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Reviewed, UniProtKB/Swiss-Prot Q06265 (EXOS9_HUMAN)

Last modified July 7, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Exosome complex exonuclease RRP45
    EC=3.1.13.-
Alternative name(s):
    Exosome component 9
    Polymyositis/scleroderma autoantigen 1
    Autoantigen PM/Scl 1
    Polymyositis/scleroderma autoantigen 75 kDa
      Short name=PM/Scl-75
    P75 polymyositis-scleroderma overlap syndrome-associated autoantigen
Gene names
Name: EXOSC9
Synonyms: PMSCL1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the exosome 3'->5' exoribonuclease complex, a complex that degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3'-untranslated regions. Required for the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA. Has a 3'-5' exonuclease activity By similarity.

Subunit structure

Component of the exosome multienzyme ribonuclease complex composed of at least 11 proteins: EXOSC1/CSL4, EXOSC2/RRP4, EXOSC3/RRP40, EXOSC4/RRP41, EXOSC5/RRP46, EXOSC6/MTR3, EXOSC7/RRP42, EXOSC8/RRP43, EXOSC9/Scl-75, DIS3/RRP44, and EXOSC10/Scl-100 (only in the nuclear complex). Also associated with the GTPase Ran By similarity.

Subcellular location

Cytoplasm. Nucleusnucleolus.

Involvement in disease

Recognized by patients with polymyositis and scleroderma or with overlap of these two conditions.

Sequence similarities

Belongs to the RNase PH family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandRNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processimmune response

Non-traceable author statement. Source: UniProtKB

rRNA processing

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear exosome (RNase complex)

Non-traceable author statement. Source: UniProtKB

nucleolus Ref.1

Traceable author statement. Source: ProtInc

   Molecular function3'-5'-exoribonuclease activity

Non-traceable author statement. Source: UniProtKB

RNA binding

Non-traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BAT1Q138381EBI-347966,EBI-348622
EXOSC4Q9NPD31EBI-347966,EBI-371823

Alternative products

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

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: Q06265-2)

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

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

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 exonuclease RRP45
PRO_0000139971

Amino acid modifications

Modified residue3061Phosphoserine Ref.7
Modified residue3921Phosphoserine Ref.7 Ref.6
Modified residue3941Phosphoserine Ref.7 Ref.6

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: dbSNP rs1803183.
VAR_051867
Natural variant4251S → T: dbSNP rs1051881.
VAR_014924

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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.

Checksum: 693B31BE41C55545
Show »

FASTA45650,803
Isoform 3.

Checksum: DC37BB31767B6621
Show »

FASTA35539,235
Isoform 4.

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: 2007859] [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: 12788944] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[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: 15815621] [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: 10465791] [Abstract]
Cited for: CHARACTERIZATION.
[6]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-394, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND SER-394, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00029697.
IPI00607722.
IPI00654592.
IPI00845426.
PIRG01425.
RefSeqNP_001029366.1.
NP_005024.2.
UniGeneHs.91728

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35A1-302[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ06265. 2 interactions.

PTM databases

PhosphoSiteQ06265.

Proteomic databases

PRIDEQ06265.

Genome annotation databases

EnsemblENSG00000123737. Homo sapiens. [Contig view]
GeneID5393.
KEGGhsa:5393.
UCSCuc003idz.1. human.
uc003iea.1. human.

Organism-specific databases

GeneCardsGC04P122941.
HGNCHGNC:9137. EXOSC9.
MIM606180. gene.
PharmGKBPA33463.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ06265.
OMAQ06265. MEKAPID.

Gene expression databases

ArrayExpressQ06265.
BgeeQ06265.
CleanExHS_EXOSC9.
GermOnlineENSG00000123737. Homo sapiens.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20906.
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: July 7, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents