Exosome complex exonuclease RRP45 - Homo sapiens (Human)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Nucleus › nucleolus.
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.

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Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	immune response Non-traceable author statement. Source: UniProtKB rRNA processing Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm 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 function	3'-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...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT1	Q13838	1	EBI-347966,EBI-348622
EXOSC4	Q9NPD3	1	EBI-347966,EBI-371823

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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

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 439

439

Exosome complex exonuclease RRP45

PRO_0000139971

Amino acid modifications

Modified residue

306

1

Phosphoserine Ref.7

Modified residue

392

1

Phosphoserine Ref.7 Ref.6

Modified residue

394

1

Phosphoserine Ref.7 Ref.6

Natural variations

Alternative sequence

1 – 84

84

Missing in isoform 3 and isoform 4.

VSP_025555

Alternative sequence

385

1

Q → QELGFHHVGQTGLEFLTS in isoform 2 and isoform 4.

VSP_025556

Natural variant

366

1

I → V: dbSNP rs1803183.

VAR_051867

Natural variant

425

1

S → T: dbSNP rs1051881.

VAR_014924

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 15, 2007. Version 3. Checksum: 7E27322F094ED3F3 Show »	FASTA	439	48,949
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 »	FASTA	456	50,803
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 DIGSQELGFH HVGQTGLEFL TSDAPIILSD SEEEEMIILE 430 440 450 PDKNPKKIRT QTTSAKQEKA PSKKPVKRRK KKRAAN « Hide
Isoform 3. Checksum: DC37BB31767B6621 Show »	FASTA	355	39,235
10 20 30 40 50 60 MAAPAFEPGR QSDLLVKLNR LMERCLRNSK CIDTESLCVV AGEKVWQIRV DLHLLNHDGN 70 80 90 100 110 120 IIDAASIAAI VALCHFRRPD VSVQGDEVTL YTPEERDPVP LSIHHMPICV SFAFFQQGTY 130 140 150 160 170 180 LLVDPNEREE RVMDGLLVIA MNKHREICTI QSSGGIMLLK DQVLRCSKIA GVKVAEITEL 190 200 210 220 230 240 ILKALENDQK VRKEGGKFGF AESIANQRIT AFKMEKAPID TSDVEEKAEE IIAEAEPPSE 250 260 270 280 290 300 VVSTPVLWTP GTAQIGEGVE NSWGDLEDSE KEDDEGGGDQ AIILDGIKMD TGVEVSDIGS 310 320 330 340 350 QDAPIILSDS EEEEMIILEP DKNPKKIRTQ TTSAKQEKAP SKKPVKRRKK KRAAN « Hide
Isoform 4. Checksum: DB666F47B5422E7E Show »	FASTA	372	41,089
10 20 30 40 50 60 MAAPAFEPGR QSDLLVKLNR LMERCLRNSK CIDTESLCVV AGEKVWQIRV DLHLLNHDGN 70 80 90 100 110 120 IIDAASIAAI VALCHFRRPD VSVQGDEVTL YTPEERDPVP LSIHHMPICV SFAFFQQGTY 130 140 150 160 170 180 LLVDPNEREE RVMDGLLVIA MNKHREICTI QSSGGIMLLK DQVLRCSKIA GVKVAEITEL 190 200 210 220 230 240 ILKALENDQK VRKEGGKFGF AESIANQRIT AFKMEKAPID TSDVEEKAEE IIAEAEPPSE 250 260 270 280 290 300 VVSTPVLWTP GTAQIGEGVE NSWGDLEDSE KEDDEGGGDQ AIILDGIKMD TGVEVSDIGS 310 320 330 340 350 360 QELGFHHVGQ TGLEFLTSDA PIILSDSEEE EMIILEPDKN PKKIRTQTTS AKQEKAPSKK 370 PVKRRKKKRA AN « Hide

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References

	« Hide 'large scale' referencesShow '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. 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.

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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.

IPI

IPI00029697.
IPI00607722.
IPI00654592.
IPI00845426.

PIR

G01425.

RefSeq

NP_001029366.1.
NP_005024.2.

UniGene

Hs.91728

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NN6	X-ray	3.35	A	1-302	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q06265. 2 interactions.

PTM databases

PhosphoSite

Q06265.

Proteomic databases

PRIDE

Q06265.

Genome annotation databases

Ensembl

ENSG00000123737. Homo sapiens. [Contig view]

GeneID

5393.

KEGG

hsa:5393.

UCSC

uc003idz.1. human.
uc003iea.1. human.

Organism-specific databases

GeneCards

GC04P122941.

HGNC

HGNC:9137. EXOSC9.

MIM

606180. gene.

PharmGKB

PA33463.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q06265.

OMA

Q06265. MEKAPID.

Gene expression databases

ArrayExpress

Q06265.

Bgee

Q06265.

CleanEx

HS_EXOSC9.

GermOnline

ENSG00000123737. Homo sapiens.

Family and domain databases

InterPro

IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
[Graphical view]

Pfam

PF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

20906.

SOURCE

Search...

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Entry information

Entry name

EXOS9_HUMAN

Accession

Primary (citable) accession number: Q06265
Secondary accession number(s): Q12883

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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents