Q9Y2L1 (RRP44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DIS3
Synonyms:	KIAA1008, RRP44

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	958 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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. Nucleus › nucleolus. Nucleus › nucleoplasm. 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 process	rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Magnesium Manganese RNA-binding
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CUT catabolic process Inferred from mutant phenotype Ref.11. Source: UniProtKB exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Traceable author statement. Source: Reactome rRNA catabolic process Inferred from mutant phenotype PubMed 20368444. Source: UniProtKB rRNA processing Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear exosome (RNase complex) Inferred from direct assay Ref.14. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	3'-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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOSC3	Q9NQT5	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 958	958	Exosome complex exonuclease RRP44		PRO_0000166419
Regions
	Domain	64 – 182	119	PINc
Amino acid modifications
	Modified residue	18	1	N6-acetyllysine Ref.13
Natural variations
	Alternative sequence	78 – 129	52	DVLED…NEHHR → VSAWRPGTWASVASSLRLPG SL in isoform 2.		VSP_014971
	Natural variant	269	1	N → S. Ref.3 Ref.6 Ref.7 Corresponds to variant rs4883918 [ dbSNP | Ensembl ].		VAR_023099
	Natural variant	326	1	T → R. Ref.4 Ref.10 Corresponds to variant rs7332388 [ dbSNP | Ensembl ].		VAR_023100
Experimental info
	Mutagenesis	146	1	D → N: Loss of endonuclease activity; when associated with N-487. Ref.14
	Mutagenesis	487	1	D → N: Loss of exonuclease activity. Loss of endonuclease activity; when associated with N-146. Ref.14
	Sequence conflict	635	1	P → S in CAH56266. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 92336BA0D06247FE	FASTA	958	109,003
	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
	Isoform 2 [UniParc]. Checksum: EDE527578627579A	FASTA	928	105,040
	10 20 30 40 50 60 MLKSKTFLKK TRAGGVMKIV REHYLRDDIG CGAPGCAACG GAHEGPALEP QPQDPASSVC 70 80 90 100 110 120 PQPHYLLPDT NVLLHQIVSA WRPGTWASVA SSLRLPGSLE TYVEQEQGEN ANDRNDRAIR 130 140 150 160 170 180 VAAKWYNEHL KKMSADNQLQ VIFITNDRRN KEKAIEEGIP AFTCEEYVKS LTANPELIDR 190 200 210 220 230 240 LACLSEEGNE IESGKIIFSE HLPLSKLQQG IKSGTYLQGT FRASRENYLE ATVWIHGDNE 250 260 270 280 290 300 ENKEIILQGL KHLNRAVHED IVAVELLPKS QWVAPSSVVL HDEGQNEEDV EKEEETERML 310 320 330 340 350 360 KTAVSEKMLK PTGRVVGIIK RNWRPYCGML SKSDIKESRR HLFTPADKRI PRIRIETRQA 370 380 390 400 410 420 STLEGRRIIV AIDGWPRNSR YPNGHFVRNL GDVGEKETET EVLLLEHDVP HQPFSQAVLS 430 440 450 460 470 480 FLPKMPWSIT EKDMKNREDL RHLCICSVDP PGCTDIDDAL HCRELENGNL EVGVHIADVS 490 500 510 520 530 540 HFIRPGNALD QESARRGTTV YLCEKRIDMV PELLSSNLCS LKCDVDRLAF SCIWEMNHNA 550 560 570 580 590 600 EILKTKFTKS VINSKASLTY AEAQLRIDSA NMNDDITTSL RGLNKLAKIL KKRRIEKGAL 610 620 630 640 650 660 TLSSPEVRFH MDSETHDPID LQTKELRETN SMVEEFMLLA NISVAKKIHE EFSEHALLRK 670 680 690 700 710 720 HPAPPPSNYE ILVKAARSRN LEIKTDTAKS LAESLDQAES PTFPYLNTLL RILATRCMMQ 730 740 750 760 770 780 AVYFCSGMDN DFHHYGLASP IYTHFTSPIR RYADVIVHRL LAVAIGADCT YPELTDKHKL 790 800 810 820 830 840 ADICKNLNFR HKMAQYAQRA SVAFHTQLFF KSKGIVSEEA YILFVRKNAI VVLIPKYGLE 850 860 870 880 890 900 GTVFFEEKDK PNPQLIYDDE IPSLKIEDTV FHVFDKVKVK IMLDSSNLQH QKIRMSLVEP 910 920 QIPGISIPTD TSNMDLNGPK KKKMKLGK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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: IDENTIFICATION BY MASS SPECTROMETRY, 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, MASS SPECTROMETRY.
[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, 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, 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].
+	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.
IPI	IPI00183462. IPI00746351.
PIR	JE0110.
RefSeq	NP_001121698.1. NM_001128226.1. NP_055768.3. NM_014953.3.
UniGene	Hs.740506.
3D structure databases
ProteinModelPortal	Q9Y2L1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y2L1. 8 interactions.
PTM databases
PhosphoSite	Q9Y2L1.
Polymorphism databases
DMDM	73620993.
2D gel databases
SWISS-2DPAGE	Q9Y2L1.
Proteomic databases
PaxDb	Q9Y2L1.
PRIDE	Q9Y2L1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377767; ENSP00000366997; ENSG00000083520. ENST00000377780; ENSP00000367011; ENSG00000083520.
GeneID	22894.
KEGG	hsa:22894.
UCSC	uc001vix.4. human. uc001viy.4. human.
Organism-specific databases
CTD	22894.
GeneCards	GC13M073329.
H-InvDB	HIX0011365.
HGNC	HGNC:20604. DIS3.
HPA	HPA039281.
MIM	607533. gene.
neXtProt	NX_Q9Y2L1.
PharmGKB	PA162383628.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0557.
HOVERGEN	HBG059397.
InParanoid	Q9Y2L1.
KO	K12585.
OMA	MPWSITE.
OrthoDB	EOG45B1DT.
PhylomeDB	Q9Y2L1.
Enzyme and pathway databases
Reactome	REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9Y2L1.
Bgee	Q9Y2L1.
CleanEx	HS_DIS3.
Genevestigator	Q9Y2L1.
GermOnline	ENSG00000083520. Homo sapiens.
Family and domain databases
InterPro	IPR002716. PIN_dom. IPR006596. PINc_nuc-bd. IPR001900. RNase_II/R. IPR022966. RNase_II/R_CS. [Graphical view]
Pfam	PF13638. PIN_4. 1 hit. PF00773. RNB. 1 hit. [Graphical view]
SMART	SM00670. PINc. 1 hit. SM00955. RNB. 1 hit. [Graphical view]
PROSITE	PS01175. RIBONUCLEASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DIS3. human.
GenomeRNAi	22894.
NextBio	43511.
SOURCE	Search...

Entry information

Entry name

RRP44_HUMAN

Accession

Primary (citable) accession number: Q9Y2L1
Secondary accession number(s): A6NI21 , 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:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.