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Q9NQT5

- EXOS3_HUMAN

UniProt

Q9NQT5 - EXOS3_HUMAN

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Protein
Exosome complex component RRP40
Gene
EXOSC3, RRP40, CGI-102
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 EXOSC5.4 Publications

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: UniProtKB
  2. RNA binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. CUT catabolic process Source: UniProtKB
  2. DNA deamination Source: UniProtKB
  3. RNA metabolic process Source: Reactome
  4. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  5. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
  6. gene expression Source: Reactome
  7. isotype switching Source: UniProtKB
  8. mRNA metabolic process Source: Reactome
  9. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  10. positive regulation of isotype switching Source: Ensembl
  11. rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

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 component RRP40
Alternative name(s):
Exosome component 3
Ribosomal RNA-processing protein 40
p10
Gene namesi
Name:EXOSC3
Synonyms:RRP40
ORF Names:CGI-102
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17944. EXOSC3.

Subcellular locationi

Cytoplasm. Nucleusnucleolus. Nucleus 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic exosome (RNase complex) Source: UniProtKB
  3. cytosol Source: Reactome
  4. exosome (RNase complex) Source: UniProtKB
  5. nuclear exosome (RNase complex) Source: UniProtKB
  6. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311G → A in PCH1B. 1 Publication
VAR_068505
Natural varianti132 – 1321D → A in PCH1B. 1 Publication
Corresponds to variant rs141138948 [ dbSNP | Ensembl ].
VAR_068506
Natural varianti139 – 1391A → P in PCH1B. 1 Publication
VAR_068507
Natural varianti238 – 2381W → R in PCH1B. 1 Publication
VAR_068508

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614678. phenotype.
Orphaneti2254. Pontocerebellar hypoplasia type 1.
PharmGKBiPA134926550.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 275274Exosome complex component RRP40
PRO_0000087131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NQT5.
PaxDbiQ9NQT5.
PeptideAtlasiQ9NQT5.
PRIDEiQ9NQT5.

PTM databases

PhosphoSiteiQ9NQT5.

Expressioni

Gene expression databases

ArrayExpressiQ9NQT5.
BgeeiQ9NQT5.
CleanExiHS_EXOSC3.
GenevestigatoriQ9NQT5.

Organism-specific databases

HPAiHPA020485.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DIS3Q9Y2L13EBI-371866,EBI-373539
DIS3LQ8TF463EBI-371866,EBI-3672244
EXOSC2Q138685EBI-371866,EBI-301735
EXOSC4Q9NPD34EBI-371866,EBI-371823
EXOSC5Q9NQT47EBI-371866,EBI-371876
EXOSC8Q96B263EBI-371866,EBI-371922

Protein-protein interaction databases

BioGridi119217. 19 interactions.
DIPiDIP-29847N.
IntActiQ9NQT5. 19 interactions.
MINTiMINT-3072286.
STRINGi9606.ENSP00000323046.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 243
Beta strandi25 – 273
Beta strandi30 – 345
Beta strandi45 – 495
Beta strandi78 – 803
Beta strandi85 – 895
Turni92 – 943
Beta strandi99 – 1035
Beta strandi113 – 12513
Beta strandi128 – 1325
Beta strandi134 – 1374
Beta strandi141 – 1433
Beta strandi145 – 1473
Beta strandi153 – 1575
Beta strandi162 – 1698
Beta strandi177 – 1793
Turni183 – 1853
Beta strandi198 – 2003
Helixi204 – 2118
Helixi217 – 2204
Beta strandi224 – 2263
Beta strandi230 – 2323
Turni233 – 2353
Beta strandi236 – 2394
Helixi244 – 25613
Turni262 – 2643
Helixi265 – 27410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35G1-275[»]
ProteinModelPortaliQ9NQT5.
SMRiQ9NQT5. Positions 17-275.

Miscellaneous databases

EvolutionaryTraceiQ9NQT5.

Family & Domainsi

Sequence similaritiesi

Belongs to the RRP40 family.

Phylogenomic databases

eggNOGiCOG1097.
HOGENOMiHOG000184644.
HOVERGENiHBG051518.
InParanoidiQ9NQT5.
KOiK03681.
OMAiVNGRVWI.
OrthoDBiEOG76HQ2F.
PhylomeDBiQ9NQT5.
TreeFamiTF314927.

Family and domain databases

InterProiIPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PANTHERiPTHR21321. PTHR21321. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NQT5-1) [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

MAEPASVAAE SLAGSRARAA RTVLGQVVLP GEELLLPEQE DAEGPGGAVE    50
RPLSLNARAC SRVRVVCGPG LRRCGDRLLV TKCGRLRHKE PGSGSGGGVY 100
WVDSQQKRYV PVKGDHVIGI VTAKSGDIFK VDVGGSEPAS LSYLSFEGAT 150
KRNRPNVQVG DLIYGQFVVA NKDMEPEMVC IDSCGRANGM GVIGQDGLLF 200
KVTLGLIRKL LAPDCEIIQE VGKLYPLEIV FGMNGRIWVK AKTIQQTLIL 250
ANILEACEHM TSDQRKQIFS RLAES 275
Length:275
Mass (Da):29,572
Last modified:January 23, 2007 - v3
Checksum:i264322144A199166
GO
Isoform 2 (identifier: Q9NQT5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-275: VGDLIYGQFV...KQIFSRLAES → AISSRL

Note: No experimental confirmation available.

Show »
Length:164
Mass (Da):17,248
Checksum:i51C07B44337D0076
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311G → A in PCH1B. 1 Publication
VAR_068505
Natural varianti132 – 1321D → A in PCH1B. 1 Publication
Corresponds to variant rs141138948 [ dbSNP | Ensembl ].
VAR_068506
Natural varianti139 – 1391A → P in PCH1B. 1 Publication
VAR_068507
Natural varianti225 – 2251Y → H.
Corresponds to variant rs3208406 [ dbSNP | Ensembl ].
VAR_054098
Natural varianti238 – 2381W → R in PCH1B. 1 Publication
VAR_068508

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 275117VGDLI…RLAES → AISSRL in isoform 2.
VSP_043457Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 6510NARACSRVRV → MLERARGCAF in AAD34097. 1 Publication
Sequence conflicti95 – 951S → G in AAD34097. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35016.1. [Q9NQT5-1]
CCDS43805.1. [Q9NQT5-2]
RefSeqiNP_001002269.1. NM_001002269.2. [Q9NQT5-2]
NP_057126.2. NM_016042.3. [Q9NQT5-1]
UniGeneiHs.602571.
Hs.713483.

Genome annotation databases

EnsembliENST00000327304; ENSP00000323046; ENSG00000107371. [Q9NQT5-1]
ENST00000396521; ENSP00000379775; ENSG00000107371. [Q9NQT5-2]
ENST00000465229; ENSP00000418422; ENSG00000107371. [Q9NQT5-2]
GeneIDi51010.
KEGGihsa:51010.
UCSCiuc004aal.3. human. [Q9NQT5-1]
uc004aam.3. human. [Q9NQT5-2]

Polymorphism databases

DMDMi14285758.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35016.1. [Q9NQT5-1 ]
CCDS43805.1. [Q9NQT5-2 ]
RefSeqi NP_001002269.1. NM_001002269.2. [Q9NQT5-2 ]
NP_057126.2. NM_016042.3. [Q9NQT5-1 ]
UniGenei Hs.602571.
Hs.713483.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NN6 X-ray 3.35 G 1-275 [» ]
ProteinModelPortali Q9NQT5.
SMRi Q9NQT5. Positions 17-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119217. 19 interactions.
DIPi DIP-29847N.
IntActi Q9NQT5. 19 interactions.
MINTi MINT-3072286.
STRINGi 9606.ENSP00000323046.

PTM databases

PhosphoSitei Q9NQT5.

Polymorphism databases

DMDMi 14285758.

Proteomic databases

MaxQBi Q9NQT5.
PaxDbi Q9NQT5.
PeptideAtlasi Q9NQT5.
PRIDEi Q9NQT5.

Protocols and materials databases

DNASUi 51010.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327304 ; ENSP00000323046 ; ENSG00000107371 . [Q9NQT5-1 ]
ENST00000396521 ; ENSP00000379775 ; ENSG00000107371 . [Q9NQT5-2 ]
ENST00000465229 ; ENSP00000418422 ; ENSG00000107371 . [Q9NQT5-2 ]
GeneIDi 51010.
KEGGi hsa:51010.
UCSCi uc004aal.3. human. [Q9NQT5-1 ]
uc004aam.3. human. [Q9NQT5-2 ]

Organism-specific databases

CTDi 51010.
GeneCardsi GC09M037772.
HGNCi HGNC:17944. EXOSC3.
HPAi HPA020485.
MIMi 606489. gene.
614678. phenotype.
neXtProti NX_Q9NQT5.
Orphaneti 2254. Pontocerebellar hypoplasia type 1.
PharmGKBi PA134926550.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1097.
HOGENOMi HOG000184644.
HOVERGENi HBG051518.
InParanoidi Q9NQT5.
KOi K03681.
OMAi VNGRVWI.
OrthoDBi EOG76HQ2F.
PhylomeDBi Q9NQT5.
TreeFami TF314927.

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 EXOSC3. human.
EvolutionaryTracei Q9NQT5.
GeneWikii Exosome_component_3.
GenomeRNAii 51010.
NextBioi 53494.
PROi Q9NQT5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NQT5.
Bgeei Q9NQT5.
CleanExi HS_EXOSC3.
Genevestigatori Q9NQT5.

Family and domain databases

InterProi IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
[Graphical view ]
PANTHERi PTHR21321. PTHR21321. 1 hit.
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF54791. SSF54791. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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. 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. 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. Cited for: VARIANTS PCH1B ALA-31; ALA-132; PRO-139 AND ARG-238.

Entry informationi

Entry nameiEXOS3_HUMAN
AccessioniPrimary (citable) accession number: Q9NQT5
Secondary accession number(s): A8K0K6, Q5QP85, Q9Y3A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 136 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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