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Q01780 (EXOSX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome 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 names
Name:EXOSC10
Synonyms:PMSCL, PMSCL2, RRP6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length885 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20

Subunit structure

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. Ref.10 Ref.12 Ref.13 Ref.18

Subcellular location

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. Ref.8 Ref.9 Ref.13 Ref.14 Ref.17

Sequence similarities

Contains 1 3'-5' exonuclease domain.

Contains 1 HRDC domain.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
rRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCUT catabolic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

RNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from direct assay PubMed 17174896. Source: GOC

dosage compensation by inactivation of X chromosome

Inferred from electronic annotation. Source: Ensembl

histone mRNA catabolic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

maturation of 5.8S rRNA

Inferred from mutant phenotype Ref.13Ref.20. Source: UniProtKB

nuclear mRNA surveillance

Inferred from mutant phenotype Ref.14. Source: UniProtKB

nuclear polyadenylation-dependent rRNA catabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

nuclear retention of unspliced pre-mRNA at the site of transcription

Inferred from mutant phenotype Ref.19. Source: UniProtKB

nuclear-transcribed mRNA catabolic process

Inferred from mutant phenotype Ref.14. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype PubMed 22890540. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.14Ref.17. Source: UniProtKB

exosome (RNase complex)

Inferred from direct assay Ref.18. Source: UniProtKB

nuclear exosome (RNase complex)

Inferred from electronic annotation. Source: InterPro

nucleolus

Inferred from direct assay Ref.17. Source: UniProtKB

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

transcriptionally active chromatin

Inferred from mutant phenotype Ref.19. Source: UniProtKB

   Molecular_function3'-5' exonuclease activity

Inferred from electronic annotation. Source: InterPro

exoribonuclease activity

Inferred from direct assay PubMed 17174896. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01780-1)

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: Q01780-2)

The sequence of this isoform differs from the canonical sequence as follows:
     695-719: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 885885Exosome component 10
PRO_0000087133

Regions

Domain503 – 58381HRDC

Natural variations

Alternative sequence695 – 71925Missing in isoform 2.
VSP_004362

Secondary structure

.................................................................... 885
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2000. Version 2.
Checksum: A37BDC8F49BF2E57

FASTA885100,831
        10         20         30         40         50         60 
MAPPSTREPR VLSATSATKS DGEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY 

        70         80         90        100        110        120 
DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDANDVI 

       130        140        150        160        170        180 
LERVGILLDE ASGVNKNQQP VLPAGLQVPK TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI 

       190        200        210        220        230        240 
IRPQLKFREK IDNSNTPFLP KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF 

       250        260        270        280        290        300 
IHQQRTQQVE QDMFAHPYQY ELNHFTPADA VLQKPQPQLY RPIEETPCHF ISSLDELVEL 

       310        320        330        340        350        360 
NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY ILNESLTDPA 

       370        380        390        400        410        420 
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR HSLDHLLKLY CNVDSNKQYQ 

       430        440        450        460        470        480 
LADWRIRPLP EEMLSYARDD THYLLYIYDK MRLEMWERGN GQPVQLQVVW QRSRDICLKK 

       490        500        510        520        530        540 
FIKPIFTDES YLELYRKQKK HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI 

       550        560        570        580        590        600 
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE 

       610        620        630        640        650        660 
RLENVLFGPH DCSHAPPDGY PIIPTSGSVP VQKQASLFPD EKEDNLLGTT CLIATAVITL 

       670        680        690        700        710        720 
FNEPSAEDSK KGPLTVAQKK AQNIMESFEN PFRMFLPSLG HRAPVSQAAK FDPSTKIYEI 

       730        740        750        760        770        780 
SNRWKLAQVQ VQKDSKEAVK KKAAEQTAAR EQAKEACKAA AEQAISVRQQ VVLENAAKKR 

       790        800        810        820        830        840 
ERATSDPRTT EQKQEKKRLK ISKKPKDPEP PEKEFTPYDY SQSDFKAFAG NSKSKVSSQF 

       850        860        870        880 
DPNKQTPSGK KCIAAKKIKQ SVGNKSMSFP TGKSDRGFRY NWPQR 

« Hide

Isoform 2 [UniParc].

Checksum: B7FBE8B15F28BFE2
Show »

FASTA86098,089

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L."
Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A., Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S., Stepien P.P., Dziembowski A., Jensen T.H.
EMBO J. 29:2342-2357(2010) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS126.1. [Q01780-2]
CCDS30584.1. [Q01780-1]
PIRA43920.
JH0796.
RefSeqNP_001001998.1. NM_001001998.1. [Q01780-1]
NP_002676.1. NM_002685.2. [Q01780-2]
UniGeneHs.632368.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPRNMR-A483-593[»]
3SAFX-ray2.50A/B180-606[»]
3SAGX-ray2.70A/B180-606[»]
3SAHX-ray2.65A/B180-606[»]
ProteinModelPortalQ01780.
SMRQ01780. Positions 179-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111403. 52 interactions.
IntActQ01780. 45 interactions.
MINTMINT-1143843.
STRING9606.ENSP00000366135.

PTM databases

PhosphoSiteQ01780.

Polymorphism databases

DMDM8928564.

2D gel databases

SWISS-2DPAGEQ01780.

Proteomic databases

MaxQBQ01780.
PaxDbQ01780.
PRIDEQ01780.

Protocols and materials databases

DNASU5394.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304457; ENSP00000307307; ENSG00000171824. [Q01780-2]
ENST00000376936; ENSP00000366135; ENSG00000171824. [Q01780-1]
GeneID5394.
KEGGhsa:5394.
UCSCuc001asa.3. human. [Q01780-1]
uc001asb.3. human. [Q01780-2]

Organism-specific databases

CTD5394.
GeneCardsGC01M011126.
HGNCHGNC:9138. EXOSC10.
HPAHPA028470.
HPA028484.
MIM605960. gene.
neXtProtNX_Q01780.
PharmGKBPA33464.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0349.
HOGENOMHOG000001579.
HOVERGENHBG051524.
InParanoidQ01780.
KOK12591.
OMAGNKSMSF.
OrthoDBEOG7Z3F3S.
PhylomeDBQ01780.
TreeFamTF105991.

Gene expression databases

ArrayExpressQ01780.
BgeeQ01780.
CleanExHS_EXOSC10.
GenevestigatorQ01780.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view]
SMARTSM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]
SUPFAMSSF47819. SSF47819. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEPS50967. HRDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEXOSC10. human.
EvolutionaryTraceQ01780.
GeneWikiExosome_component_10.
GenomeRNAi5394.
NextBio20912.
PROQ01780.
SOURCESearch...

Entry information

Entry nameEXOSX_HUMAN
AccessionPrimary (citable) accession number: Q01780
Secondary accession number(s): B1AKQ0, B1AKQ1, Q15158
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM