Q9NQT5 (EXOS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.16
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.14 Ref.17 Ref.18
Subcellular location	Cytoplasm. Nucleus › nucleolus. Nucleus Ref.6 Ref.11 Ref.14.
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.21
Sequence similarities	Belongs to the RRP40 family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	RNA-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CUT catabolic process Inferred from mutant phenotype Ref.13. Source: UniProtKB DNA deamination Inferred from direct assay Ref.16. Source: UniProtKB exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Inferred from mutant phenotype Ref.10. Source: UniProtKB isotype switching Inferred from sequence or structural similarity. Source: UniProtKB rRNA processing Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cytoplasmic exosome (RNase complex) Inferred from direct assay Ref.1. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nuclear exosome (RNase complex) Inferred from direct assay Ref.1. Source: UniProtKB nucleolus Inferred from direct assay Ref.14. Source: UniProtKB transcriptionally active chromatin Inferred from mutant phenotype PubMed 20699273. Source: UniProtKB
Molecular_function	3'-5'-exoribonuclease activity Non-traceable author statement Ref.1. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DIS3	Q9Y2L1	2	EBI-371866,EBI-373539
EXOSC2	Q13868	5	EBI-371866,EBI-301735
EXOSC4	Q9NPD3	3	EBI-371866,EBI-371823
EXOSC5	Q9NQT4	7	EBI-371866,EBI-371876
EXOSC8	Q96B26	3	EBI-371866,EBI-371922

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 275

274

Exosome complex component RRP40

PRO_0000087131

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Natural variations

Alternative sequence

159 – 275

117

VGDLI…RLAES → AISSRL in isoform 2.

VSP_043457

Natural variant

31

1

G → A in PCH1B. Ref.21

VAR_068505

Natural variant

132

1

D → A in PCH1B. Ref.21
Corresponds to variant rs141138948 [ dbSNP | Ensembl ].

VAR_068506

Natural variant

139

1

A → P in PCH1B. Ref.21

VAR_068507

Natural variant

225

1

Y → H.
Corresponds to variant rs3208406 [ dbSNP | Ensembl ].

VAR_054098

Natural variant

238

1

W → R in PCH1B. Ref.21

VAR_068508

Experimental info

Sequence conflict

56 – 65

10

NARACSRVRV → MLERARGCAF in AAD34097. Ref.7

Sequence conflict

95

1

S → G in AAD34097. Ref.7

Secondary structure

1

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275

Helix Strand Turn

Details...

Helix

22 – 24

3

Beta strand

25 – 27

3

Beta strand

30 – 34

5

Beta strand

45 – 49

5

Beta strand

78 – 80

3

Beta strand

85 – 89

5

Turn

92 – 94

3

Beta strand

99 – 103

5

Beta strand

113 – 125

13

Beta strand

128 – 132

5

Beta strand

134 – 137

4

Beta strand

141 – 143

3

Beta strand

145 – 147

3

Beta strand

153 – 157

5

Beta strand

162 – 169

8

Beta strand

177 – 179

3

Turn

183 – 185

3

Beta strand

198 – 200

3

Helix

204 – 211

8

Helix

217 – 220

4

Beta strand

224 – 226

3

Beta strand

230 – 232

3

Turn

233 – 235

3

Beta strand

236 – 239

4

Helix

244 – 256

13

Turn

262 – 264

3

Helix

265 – 274

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 264322144A199166	FASTA	275	29,572
	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
	Isoform 2 [UniParc]. Checksum: 51C07B44337D0076	FASTA	164	17,248
	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 VTAKSGDIFK VDVGGSEPAS LSYLSFEGAT KRNRPNVQAI SSRL

References

	« Hide 'large scale' referencesShow '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. , 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]	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 (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, 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]	"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, MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH DIS3L.
[15]	"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].
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	Erratum Liu Q., Greimann J.C., Lima C.D. Cell 131:188-189(2007)
[21]	"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. , 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.

IPI

IPI00015956.
IPI00434985.

RefSeq

NP_001002269.1. NM_001002269.2.
NP_057126.2. NM_016042.3.

UniGene

Hs.602571.
Hs.713483.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NN6	X-ray	3.35	G	1-275	[»]

ProteinModelPortal

Q9NQT5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29847N.

IntAct

Q9NQT5. 19 interactions.

MINT

MINT-3072286.

STRING

9606.ENSP00000323046.

PTM databases

PhosphoSite

Q9NQT5.

Polymorphism databases

DMDM

14285758.

Proteomic databases

PaxDb

Q9NQT5.

PeptideAtlas

Q9NQT5.

PRIDE

Q9NQT5.

Protocols and materials databases

DNASU

51010.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327304; ENSP00000323046; ENSG00000107371.
ENST00000396521; ENSP00000379775; ENSG00000107371.
ENST00000465229; ENSP00000418422; ENSG00000107371.

GeneID

51010.

KEGG

hsa:51010.

UCSC

uc004aal.2. human.
uc004aam.2. human.

Organism-specific databases

CTD

51010.

GeneCards

GC09M037772.

HGNC

HGNC:17944. EXOSC3.

HPA

HPA020485.

MIM

606489. gene.
614678. phenotype.

neXtProt

NX_Q9NQT5.

Orphanet

2254. Pontocerebellar hypoplasia type 1.

PharmGKB

PA134926550.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1097.

HOGENOM

HOG000184644.

HOVERGEN

HBG051518.

InParanoid

Q9NQT5.

KO

K03681.

OMA

HKEPGSG.

PhylomeDB

Q9NQT5.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9NQT5.

Bgee

Q9NQT5.

CleanEx

HS_EXOSC3.

Genevestigator

Q9NQT5.

GermOnline

ENSG00000107371. Homo sapiens.

Family and domain databases

InterPro

IPR026699. Exosome_RNA_bind1/RRP40/RRP4.
[Graphical view]

PANTHER

PTHR21321. PTHR21321. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

EXOSC3. human.

EvolutionaryTrace

Q9NQT5.

GenomeRNAi

51010.

NextBio

53494.

SOURCE

Search...

Entry information

Entry name

EXOS3_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 123 of the entry and version 3 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.