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Q06265 (EXOS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 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 names
Name:EXOSC9
Synonyms:PMSCL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence 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. EXOSC9 binds to ARE-containing RNAs. Ref.7 Ref.9 Ref.10 Ref.11

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. Ref.3 Ref.6 Ref.16

Subcellular location

Cytoplasm. Nucleusnucleolus Ref.3 Ref.11.

Isoform 1: Nucleusnucleolus Ref.3 Ref.11.

Isoform 2: Nucleusnucleolus Ref.3 Ref.11.

Isoform 3: Nucleus. Note: Excluded from the nucleolus. Ref.3 Ref.11

Sequence similarities

Belongs to the RNase PH family.

Caution

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

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, exonucleolytic

Non-traceable author statement PubMed 11879549. Source: GOC

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Inferred from mutant phenotype Ref.7. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

immune response

Non-traceable author statement PubMed 11879549. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear mRNA surveillance

Inferred from mutant phenotype Ref.11. Source: UniProtKB

nuclear polyadenylation-dependent rRNA catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

nuclear-transcribed mRNA catabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

positive regulation of cell growth

Inferred from mutant phenotype Ref.11. Source: UniProtKB

rRNA processing

Non-traceable author statement PubMed 11879549. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exosome (RNase complex)

Inferred from direct assay Ref.16. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nuclear exosome (RNase complex)

Inferred from direct assay PubMed 22791713. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.11PubMed 22791713. Source: UniProtKB

   Molecular_function3'-5'-exoribonuclease activity

Non-traceable author statement PubMed 11879549. Source: UniProtKB

AU-rich element binding

Inferred from direct assay Ref.7. Source: UniProtKB

RNA binding

Non-traceable author statement PubMed 11879549. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EXOSC4Q9NPD33EBI-347966,EBI-371823

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06265-1)

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.
Isoform 2 (identifier: Q06265-2)

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

The sequence of this isoform differs from the canonical sequence as follows:
     385-385: Q → QELGFHHVGQTGLEFLTS
Isoform 3 (identifier: Q06265-3)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
Isoform 4 (identifier: Q06265-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Exosome complex component RRP45
PRO_0000139971

Regions

Region1 – 268268ARE binding

Amino acid modifications

Modified residue2971N6-acetyllysine Ref.15
Modified residue3061Phosphoserine Ref.12 Ref.14 Ref.17 Ref.19
Modified residue3921Phosphoserine Ref.12 Ref.17
Modified residue3941Phosphoserine Ref.12 Ref.17

Natural variations

Alternative sequence1 – 8484Missing in isoform 3 and isoform 4.
VSP_025555
Alternative sequence3851Q → QELGFHHVGQTGLEFLTS in isoform 2 and isoform 4.
VSP_025556
Natural variant3661I → V.
Corresponds to variant rs1803183 [ dbSNP | Ensembl ].
VAR_051867
Natural variant4251S → T.
Corresponds to variant rs1051881 [ dbSNP | Ensembl ].
VAR_014924

Secondary structure

................................................ 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PM/SCL-75c-alpha) [UniParc].

Last modified May 15, 2007. Version 3.
Checksum: 7E27322F094ED3F3

FASTA43948,949
        10         20         30         40         50         60 
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL GKTRVLGQVS 

        70         80         90        100        110        120 
CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLMERCL RNSKCIDTES 

       130        140        150        160        170        180 
LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGD EVTLYTPEER 

       190        200        210        220        230        240 
DPVPLSIHHM PICVSFAFFQ QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI 

       250        260        270        280        290        300 
MLLKDQVLRC SKIAGVKVAE ITELILKALE NDQKVRKEGG KFGFAESIAN QRITAFKMEK 

       310        320        330        340        350        360 
APIDTSDVEE KAEEIIAEAE PPSEVVSTPV LWTPGTAQIG EGVENSWGDL EDSEKEDDEG 

       370        380        390        400        410        420 
GGDQAIILDG IKMDTGVEVS DIGSQDAPII LSDSEEEEMI ILEPDKNPKK IRTQTTSAKQ 

       430 
EKAPSKKPVK RRKKKRAAN 

« Hide

Isoform 2 (PM/SCL-75c-beta) [UniParc].

Checksum: 693B31BE41C55545
Show »

FASTA45650,803
Isoform 3 (PM/SCL-75a-alpha) [UniParc].

Checksum: DC37BB31767B6621
Show »

FASTA35539,235
Isoform 4 (PM/SCL-75a-beta) [UniParc].

Checksum: DB666F47B5422E7E
Show »

FASTA37241,089

References

« Hide 'large scale' references
[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(1991) [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 (APR-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(2003) [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. expand/collapse author list , 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(2005) [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(1999) [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(2001) [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(2002) [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(2006) [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(2006) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEGRADATION, SUBCELLULAR LOCATION.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [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.
[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(2009) [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(2009) [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(2009) [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(2010) [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(2010) [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]"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].
[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(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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), LACK OF CATALYTIC ACTIVITY, RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
[22]Erratum
Liu Q., Greimann J.C., Lima C.D.
Cell 131:188-189(2007)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG01425.
RefSeqNP_001029366.1. NM_001034194.1.
NP_005024.2. NM_005033.2.
UniGeneHs.91728.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35A1-302[»]
ProteinModelPortalQ06265.
SMRQ06265. Positions 2-278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111402. 18 interactions.
IntActQ06265. 14 interactions.
MINTMINT-1036055.
STRING9606.ENSP00000368984.

PTM databases

PhosphoSiteQ06265.

Polymorphism databases

DMDM147744559.

Proteomic databases

PaxDbQ06265.
PRIDEQ06265.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243498; ENSP00000243498; ENSG00000123737. [Q06265-1]
ENST00000379663; ENSP00000368984; ENSG00000123737. [Q06265-2]
GeneID5393.
KEGGhsa:5393.
UCSCuc003idz.3. human. [Q06265-2]
uc003iea.3. human. [Q06265-1]

Organism-specific databases

CTD5393.
GeneCardsGC04P122722.
HGNCHGNC:9137. EXOSC9.
HPAHPA041838.
HPA048257.
MIM606180. gene.
neXtProtNX_Q06265.
PharmGKBPA33463.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2123.
HOGENOMHOG000229504.
HOVERGENHBG051523.
KOK03678.
OMADYRNIRI.
OrthoDBEOG7X9G70.
PhylomeDBQ06265.
TreeFamTF300092.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ06265.
BgeeQ06265.
CleanExHS_EXOSC9.
GenevestigatorQ06265.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ06265.
GeneWikiExosome_component_9.
GenomeRNAi5393.
NextBio20906.
PROQ06265.
SOURCESearch...

Entry information

Entry nameEXOS9_HUMAN
AccessionPrimary (citable) accession number: Q06265
Secondary accession number(s): Q12883 expand/collapse secondary AC list , Q4W5P5, Q86Y41, Q86Y48
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM