Q01780 (EXOSX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	885 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19
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. Ref.10 Ref.12 Ref.17
Subcellular location	Cytoplasm. Nucleus › nucleolus. 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.12 Ref.13 Ref.16
Sequence similarities	Contains 1 3'-5' exonuclease domain. Contains 1 HRDC domain.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay rRNA processing
Cellular component	Cytoplasm Exosome Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CUT catabolic process Inferred from mutant phenotype Ref.15. Source: UniProtKB dosage compensation by inactivation of X chromosome Inferred from electronic annotation. Source: Compara histone mRNA catabolic process Inferred from mutant phenotype Ref.14. Source: UniProtKB maturation of 5.8S rRNA Inferred from mutant phenotype Ref.12Ref.19. 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.18. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype PubMed 22890540. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.13Ref.16. Source: UniProtKB exosome (RNase complex) Inferred from direct assay Ref.17. Source: UniProtKB nuclear exosome (RNase complex) Inferred from electronic annotation. Source: InterPro nucleolus Inferred from direct assay Ref.16. Source: UniProtKB transcriptionally active chromatin Inferred from mutant phenotype Ref.18. Source: UniProtKB
Molecular_function	3'-5' exonuclease activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW exoribonuclease activity Inferred from direct assay PubMed 17174896. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C1D	Q13901	5	EBI-358236,EBI-3844053
MPHOSPH6	Q99547	4	EBI-358236,EBI-373187

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 885

885

Exosome component 10

PRO_0000087133

Regions

Domain

503 – 583

81

HRDC

Natural variations

Alternative sequence

695 – 719

25

Missing in isoform 2.

VSP_004362

Secondary structure

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885

Helix Strand Turn

Details...

Helix

183 – 186

4

Beta strand

194 – 196

3

Helix

214 – 216

3

Helix

218 – 220

3

Beta strand

253 – 255

3

Helix

259 – 263

5

Helix

269 – 272

4

Helix

283 – 285

3

Beta strand

288 – 291

4

Helix

294 – 304

11

Beta strand

308 – 317

10

Beta strand

325 – 332

8

Beta strand

337 – 341

5

Turn

342 – 345

4

Helix

346 – 352

7

Helix

353 – 356

4

Beta strand

361 – 367

7

Helix

369 – 379

11

Beta strand

384 – 388

5

Helix

389 – 395

7

Helix

403 – 411

9

Turn

418 – 421

4

Helix

431 – 442

12

Helix

444 – 458

15

Beta strand

461 – 463

3

Helix

464 – 476

13

Helix

490 – 492

3

Helix

493 – 496

4

Beta strand

497 – 500

4

Helix

504 – 524

21

Helix

528 – 531

4

Helix

534 – 543

10

Helix

548 – 552

5

Beta strand

555 – 557

3

Helix

560 – 564

5

Helix

566 – 577

12

Helix

583 – 586

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: A37BDC8F49BF2E57	FASTA	885	100,831
	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
	Isoform 2 [UniParc]. Checksum: B7FBE8B15F28BFE2	FASTA	860	98,089
	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 PFRMISNRWK LAQVQVQKDS KEAVKKKAAE 730 740 750 760 770 780 QTAAREQAKE ACKAAAEQAI SVRQQVVLEN AAKKRERATS DPRTTEQKQE KKRLKISKKP 790 800 810 820 830 840 KDPEPPEKEF TPYDYSQSDF KAFAGNSKSK VSSQFDPNKQ TPSGKKCIAA KKIKQSVGNK 850 860 SMSFPTGKSD RGFRYNWPQR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: IDENTIFICATION BY MASS SPECTROMETRY, 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]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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].
[21]	"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.

IPI

IPI00009464.
IPI00220336.

PIR

A43920.
JH0796.

RefSeq

NP_001001998.1. NM_001001998.1.
NP_002676.1. NM_002685.2.

UniGene

Hs.632368.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CPR	NMR	-	A	483-593	[»]
3SAF	X-ray	2.50	A/B	180-606	[»]
3SAG	X-ray	2.70	A/B	180-606	[»]
3SAH	X-ray	2.65	A/B	180-606	[»]

ProteinModelPortal

Q01780.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01780. 42 interactions.

MINT

MINT-1143843.

STRING

9606.ENSP00000366135.

PTM databases

PhosphoSite

Q01780.

Polymorphism databases

DMDM

8928564.

2D gel databases

SWISS-2DPAGE

Q01780.

Proteomic databases

PaxDb

Q01780.

PRIDE

Q01780.

Protocols and materials databases

DNASU

5394.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304457; ENSP00000307307; ENSG00000171824.
ENST00000376936; ENSP00000366135; ENSG00000171824.

GeneID

5394.

KEGG

hsa:5394.

UCSC

uc001asa.3. human.
uc001asb.3. human.

Organism-specific databases

CTD

5394.

GeneCards

GC01M011126.

HGNC

HGNC:9138. EXOSC10.

HPA

HPA028470.
HPA028484.

MIM

605960. gene.

neXtProt

NX_Q01780.

PharmGKB

PA33464.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0349.

HOGENOM

HOG000001579.

HOVERGEN

HBG051524.

InParanoid

Q01780.

KO

K12591.

OMA

GNKSMSF.

OrthoDB

EOG4X6C7P.

PhylomeDB

Q01780.

Gene expression databases

ArrayExpress

Q01780.

Bgee

Q01780.

CleanEx

HS_EXOSC10.

Genevestigator

Q01780.

GermOnline

ENSG00000171824. Homo sapiens.

Family and domain databases

InterPro

IPR002562. 3'-5'_exonuclease_dom.
IPR012588. Exosome-assoc_fac_Rrp6_N.
IPR010997. HRDC-like.
IPR002121. HRDC_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]

Pfam

PF01612. DNA_pol_A_exo1. 1 hit.
PF00570. HRDC. 1 hit.
PF08066. PMC2NT. 1 hit.
[Graphical view]

SMART

SM00474. 35EXOc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]

SUPFAM

SSF47819. HRDC_like. 1 hit.
SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50967. HRDC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

EXOSC10. human.

EvolutionaryTrace

Q01780.

GenomeRNAi

5394.

NextBio

20912.

SOURCE

Search...

Entry information

Entry name

EXOSX_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 2 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.