Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Exosome complex component RRP45

Gene

EXOSC9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. EXOSC9 binds to ARE-containing RNAs.4 Publications

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: UniProtKB
  2. AU-rich element binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: UniProtKB

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
  2. gene expression Source: Reactome
  3. immune response Source: UniProtKB
  4. nuclear mRNA surveillance Source: UniProtKB
  5. nuclear polyadenylation-dependent rRNA catabolic process Source: UniProtKB
  6. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  8. positive regulation of cell growth Source: UniProtKB
  9. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  10. 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 RRP45
Alternative name(s):
Autoantigen PM/Scl 1
Exosome component 9
P75 polymyositis-scleroderma overlap syndrome-associated autoantigen
Polymyositis/scleroderma autoantigen 1
Polymyositis/scleroderma autoantigen 75 kDa
Short name:
PM/Scl-75
Gene namesi
Name:EXOSC9
Synonyms:PMSCL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9137. EXOSC9.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication. Nucleusnucleolus 1 Publication. Nucleusnucleoplasm 1 Publication
Note: Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744).1 Publication
Isoform 3 : Nucleus
Note: Excluded from the nucleolus.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. exosome (RNase complex) Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. intermediate filament cytoskeleton Source: HPA
  6. nuclear chromosome Source: UniProtKB
  7. nuclear exosome (RNase complex) Source: UniProtKB
  8. nucleolus Source: UniProtKB
  9. nucleoplasm Source: UniProtKB
  10. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi388 – 3914PIIL → EECP: Abolishes interaction with SETX. 1 Publication
Mutagenesisi388 – 3914Missing : Abolishes interaction with SETX. 1 Publication
Mutagenesisi390 – 3912Missing : Abolishes interaction with SETX. 1 Publication
Mutagenesisi395 – 3984EEEE → AAAA: Abolishes interaction with SETX. 1 Publication
Mutagenesisi395 – 3984Missing : Abolishes interaction with SETX. 1 Publication

Organism-specific databases

PharmGKBiPA33463.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Exosome complex component RRP45PRO_0000139971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei297 – 2971N6-acetyllysine1 Publication
Modified residuei306 – 3061Phosphoserine5 Publications
Modified residuei346 – 3461Phosphoserine1 Publication
Modified residuei392 – 3921Phosphoserine2 Publications
Modified residuei394 – 3941Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ06265.
PaxDbiQ06265.
PRIDEiQ06265.

PTM databases

PhosphoSiteiQ06265.

Expressioni

Gene expression databases

BgeeiQ06265.
CleanExiHS_EXOSC9.
ExpressionAtlasiQ06265. baseline and differential.
GenevestigatoriQ06265.

Organism-specific databases

HPAiHPA041838.
HPA048257.

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 (PubMed:11719186, PubMed:12788944, PubMed:20531389). Interacts (via C-terminus region) with SETX (via N-terminus domain); the interaction enhances SETX sumoylation (PubMed:24105744).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EXOSC4Q9NPD33EBI-347966,EBI-371823

Protein-protein interaction databases

BioGridi111402. 22 interactions.
DIPiDIP-31286N.
IntActiQ06265. 15 interactions.
MINTiMINT-1036055.
STRINGi9606.ENSP00000368984.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1912Combined sources
Beta strandi36 – 394Combined sources
Beta strandi45 – 528Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 643Combined sources
Turni69 – 724Combined sources
Beta strandi76 – 827Combined sources
Turni84 – 863Combined sources
Beta strandi92 – 943Combined sources
Helixi96 – 994Combined sources
Helixi101 – 11313Combined sources
Beta strandi118 – 1214Combined sources
Turni125 – 1273Combined sources
Beta strandi128 – 13811Combined sources
Helixi146 – 15914Combined sources
Helixi176 – 1794Combined sources
Beta strandi191 – 1988Combined sources
Turni200 – 2023Combined sources
Beta strandi203 – 2086Combined sources
Helixi211 – 2166Combined sources
Beta strandi220 – 2267Combined sources
Turni227 – 2293Combined sources
Beta strandi230 – 2389Combined sources
Helixi244 – 27734Combined sources
Helixi287 – 2904Combined sources
Beta strandi291 – 2988Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35A1-302[»]
ProteinModelPortaliQ06265.
SMRiQ06265. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06265.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 268268ARE bindingAdd
BLAST

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051523.
InParanoidiQ06265.
KOiK03678.
OMAiKMDTGVE.
OrthoDBiEOG7X9G70.
PhylomeDBiQ06265.
TreeFamiTF300092.

