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Q01780

- EXOSX_HUMAN

UniProt

Q01780 - EXOSX_HUMAN

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Protein
Exosome component 10
Gene
EXOSC10, PMSCL, PMSCL2, RRP6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 has 3'-5' exonuclease activity By similarity. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of SKIV2L2, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA.8 Publications

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: InterPro
  2. exoribonuclease activity Source: UniProtKB
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. CUT catabolic process Source: UniProtKB
  2. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  3. dosage compensation by inactivation of X chromosome Source: Ensembl
  4. histone mRNA catabolic process Source: UniProtKB
  5. maturation of 5.8S rRNA Source: UniProtKB
  6. nuclear mRNA surveillance Source: UniProtKB
  7. nuclear polyadenylation-dependent rRNA catabolic process Source: UniProtKB
  8. nuclear retention of unspliced pre-mRNA at the site of transcription Source: UniProtKB
  9. nuclear-transcribed mRNA catabolic process Source: UniProtKB
  10. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Nonsense-mediated mRNA decay, rRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome component 10 (EC:3.1.13.-)
Alternative name(s):
Autoantigen PM/Scl 2
P100 polymyositis-scleroderma overlap syndrome-associated autoantigen
Polymyositis/scleroderma autoantigen 100 kDa
Short name:
PM/Scl-100
Polymyositis/scleroderma autoantigen 2
Gene namesi
Name:EXOSC10
Synonyms:PMSCL, PMSCL2, RRP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9138. EXOSC10.

Subcellular locationi

Cytoplasm. Nucleusnucleolus. Nucleus
Note: Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence of a nucleolar RNA exosome complex form.5 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885Exosome component 10
PRO_0000087133Add
BLAST

Proteomic databases

MaxQBiQ01780.
PaxDbiQ01780.
PRIDEiQ01780.

2D gel databases

SWISS-2DPAGEQ01780.

PTM databases

PhosphoSiteiQ01780.

Expressioni

Gene expression databases

ArrayExpressiQ01780.
BgeeiQ01780.
CleanExiHS_EXOSC10.
GenevestigatoriQ01780.

Organism-specific databases

HPAiHPA028470.
HPA028484.

Interactioni

Subunit structurei

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Interacts with C1D and MPHOSPH6. Interacts with ALYREF/THOC4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C1DQ139015EBI-358236,EBI-3844053
DIS3Q9Y2L14EBI-358236,EBI-373539
EXOSC4Q9NPD33EBI-358236,EBI-371823
MPHOSPH6Q995474EBI-358236,EBI-373187

Protein-protein interaction databases

BioGridi111403. 53 interactions.
IntActiQ01780. 45 interactions.
MINTiMINT-1143843.
STRINGi9606.ENSP00000366135.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi183 – 1864
Beta strandi194 – 1963
Helixi214 – 2163
Helixi218 – 2203
Beta strandi253 – 2553
Helixi259 – 2635
Helixi269 – 2724
Helixi283 – 2853
Beta strandi288 – 2914
Helixi294 – 30411
Beta strandi308 – 31710
Beta strandi325 – 3328
Beta strandi337 – 3415
Turni342 – 3454
Helixi346 – 3527
Helixi353 – 3564
Beta strandi361 – 3677
Helixi369 – 37911
Beta strandi384 – 3885
Helixi389 – 3957
Helixi403 – 4119
Turni418 – 4214
Helixi431 – 44212
Helixi444 – 45815
Beta strandi461 – 4633
Helixi464 – 47613
Helixi490 – 4923
Helixi493 – 4964
Beta strandi497 – 5004
Helixi504 – 52421
Helixi528 – 5314
Helixi534 – 54310
Helixi548 – 5525
Beta strandi555 – 5573
Helixi560 – 5645
Helixi566 – 57712
Helixi583 – 5864

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPRNMR-A483-593[»]
3SAFX-ray2.50A/B180-606[»]
3SAGX-ray2.70A/B180-606[»]
3SAHX-ray2.65A/B180-606[»]
ProteinModelPortaliQ01780.
SMRiQ01780. Positions 179-595.

Miscellaneous databases

EvolutionaryTraceiQ01780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 58381HRDC
Add
BLAST

Sequence similaritiesi

Contains 1 HRDC domain.

