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Q9NQT5 (EXOS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 component RRP40
Alternative name(s):
Exosome component 3
Ribosomal RNA-processing protein 40
p10
Gene names
Name:EXOSC3
Synonyms:RRP40
ORF Names:CGI-102
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-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. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5. Ref.10 Ref.11 Ref.13 Ref.17

Subunit structure

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with GTPBP1. Interacts with ZC3HAV1. Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner. Ref.9 Ref.12 Ref.15 Ref.18 Ref.19

Subcellular location

Cytoplasm. Nucleusnucleolus. Nucleus Ref.6 Ref.11 Ref.15.

Involvement in disease

Pontocerebellar hypoplasia 1B (PCH1B) [MIM:614678]: A severe autosomal recessive neurologic disorder characterized by a combination of cerebellar and spinal motor neuron degeneration beginning at birth. There is diffuse muscle weakness, progressive microcephaly, global developmental delay, and brainstem involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Sequence similarities

Belongs to the RRP40 family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandRNA-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCUT catabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

DNA deamination

Inferred from direct assay Ref.17. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, exonucleolytic

Non-traceable author statement Ref.1. Source: GOC

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

Inferred from mutant phenotype Ref.10. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

isotype switching

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

positive regulation of isotype switching

Inferred from electronic annotation. Source: Ensembl

rRNA processing

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasmic exosome (RNase complex)

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exosome (RNase complex)

Inferred from direct assay Ref.15. Source: UniProtKB

nuclear exosome (RNase complex)

Inferred from direct assay Ref.1. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

transcriptionally active chromatin

Inferred from mutant phenotype PubMed 20699273. Source: UniProtKB

   Molecular_function3'-5'-exoribonuclease activity

Non-traceable author statement Ref.1. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.19. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQT5-1)

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: Q9NQT5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     159-275: VGDLIYGQFV...KQIFSRLAES → AISSRL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 275274Exosome complex component RRP40
PRO_0000087131

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.14 Ref.20 Ref.21

Natural variations

Alternative sequence159 – 275117VGDLI…RLAES → AISSRL in isoform 2.
VSP_043457
Natural variant311G → A in PCH1B. Ref.24
VAR_068505
Natural variant1321D → A in PCH1B. Ref.24
Corresponds to variant rs141138948 [ dbSNP | Ensembl ].
VAR_068506
Natural variant1391A → P in PCH1B. Ref.24
VAR_068507
Natural variant2251Y → H.
Corresponds to variant rs3208406 [ dbSNP | Ensembl ].
VAR_054098
Natural variant2381W → R in PCH1B. Ref.24
VAR_068508

Experimental info

Sequence conflict56 – 6510NARACSRVRV → MLERARGCAF in AAD34097. Ref.7
Sequence conflict951S → G in AAD34097. Ref.7

Secondary structure

................................................... 275
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 264322144A199166

FASTA27529,572
        10         20         30         40         50         60 
MAEPASVAAE SLAGSRARAA RTVLGQVVLP GEELLLPEQE DAEGPGGAVE RPLSLNARAC 

        70         80         90        100        110        120 
SRVRVVCGPG LRRCGDRLLV TKCGRLRHKE PGSGSGGGVY WVDSQQKRYV PVKGDHVIGI 

       130        140        150        160        170        180 
VTAKSGDIFK VDVGGSEPAS LSYLSFEGAT KRNRPNVQVG DLIYGQFVVA NKDMEPEMVC 

       190        200        210        220        230        240 
IDSCGRANGM GVIGQDGLLF KVTLGLIRKL LAPDCEIIQE VGKLYPLEIV FGMNGRIWVK 

       250        260        270 
AKTIQQTLIL ANILEACEHM TSDQRKQIFS RLAES 

« Hide

Isoform 2 [UniParc].

Checksum: 51C07B44337D0076
Show »