Family and domain databases

InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06265-1) [UniParc]FASTAAdd to basket

Also known as: PM/SCL-75c-alpha

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

        10         20         30         40         50
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL
60 70 80 90 100
GKTRVLGQVS CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV
110 120 130 140 150
KLNRLMERCL RNSKCIDTES LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS
160 170 180 190 200
IAAIVALCHF RRPDVSVQGD EVTLYTPEER DPVPLSIHHM PICVSFAFFQ
210 220 230 240 250
QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI MLLKDQVLRC
260 270 280 290 300
SKIAGVKVAE ITELILKALE NDQKVRKEGG KFGFAESIAN QRITAFKMEK
310 320 330 340 350
APIDTSDVEE KAEEIIAEAE PPSEVVSTPV LWTPGTAQIG EGVENSWGDL
360 370 380 390 400
EDSEKEDDEG GGDQAIILDG IKMDTGVEVS DIGSQDAPII LSDSEEEEMI
410 420 430
ILEPDKNPKK IRTQTTSAKQ EKAPSKKPVK RRKKKRAAN
Length:439
Mass (Da):48,949
Last modified:May 15, 2007 - v3
Checksum:i7E27322F094ED3F3
GO
Isoform 2 (identifier: Q06265-2) [UniParc]FASTAAdd to basket

Also known as: PM/SCL-75c-beta

The sequence of this isoform differs from the canonical sequence as follows:
     385-385: Q → QELGFHHVGQTGLEFLTS

Note: Contains a phosphoserine at position 409. Contains a phosphoserine at position 411.1 Publication

Show »
Length:456
Mass (Da):50,803
Checksum:i693B31BE41C55545
GO
Isoform 3 (identifier: Q06265-3) [UniParc]FASTAAdd to basket

Also known as: PM/SCL-75a-alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Show »
Length:355
Mass (Da):39,235
Checksum:iDC37BB31767B6621
GO
Isoform 4 (identifier: Q06265-4) [UniParc]FASTAAdd to basket

Also known as: PM/SCL-75a-beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
     385-385: Q → QELGFHHVGQTGLEFLTS

Note: Contains a phosphoserine at position 325. Contains a phosphoserine at position 327.1 Publication

Show »
Length:372
Mass (Da):41,089
Checksum:iDB666F47B5422E7E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti366 – 3661I → V.
Corresponds to variant rs1803183 [ dbSNP | Ensembl ].
VAR_051867
Natural varianti425 – 4251S → T.
Corresponds to variant rs1051881 [ dbSNP | Ensembl ].
VAR_014924

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8484Missing in isoform 3 and isoform 4. 2 PublicationsVSP_025555Add
BLAST
Alternative sequencei385 – 3851Q → QELGFHHVGQTGLEFLTS in isoform 2 and isoform 4. 2 PublicationsVSP_025556

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58460 mRNA. Translation: AAA58384.1.
U09215 mRNA. Translation: AAA18832.1.
AJ505989 mRNA. Translation: CAD44530.1.
AJ517294 mRNA. Translation: CAD56889.1.
AC079341 Genomic DNA. Translation: AAY40968.1.
CCDSiCCDS34057.1. [Q06265-2]
CCDS3722.2. [Q06265-1]
PIRiG01425.
RefSeqiNP_001029366.1. NM_001034194.1. [Q06265-2]
NP_005024.2. NM_005033.2. [Q06265-1]
UniGeneiHs.91728.