Phylogenomic databases

eggNOGiCOG0349.
HOGENOMiHOG000001579.
HOVERGENiHBG051524.
InParanoidiQ01780.
KOiK12591.
OMAiGNKSMSF.
OrthoDBiEOG7Z3F3S.
PhylomeDBiQ01780.
TreeFamiTF105991.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view]
SMARTiSM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]
SUPFAMiSSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50967. HRDC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q01780-1) [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

MAPPSTREPR VLSATSATKS DGEMVLPGFP DADSFVKFAL GSVVAVTKAS    50
GGLPQFGDEY DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR 100
SKVTELEDKF DLLVDANDVI LERVGILLDE ASGVNKNQQP VLPAGLQVPK 150
TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI IRPQLKFREK IDNSNTPFLP 200
KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF IHQQRTQQVE 250
QDMFAHPYQY ELNHFTPADA VLQKPQPQLY RPIEETPCHF ISSLDELVEL 300
NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY 350
ILNESLTDPA IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR 400
HSLDHLLKLY CNVDSNKQYQ LADWRIRPLP EEMLSYARDD THYLLYIYDK 450
MRLEMWERGN GQPVQLQVVW QRSRDICLKK FIKPIFTDES YLELYRKQKK 500
HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI AEELPKEPQG 550
IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE 600
RLENVLFGPH DCSHAPPDGY PIIPTSGSVP VQKQASLFPD EKEDNLLGTT 650
CLIATAVITL FNEPSAEDSK KGPLTVAQKK AQNIMESFEN PFRMFLPSLG 700
HRAPVSQAAK FDPSTKIYEI SNRWKLAQVQ VQKDSKEAVK KKAAEQTAAR 750
EQAKEACKAA AEQAISVRQQ VVLENAAKKR ERATSDPRTT EQKQEKKRLK 800
ISKKPKDPEP PEKEFTPYDY SQSDFKAFAG NSKSKVSSQF DPNKQTPSGK 850
KCIAAKKIKQ SVGNKSMSFP TGKSDRGFRY NWPQR 885
Length:885
Mass (Da):100,831
Last modified:December 1, 2000 - v2
Checksum:iA37BDC8F49BF2E57
GO
Isoform 2 (identifier: Q01780-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     695-719: Missing.

Note: No experimental confirmation available.

Show »
Length:860
Mass (Da):98,089
Checksum:iB7FBE8B15F28BFE2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei695 – 71925Missing in isoform 2.
VSP_004362Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66113 mRNA. Translation: CAA46904.1.
L01457 mRNA. Translation: AAB59352.1.
AJ300188 Genomic DNA. Translation: CAC15569.1.
AL109811 Genomic DNA. Translation: CAI22106.1.
AL109811 Genomic DNA. Translation: CAI22107.1.
CH471130 Genomic DNA. Translation: EAW71679.1.
BC039901 mRNA. Translation: AAH39901.1.
BC073788 mRNA. Translation: AAH73788.1.
CCDSiCCDS126.1. [Q01780-2]
CCDS30584.1. [Q01780-1]
PIRiA43920.
JH0796.
RefSeqiNP_001001998.1. NM_001001998.1. [Q01780-1]
NP_002676.1. NM_002685.2. [Q01780-2]
UniGeneiHs.632368.

Genome annotation databases

EnsembliENST00000304457; ENSP00000307307; ENSG00000171824. [Q01780-2]
ENST00000376936; ENSP00000366135; ENSG00000171824. [Q01780-1]
GeneIDi5394.
KEGGihsa:5394.
UCSCiuc001asa.3. human. [Q01780-1]
uc001asb.3. human. [Q01780-2]

Polymorphism databases

DMDMi8928564.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66113 mRNA. Translation: CAA46904.1 .
L01457 mRNA. Translation: AAB59352.1 .
AJ300188 Genomic DNA. Translation: CAC15569.1 .
AL109811 Genomic DNA. Translation: CAI22106.1 .
AL109811 Genomic DNA. Translation: CAI22107.1 .
CH471130 Genomic DNA. Translation: EAW71679.1 .
BC039901 mRNA. Translation: AAH39901.1 .
BC073788 mRNA. Translation: AAH73788.1 .
CCDSi CCDS126.1. [Q01780-2 ]
CCDS30584.1. [Q01780-1 ]
PIRi A43920.
JH0796.
RefSeqi NP_001001998.1. NM_001001998.1. [Q01780-1 ]
NP_002676.1. NM_002685.2. [Q01780-2 ]
UniGenei Hs.632368.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CPR NMR - A 483-593 [» ]
3SAF X-ray 2.50 A/B 180-606 [» ]
3SAG X-ray 2.70 A/B 180-606 [» ]
3SAH X-ray 2.65 A/B 180-606 [» ]
ProteinModelPortali Q01780.
SMRi Q01780. Positions 179-595.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111403. 53 interactions.
IntActi Q01780. 45 interactions.
MINTi MINT-1143843.
STRINGi 9606.ENSP00000366135.

PTM databases

PhosphoSitei Q01780.

Polymorphism databases

DMDMi 8928564.

2D gel databases

SWISS-2DPAGE Q01780.

Proteomic databases

MaxQBi Q01780.
PaxDbi Q01780.
PRIDEi Q01780.

Protocols and materials databases

DNASUi 5394.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304457 ; ENSP00000307307 ; ENSG00000171824 . [Q01780-2 ]
ENST00000376936 ; ENSP00000366135 ; ENSG00000171824 . [Q01780-1 ]
GeneIDi 5394.
KEGGi hsa:5394.
UCSCi uc001asa.3. human. [Q01780-1 ]
uc001asb.3. human. [Q01780-2 ]

Organism-specific databases

CTDi 5394.
GeneCardsi GC01M011126.
HGNCi HGNC:9138. EXOSC10.
HPAi HPA028470.
HPA028484.
MIMi 605960. gene.
neXtProti NX_Q01780.
PharmGKBi PA33464.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0349.
HOGENOMi HOG000001579.
HOVERGENi HBG051524.
InParanoidi Q01780.
KOi K12591.
OMAi GNKSMSF.
OrthoDBi EOG7Z3F3S.
PhylomeDBi Q01780.
TreeFami TF105991.

Miscellaneous databases

ChiTaRSi EXOSC10. human.
EvolutionaryTracei Q01780.
GeneWikii Exosome_component_10.
GenomeRNAii 5394.
NextBioi 20912.
PROi Q01780.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01780.
Bgeei Q01780.
CleanExi HS_EXOSC10.
Genevestigatori Q01780.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view ]
SMARTi SM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view ]
SUPFAMi SSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEi PS50967. HRDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the cDNA coding for a polymyositis-scleroderma overlap syndrome-related nucleolar 100-kD protein."
    Bluethner M., Bautz F.A.
    J. Exp. Med. 176:973-980(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Cloning of a complementary DNA coding for the 100-kD antigenic protein of the PM-Scl autoantigen."
    Ge Q., Frank M.B., O'Brien C., Targoff I.N.
    J. Clin. Invest. 90:559-570(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Thymocyte.
  3. "The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
    Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
    Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lymph and Skin.
  7. "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.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
    Lejeune F., Li X., Maquat L.E.
    Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, SUBCELLULAR LOCATION.
  10. "A protein interaction framework for human mRNA degradation."
    Lehner B., Sanderson C.M.
    Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN INTERACTION.
  11. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
  12. "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
    Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
    Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALYREF.
  13. "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing."
    Schilders G., van Dijk E., Pruijn G.J.M.
    Nucleic Acids Res. 35:2564-2572(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH C1D AND MPHOSPH6.
  14. "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.
  15. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
    Mullen T.E., Marzluff W.F.
    Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
  16. "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.
  17. Cited for: ASSOCIATION WITH THE RNA EXOSOME COMPLEX, SUBCELLULAR LOCATION.
  18. "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.
  19. "A link between nuclear RNA surveillance, the human exosome and RNA polymerase II transcriptional termination."
    de Almeida S.F., Garcia-Sacristan A., Custodio N., Carmo-Fonseca M.
    Nucleic Acids Res. 38:8015-8026(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEAR MRNA SURVEILLANCE.
  20. "Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells."
    Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.
    Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RRNA MATURATION.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Solution structure of the HRDC domain of human exosome component 10."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 483-593.

Entry informationi

Entry nameiEXOSX_HUMAN
AccessioniPrimary (citable) accession number: Q01780
Secondary accession number(s): B1AKQ0, B1AKQ1, Q15158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 1, 2000
Last modified: September 3, 2014
This is version 154 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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