FASTA16417,248

References

« Hide 'large scale' references
[1]"Three novel components of the human exosome."
Brouwer R., Allmang C., Raijmakers R., van Aarssen Y., Egberts W.V., Petfalski E., van Venrooij W.J., Tollervey D., Pruijn G.J.M.
J. Biol. Chem. 276:6177-6184(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]"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] (ISOFORMS 1 AND 2).
Tissue: Cerebellum.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
Tissue: Skin and Uterus.
[6]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-16 AND 202-208, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-275 (ISOFORM 1).
[8]"The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"AU binding proteins recruit the exosome to degrade ARE-containing mRNAs."
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R., Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.
Cell 107:451-464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
[10]"The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements."
Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., Lutz C.S., Wilusz J.
EMBO J. 21:165-174(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOPLASMIC MRNA DEGRADATION.
[11]"Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways."
van Dijk E.L., Schilders G., Pruijn G.J.
RNA 13:1027-1035(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
[12]"p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein."
Chen G., Guo X., Lv F., Xu Y., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX17.
[13]"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.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH DIS3L.
[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]"The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates."
Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J., Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K., Gregory R.I., Deng H., Lima C.D., Alt F.W.
Cell 144:353-363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE.
[18]"Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTPBP1.
[19]"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3HAV1.
[20]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Reconstitution, activities, and structure of the eukaryotic RNA exosome."
Liu Q., Greimann J.C., Lima C.D.
Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
[23]Erratum
Liu Q., Greimann J.C., Lima C.D.
Cell 131:188-189(2007)
[24]"Mutations in the RNA exosome component gene EXOSC3 cause pontocerebellar hypoplasia and spinal motor neuron degeneration."
Wan J., Yourshaw M., Mamsa H., Rudnik-Schoneborn S., Menezes M.P., Hong J.E., Leong D.W., Senderek J., Salman M.S., Chitayat D., Seeman P., von Moers A., Graul-Neumann L., Kornberg A.J., Castro-Gago M., Sobrido M.J., Sanefuji M., Shieh P.B. expand/collapse author list , Salamon N., Kim R.C., Vinters H.V., Chen Z., Zerres K., Ryan M.M., Nelson S.F., Jen J.C.
Nat. Genet. 44:704-708(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCH1B ALA-31; ALA-132; PRO-139 AND ARG-238.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF281132 mRNA. Translation: AAF82133.1.
AK289571 mRNA. Translation: BAF82260.1.
AK290864 mRNA. Translation: BAF83553.1.
AL138752 Genomic DNA. Translation: CAI13880.1.
CH471071 Genomic DNA. Translation: EAW58264.1.
BC002437 mRNA. Translation: AAH02437.1.
BC008880 mRNA. Translation: AAH08880.1.
AF151860 mRNA. Translation: AAD34097.1.
CCDSCCDS35016.1. [Q9NQT5-1]
CCDS43805.1. [Q9NQT5-2]
RefSeqNP_001002269.1. NM_001002269.2. [Q9NQT5-2]
NP_057126.2. NM_016042.3. [Q9NQT5-1]
UniGeneHs.602571.
Hs.713483.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35G1-275[»]
ProteinModelPortalQ9NQT5.
SMRQ9NQT5. Positions 17-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119217. 19 interactions.
DIPDIP-29847N.
IntActQ9NQT5. 19 interactions.
MINTMINT-3072286.
STRING9606.ENSP00000323046.

PTM databases

PhosphoSiteQ9NQT5.

Polymorphism databases

DMDM14285758.

Proteomic databases

MaxQBQ9NQT5.
PaxDbQ9NQT5.
PeptideAtlasQ9NQT5.
PRIDEQ9NQT5.

Protocols and materials databases

DNASU51010.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327304; ENSP00000323046; ENSG00000107371. [Q9NQT5-1]
ENST00000396521; ENSP00000379775; ENSG00000107371. [Q9NQT5-2]
ENST00000465229; ENSP00000418422; ENSG00000107371. [Q9NQT5-2]
GeneID51010.
KEGGhsa:51010.
UCSCuc004aal.3. human. [Q9NQT5-1]
uc004aam.3. human. [Q9NQT5-2]

Organism-specific databases

CTD51010.
GeneCardsGC09M037772.
HGNCHGNC:17944. EXOSC3.
HPAHPA020485.
MIM606489. gene.
614678. phenotype.
neXtProtNX_Q9NQT5.
Orphanet2254. Pontocerebellar hypoplasia type 1.
PharmGKBPA134926550.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1097.
HOGENOMHOG000184644.
HOVERGENHBG051518.
InParanoidQ9NQT5.
KOK03681.
OMAVNGRVWI.
OrthoDBEOG76HQ2F.
PhylomeDBQ9NQT5.
TreeFamTF314927.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NQT5.
BgeeQ9NQT5.
CleanExHS_EXOSC3.
GenevestigatorQ9NQT5.

Family and domain databases

InterProIPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PANTHERPTHR21321. PTHR21321. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEXOSC3. human.
EvolutionaryTraceQ9NQT5.
GeneWikiExosome_component_3.
GenomeRNAi51010.
NextBio53494.
PROQ9NQT5.
SOURCESearch...

Entry information

Entry nameEXOS3_HUMAN
AccessionPrimary (citable) accession number: Q9NQT5
Secondary accession number(s): A8K0K6, Q5QP85, Q9Y3A8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 135 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 9

Human chromosome 9: entries, gene names and cross-references to MIM