Genome annotation databases

EnsembliENST00000243498; ENSP00000243498; ENSG00000123737. [Q06265-1]
ENST00000379663; ENSP00000368984; ENSG00000123737. [Q06265-2]
GeneIDi5393.
KEGGihsa:5393.
UCSCiuc003idz.3. human. [Q06265-2]
uc003iea.3. human. [Q06265-1]

Polymorphism databases

DMDMi147744559.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58460 mRNA. Translation: AAA58384.1.
U09215 mRNA. Translation: AAA18832.1.
AJ505989 mRNA. Translation: CAD44530.1.
AJ517294 mRNA. Translation: CAD56889.1.
AC079341 Genomic DNA. Translation: AAY40968.1.
CCDSiCCDS34057.1. [Q06265-2]
CCDS3722.2. [Q06265-1]
PIRiG01425.
RefSeqiNP_001029366.1. NM_001034194.1. [Q06265-2]
NP_005024.2. NM_005033.2. [Q06265-1]
UniGeneiHs.91728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35A1-302[»]
ProteinModelPortaliQ06265.
SMRiQ06265. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111402. 22 interactions.
DIPiDIP-31286N.
IntActiQ06265. 15 interactions.
MINTiMINT-1036055.
STRINGi9606.ENSP00000368984.

PTM databases

PhosphoSiteiQ06265.

Polymorphism databases

DMDMi147744559.

Proteomic databases

MaxQBiQ06265.
PaxDbiQ06265.
PRIDEiQ06265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243498; ENSP00000243498; ENSG00000123737. [Q06265-1]
ENST00000379663; ENSP00000368984; ENSG00000123737. [Q06265-2]
GeneIDi5393.
KEGGihsa:5393.
UCSCiuc003idz.3. human. [Q06265-2]
uc003iea.3. human. [Q06265-1]

Organism-specific databases

CTDi5393.
GeneCardsiGC04P122722.
HGNCiHGNC:9137. EXOSC9.
HPAiHPA041838.
HPA048257.
MIMi606180. gene.
neXtProtiNX_Q06265.
PharmGKBiPA33463.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2123.
GeneTreeiENSGT00530000063093.
HOGENOMiHOG000229504.
HOVERGENiHBG051523.
InParanoidiQ06265.
KOiK03678.
OMAiKMDTGVE.
OrthoDBiEOG7X9G70.
PhylomeDBiQ06265.
TreeFamiTF300092.

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.

Miscellaneous databases

EvolutionaryTraceiQ06265.
GeneWikiiExosome_component_9.
GenomeRNAii5393.
NextBioi20906.
PROiQ06265.
SOURCEiSearch...

Gene expression databases

BgeeiQ06265.
CleanExiHS_EXOSC9.
ExpressionAtlasiQ06265. baseline and differential.
GenevestigatoriQ06265.

Family and domain databases

InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of an autoantigen of PM-Scl in the polymyositis/scleroderma overlap syndrome: a unique and complete human cDNA encoding an apparent 75-kD acidic protein of the nucleolar complex."
    Alderuccio F., Chan E.K.L., Tan E.M.
    J. Exp. Med. 173:941-952(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Lymphoblastoma.
  2. "Nucleotide sequence of an alternatively spliced cDNA coding for PM-Scl-75, an autoantigen of the Polymyositis/Scleroderma overlap syndrome."
    Stahnke G., Haubruck H.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  3. "The association of the human PM/Scl-75 autoantigen with the exosome is dependent on a newly identified N terminus."
    Raijmakers R., Egberts W.V., van Venrooij W.J., Pruijn G.J.
    J. Biol. Chem. 278:30698-30704(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, IDENTIFICATION IN THE RNA EXOSOME COMPLEX.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA EXOSOME CORE COMPLEX.
  7. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOPLASMIC MRNA DEGRADATION, ARE BINDING.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Adenylation and exosome-mediated degradation of cotranscriptionally cleaved pre-messenger RNA in human cells."
    West S., Gromak N., Norbury C.J., Proudfoot N.J.
    Mol. Cell 21:437-443(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
  10. "Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome."
    Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C., Wilusz C.J., Wilusz J.
    RNA 12:1810-1816(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ARE-CONTAINING MRNA-BINDING.
  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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage."
    Richard P., Feng S., Manley J.L.
    Genes Dev. 27:2227-2232(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETX, SUBCELLULAR LOCATION, MUTAGENESIS OF 388-PRO--LEU-391; 390-ILE-LEU-391 AND 395-GLU--GLU-398.
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-346, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-411 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-327 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
  24. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2006)

Entry informationi

Entry nameiEXOS9_HUMAN
AccessioniPrimary (citable) accession number: Q06265
Secondary accession number(s): Q12883
, Q4W5P5, Q86Y41, Q86Y48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 15, 2007
Last modified: March 4, 2015
This is version 144 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

Caution

The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.