show »

FASTA928105,040

References

« Hide 'large scale' references
[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]"A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer development: identification and characterization of candidate genes."
Rozenblum E., Vahteristo P., Sandberg T., Bergthorsson J.T., Syrjakoski K., Weaver D., Haraldsson K., Johannsdottir H.K., Vehmanen P., Nigam S., Golberger N., Robbins C., Pak E., Dutra A., Gillander E., Stephan D.A., Bailey-Wilson J., Juo S.-H.H. expand/collapse author list , Kainu T., Arason A., Barkardottir R.B., Nevanlinna H., Borg A., Kallioniemi O.-P.
Hum. Genet. 110:111-121(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L."
Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A., Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S., Stepien P.P., Dziembowski A., Jensen T.H.
EMBO J. 29:2342-2357(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45057.1. [Q9Y2L1-2]
CCDS9447.1. [Q9Y2L1-1]
PIRJE0110.
RefSeqNP_001121698.1. NM_001128226.2. [Q9Y2L1-2]
NP_055768.3. NM_014953.4. [Q9Y2L1-1]
UniGeneHs.744104.

3D structure databases

ProteinModelPortalQ9Y2L1.
SMRQ9Y2L1. Positions 10-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116559. 25 interactions.
IntActQ9Y2L1. 14 interactions.
MINTMINT-3034163.

PTM databases

PhosphoSiteQ9Y2L1.

Polymorphism databases

DMDM73620993.

2D gel databases

SWISS-2DPAGEQ9Y2L1.

Proteomic databases

MaxQBQ9Y2L1.
PaxDbQ9Y2L1.
PRIDEQ9Y2L1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377767; ENSP00000366997; ENSG00000083520. [Q9Y2L1-1]
ENST00000377780; ENSP00000367011; ENSG00000083520. [Q9Y2L1-2]
GeneID22894.
KEGGhsa:22894.
UCSCuc001vix.4. human. [Q9Y2L1-1]
uc001viy.4. human. [Q9Y2L1-2]

Organism-specific databases

CTD22894.
GeneCardsGC13M073329.
H-InvDBHIX0011365.
HGNCHGNC:20604. DIS3.
HPAHPA039281.
MIM607533. gene.
neXtProtNX_Q9Y2L1.
PharmGKBPA162383628.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0557.
HOVERGENHBG059397.
InParanoidQ9Y2L1.
KOK12585.
OMAENANDRN.
OrthoDBEOG7KH9J1.
PhylomeDBQ9Y2L1.
TreeFamTF105755.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y2L1.
BgeeQ9Y2L1.
CleanExHS_DIS3.
GenevestigatorQ9Y2L1.

Family and domain databases

Gene3D3.40.50.1010. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR002716. PIN_dom.
IPR029060. PIN_domain-like.
IPR022966. RNase_II/R_CS.
[Graphical view]
PfamPF13638. PIN_4. 1 hit.
[Graphical view]
SMARTSM00670. PINc. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 4 hits.
SSF88723. SSF88723. 1 hit.
PROSITEPS01175. RIBONUCLEASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDIS3. human.
GeneWikiDIS3.
GenomeRNAi22894.
NextBio43511.
PROQ9Y2L1.
SOURCESearch...

Entry information

Entry nameRRP44_HUMAN
AccessionPrimary (citable) accession number: Q9Y2L1
Secondary accession number(s): A6NI21 expand/collapse secondary AC list , B2RBL2, Q5W0P7, Q5W0P8, Q658Z7, Q7Z481, Q8WWI2, Q9UG36
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM