Q06265 (EXOS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15
Subcellular location	Cytoplasm. Nucleus › nucleolus Ref.3 Ref.11. Isoform 1: Nucleus › nucleolus Ref.3 Ref.11. Isoform 2: Nucleus › nucleolus 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 process	rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Inferred from mutant phenotype Ref.7. Source: UniProtKB immune response Non-traceable author statement PubMed 11879549. Source: UniProtKB 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 positive regulation of cell growth Inferred from mutant phenotype Ref.11. Source: UniProtKB rRNA processing Non-traceable author statement PubMed 11879549. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear exosome (RNase complex) Inferred from direct assay PubMed 22791713. Source: UniProtKB nucleolus Inferred from direct assay PubMed 22791713PubMed 22791713. Source: UniProtKB nucleus Inferred from direct assay PubMed 22791713. Source: UniProtKB
Molecular_function	3'-5'-exoribonuclease activity Non-traceable author statement PubMed 11879549. Source: UniProtKB AU-rich element binding Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 439

439

Exosome complex component RRP45

PRO_0000139971

Regions

Region

1 – 268

268

ARE binding

Amino acid modifications

Modified residue

297

1

N6-acetyllysine Ref.14

Modified residue

306

1

Phosphoserine Ref.12 Ref.13 Ref.16 Ref.18

Modified residue

392

1

Phosphoserine Ref.12 Ref.16

Modified residue

394

1

Phosphoserine Ref.12 Ref.16

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.
Corresponds to variant rs1803183 [ dbSNP | Ensembl ].

VAR_051867

Natural variant

425

1

S → T.
Corresponds to variant rs1051881 [ dbSNP | Ensembl ].

VAR_014924

Secondary structure

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439

Helix Strand Turn

Details...

Helix

8 – 19

12

Beta strand

36 – 39

4

Beta strand

45 – 52

8

Beta strand

54 – 59

6

Beta strand

62 – 64

3

Turn

69 – 72

4

Beta strand

76 – 82

7

Turn

84 – 86

3

Beta strand

92 – 94

3

Helix

96 – 99

4

Helix

101 – 113

13

Beta strand

118 – 121

4

Turn

125 – 127

3

Beta strand

128 – 138

11

Helix

146 – 159

14

Helix

176 – 179

4

Beta strand

191 – 198

8

Turn

200 – 202

3

Beta strand

203 – 208

6

Helix

211 – 216

6

Beta strand

220 – 226

7

Turn

227 – 229

3

Beta strand

230 – 238

9

Helix

244 – 277

34

Helix

287 – 290

4

Beta strand

291 – 298

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PM/SCL-75c-alpha) [UniParc]. Last modified May 15, 2007. Version 3. Checksum: 7E27322F094ED3F3	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
	Isoform 2 (PM/SCL-75c-beta) [UniParc]. Checksum: 693B31BE41C55545	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
	Isoform 3 (PM/SCL-75a-alpha) [UniParc]. Checksum: DC37BB31767B6621	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
	Isoform 4 (PM/SCL-75a-beta) [UniParc]. Checksum: DB666F47B5422E7E	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

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] [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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[15]	"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, MASS SPECTROMETRY.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	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.

IPI

IPI00029697.
IPI00607722.
IPI00654592.
IPI00845426.

PIR

G01425.

RefSeq

NP_001029366.1. NM_001034194.1.
NP_005024.2. NM_005033.2.

UniGene

Hs.91728.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q06265.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q06265. 11 interactions.

MINT

MINT-1036055.

STRING

9606.ENSP00000368984.

PTM databases

PhosphoSite

Q06265.

Polymorphism databases

DMDM

147744559.

Proteomic databases

PaxDb

Q06265.

PRIDE

Q06265.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000243498; ENSP00000243498; ENSG00000123737.
ENST00000379663; ENSP00000368984; ENSG00000123737.

GeneID

5393.

KEGG

hsa:5393.

UCSC

uc003idz.3. human.
uc003iea.3. human.

Organism-specific databases

CTD

5393.

GeneCards

GC04P122722.

HGNC

HGNC:9137. EXOSC9.

HPA

HPA041838.

MIM

606180. gene.

neXtProt

NX_Q06265.

PharmGKB

PA33463.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2123.

HOGENOM

HOG000229504.

HOVERGEN

HBG051523.

KO

K03678.

OMA

YRNIRIS.

OrthoDB

EOG43TZVZ.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q06265.

Bgee

Q06265.

CleanEx

HS_EXOSC9.

Genevestigator

Q06265.

GermOnline

ENSG00000123737. Homo sapiens.

Family and domain databases

InterPro

IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]

Pfam

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

SUPFAM

SSF55666. 3_ExoRNase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q06265.

GenomeRNAi

5393.

NextBio

20906.

SOURCE

Search...

Entry information

Entry name

EXOS9_HUMAN

Accession

Primary (citable) accession number: Q06265
Secondary accession number(s): Q12883 , Q4W5P5, Q86Y41, Q86Y48

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	May 15, 2007
Last modified:	May 1, 2013
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.