Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Exosome component 10 (EC 3.1.13.-) (Autoantigen PM/Scl 2) (P100 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 100 kDa) (PM/Scl-100) (Polymyositis/scleroderma autoantigen 2)

 EXOSX_HUMAN             Reviewed;         885 AA.
Q01780; B1AKQ0; B1AKQ1; Q15158;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
10-OCT-2018, entry version 198.
RecName: Full=Exosome component 10 {ECO:0000305};
EC=3.1.13.-;
AltName: Full=Autoantigen PM/Scl 2;
AltName: Full=P100 polymyositis-scleroderma overlap syndrome-associated autoantigen;
AltName: Full=Polymyositis/scleroderma autoantigen 100 kDa;
Short=PM/Scl-100;
AltName: Full=Polymyositis/scleroderma autoantigen 2;
Name=EXOSC10 {ECO:0000312|HGNC:HGNC:9138};
Synonyms=PMSCL, PMSCL2, RRP6 {ECO:0000303|PubMed:26166824};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1383382; DOI=10.1084/jem.176.4.973;
Bluethner M., Bautz F.A.;
"Cloning and characterization of the cDNA coding for a polymyositis-
scleroderma overlap syndrome-related nucleolar 100-kD protein.";
J. Exp. Med. 176:973-980(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Thymocyte;
PubMed=1644924; DOI=10.1172/JCI115895;
Ge Q., Frank M.B., O'Brien C., Targoff I.N.;
"Cloning of a complementary DNA coding for the 100-kD antigenic
protein of the PM-Scl autoantigen.";
J. Clin. Invest. 90:559-570(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=11426320; DOI=10.1038/sj.gene.6363745;
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.;
"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.";
Genes Immun. 2:119-127(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION.
PubMed=10465791; DOI=10.1101/gad.13.16.2148;
Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
Mitchell P.;
"The yeast exosome and human PM-Scl are related complexes of 3'-->5'
exonucleases.";
Genes Dev. 13:2148-2158(1999).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[9]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND SUBCELLULAR LOCATION.
PubMed=14527413; DOI=10.1016/S1097-2765(03)00349-6;
Lejeune F., Li X., Maquat L.E.;
"Nonsense-mediated mRNA decay in mammalian cells involves decapping,
deadenylating, and exonucleolytic activities.";
Mol. Cell 12:675-687(2003).
[10]
PROTEIN INTERACTION.
PubMed=15231747; DOI=10.1101/gr.2122004;
Lehner B., Sanderson C.M.;
"A protein interaction framework for human mRNA degradation.";
Genome Res. 14:1315-1323(2004).
[11]
INTERACTION WITH DHX36.
PubMed=14731398; DOI=10.1016/S1097-2765(03)00481-7;
Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
"Facilitation of mRNA deadenylation and decay by the exosome-bound,
DExH protein RHAU.";
Mol. Cell 13:101-111(2004).
[12]
FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
PubMed=16455498; DOI=10.1016/j.molcel.2005.12.008;
West S., Gromak N., Norbury C.J., Proudfoot N.J.;
"Adenylation and exosome-mediated degradation of cotranscriptionally
cleaved pre-messenger RNA in human cells.";
Mol. Cell 21:437-443(2006).
[13]
INTERACTION WITH ALYREF.
PubMed=17234882; DOI=10.1101/gad.1503107;
Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.;
"The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA
splicing and export.";
Genes Dev. 21:160-174(2007).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1D AND MPHOSPH6.
PubMed=17412707; DOI=10.1093/nar/gkm082;
Schilders G., van Dijk E., Pruijn G.J.M.;
"C1D and hMtr4p associate with the human exosome subunit PM/Scl-100
and are involved in pre-rRNA processing.";
Nucleic Acids Res. 35:2564-2572(2007).
[15]
FUNCTION IN MRNA DEGRADATION, AND SUBCELLULAR LOCATION.
PubMed=17545563; DOI=10.1261/rna.575107;
van Dijk E.L., Schilders G., Pruijn G.J.;
"Human cell growth requires a functional cytoplasmic exosome, which is
involved in various mRNA decay pathways.";
RNA 13:1027-1035(2007).
[16]
FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[17]
FUNCTION IN PROMPT DEGRADATION.
PubMed=19056938; DOI=10.1126/science.1164096;
Preker P., Nielsen J., Kammler S., Lykke-Andersen S.,
Christensen M.S., Mapendano C.K., Schierup M.H., Jensen T.H.;
"RNA exosome depletion reveals transcription upstream of active human
promoters.";
Science 322:1851-1854(2008).
[18]
ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=20531386; DOI=10.1038/emboj.2010.121;
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.;
"The human core exosome interacts with differentially localized
processive RNases: hDIS3 and hDIS3L.";
EMBO J. 29:2342-2357(2010).
[19]
IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20531389; DOI=10.1038/emboj.2010.122;
Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
Heck A.J., Raijmakers R., Pruijn G.J.;
"Dis3-like 1: a novel exoribonuclease associated with the human
exosome.";
EMBO J. 29:2358-2367(2010).
[20]
FUNCTION IN NUCLEAR MRNA SURVEILLANCE.
PubMed=20699273; DOI=10.1093/nar/gkq703;
de Almeida S.F., Garcia-Sacristan A., Custodio N., Carmo-Fonseca M.;
"A link between nuclear RNA surveillance, the human exosome and RNA
polymerase II transcriptional termination.";
Nucleic Acids Res. 38:8015-8026(2010).
[21]
FUNCTION IN RRNA MATURATION.
PubMed=20368444; DOI=10.1073/pnas.0910621107;
Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.;
"Addition of poly(A) and poly(A)-rich tails during RNA degradation in
the cytoplasm of human cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[26]
IDENTIFICATION IN THE RNA EXOSOME COMPLEX.
PubMed=26166824; DOI=10.1016/j.bbrc.2015.07.032;
Yoshikatsu Y., Ishida Y., Sudo H., Yuasa K., Tsuji A., Nagahama M.;
"NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome
and is involved in pre-rRNA processing.";
Biochem. Biophys. Res. Commun. 464:780-786(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19; LYS-583; LYS-710;
LYS-826; LYS-833; LYS-859 AND LYS-873, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[29]
STRUCTURE BY NMR OF 483-593.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the HRDC domain of human exosome component
10.";
Submitted (NOV-2005) to the PDB data bank.
-!- 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 MTREX, C1D and MPP6 wth the RNA exosome
involved in the maturation of 5.8S rRNA. {ECO:0000250,
ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498,
ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563,
ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938,
ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273}.
-!- SUBUNIT: Component of the RNA exosome complex (PubMed:20531389,
PubMed:26166824). 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 (PubMed:20531389). Interacts with C1D
and MPHOSPH6 (PubMed:17412707). Interacts with ALYREF/THOC4
(PubMed:17234882). Interacts with MTREX; the interaction mediates
the association of MTREX with nuclear RNA exosomes
(PubMed:26166824). Interacts with DHX36; this interaction occurs
in a RNase-insensitive manner (PubMed:14731398).
{ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:17234882,
ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:20531389,
ECO:0000269|PubMed:26166824}.
-!- INTERACTION:
Q13901:C1D; NbExp=5; IntAct=EBI-358236, EBI-3844053;
P17844:DDX5; NbExp=3; IntAct=EBI-358236, EBI-351962;
Q9Y2L1:DIS3; NbExp=4; IntAct=EBI-358236, EBI-373539;
Q9NPD3:EXOSC4; NbExp=4; IntAct=EBI-358236, EBI-371823;
Q9NQT4:EXOSC5; NbExp=3; IntAct=EBI-358236, EBI-371876;
Q99547:MPHOSPH6; NbExp=4; IntAct=EBI-358236, EBI-373187;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q01780-1; Sequence=Displayed;
Name=2;
IsoId=Q01780-2; Sequence=VSP_004362;
Note=No experimental confirmation available.;
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X66113; CAA46904.1; -; mRNA.
EMBL; L01457; AAB59352.1; -; mRNA.
EMBL; AJ300188; CAC15569.1; -; Genomic_DNA.
EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471130; EAW71679.1; -; Genomic_DNA.
EMBL; BC039901; AAH39901.1; -; mRNA.
EMBL; BC073788; AAH73788.1; -; mRNA.
CCDS; CCDS126.1; -. [Q01780-2]
CCDS; CCDS30584.1; -. [Q01780-1]
PIR; A43920; A43920.
PIR; JH0796; JH0796.
RefSeq; NP_001001998.1; NM_001001998.2. [Q01780-1]
RefSeq; NP_002676.1; NM_002685.3. [Q01780-2]
UniGene; Hs.632368; -.
PDB; 2CPR; NMR; -; A=483-593.
PDB; 3SAF; X-ray; 2.50 A; A/B=180-606.
PDB; 3SAG; X-ray; 2.70 A; A/B=180-606.
PDB; 3SAH; X-ray; 2.65 A; A/B=180-606.
PDB; 6D6Q; EM; 3.45 A; J=1-648, J=705-804.
PDB; 6D6R; EM; 3.45 A; J=1-648, J=705-804.
PDBsum; 2CPR; -.
PDBsum; 3SAF; -.
PDBsum; 3SAG; -.
PDBsum; 3SAH; -.
PDBsum; 6D6Q; -.
PDBsum; 6D6R; -.
ProteinModelPortal; Q01780; -.
SMR; Q01780; -.
BioGrid; 111403; 79.
ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant.
ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
CORUM; Q01780; -.
DIP; DIP-31249N; -.
IntAct; Q01780; 60.
MINT; Q01780; -.
STRING; 9606.ENSP00000366135; -.
iPTMnet; Q01780; -.
PhosphoSitePlus; Q01780; -.
SwissPalm; Q01780; -.
BioMuta; EXOSC10; -.
DMDM; 8928564; -.
SWISS-2DPAGE; Q01780; -.
EPD; Q01780; -.
MaxQB; Q01780; -.
PaxDb; Q01780; -.
PeptideAtlas; Q01780; -.
PRIDE; Q01780; -.
ProteomicsDB; 57986; -.
ProteomicsDB; 57987; -. [Q01780-2]
DNASU; 5394; -.
Ensembl; ENST00000304457; ENSP00000307307; ENSG00000171824. [Q01780-2]
Ensembl; ENST00000376936; ENSP00000366135; ENSG00000171824. [Q01780-1]
GeneID; 5394; -.
KEGG; hsa:5394; -.
UCSC; uc001asa.4; human. [Q01780-1]
CTD; 5394; -.
DisGeNET; 5394; -.
EuPathDB; HostDB:ENSG00000171824.13; -.
GeneCards; EXOSC10; -.
HGNC; HGNC:9138; EXOSC10.
HPA; CAB037141; -.
HPA; HPA028470; -.
HPA; HPA028484; -.
MIM; 605960; gene.
neXtProt; NX_Q01780; -.
OpenTargets; ENSG00000171824; -.
PharmGKB; PA33464; -.
eggNOG; KOG2206; Eukaryota.
eggNOG; COG0349; LUCA.
GeneTree; ENSGT00390000015408; -.
HOGENOM; HOG000001579; -.
HOVERGEN; HBG051524; -.
InParanoid; Q01780; -.
KO; K12591; -.
OMA; GNKSMSF; -.
OrthoDB; EOG091G03BH; -.
PhylomeDB; Q01780; -.
TreeFam; TF105991; -.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; EXOSC10; human.
EvolutionaryTrace; Q01780; -.
GeneWiki; Exosome_component_10; -.
GenomeRNAi; 5394; -.
PRO; PR:Q01780; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000171824; Expressed in 229 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_EXOSC10; -.
ExpressionAtlas; Q01780; baseline and differential.
Genevisible; Q01780; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; IMP:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:BHF-UCL.
GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:UniProtKB.
GO; GO:0071048; P:nuclear retention of unspliced pre-mRNA at the site of transcription; IMP:UniProtKB.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
InterPro; IPR010997; HRDC-like_sf.
InterPro; IPR002121; HRDC_dom.
InterPro; IPR012337; RNaseH-like_sf.
Pfam; PF01612; DNA_pol_A_exo1; 1.
Pfam; PF00570; HRDC; 1.
Pfam; PF08066; PMC2NT; 1.
SMART; SM00474; 35EXOc; 1.
SMART; SM00341; HRDC; 1.
SUPFAM; SSF47819; SSF47819; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50967; HRDC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Exonuclease; Exosome; Hydrolase; Isopeptide bond;
Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
CHAIN 1 885 Exosome component 10.
/FTId=PRO_0000087133.
DOMAIN 503 583 HRDC. {ECO:0000255|PROSITE-
ProRule:PRU00328}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 710 710 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 826 826 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 833 833 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 859 859 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 873 873 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 695 719 Missing (in isoform 2).
{ECO:0000303|PubMed:1644924}.
/FTId=VSP_004362.
HELIX 183 186 {ECO:0000244|PDB:3SAF}.
STRAND 194 196 {ECO:0000244|PDB:3SAF}.
HELIX 214 216 {ECO:0000244|PDB:3SAF}.
HELIX 218 220 {ECO:0000244|PDB:3SAF}.
STRAND 253 255 {ECO:0000244|PDB:3SAF}.
HELIX 259 263 {ECO:0000244|PDB:3SAF}.
HELIX 269 272 {ECO:0000244|PDB:3SAF}.
HELIX 283 285 {ECO:0000244|PDB:3SAF}.
STRAND 288 291 {ECO:0000244|PDB:3SAF}.
HELIX 294 304 {ECO:0000244|PDB:3SAF}.
STRAND 308 317 {ECO:0000244|PDB:3SAF}.
STRAND 325 332 {ECO:0000244|PDB:3SAF}.
STRAND 337 341 {ECO:0000244|PDB:3SAF}.
TURN 342 345 {ECO:0000244|PDB:3SAF}.
HELIX 346 352 {ECO:0000244|PDB:3SAF}.
HELIX 353 356 {ECO:0000244|PDB:3SAF}.
STRAND 361 367 {ECO:0000244|PDB:3SAF}.
HELIX 369 379 {ECO:0000244|PDB:3SAF}.
STRAND 384 388 {ECO:0000244|PDB:3SAF}.
HELIX 389 395 {ECO:0000244|PDB:3SAF}.
HELIX 403 411 {ECO:0000244|PDB:3SAF}.
TURN 418 421 {ECO:0000244|PDB:3SAF}.
HELIX 431 442 {ECO:0000244|PDB:3SAF}.
HELIX 444 458 {ECO:0000244|PDB:3SAF}.
STRAND 461 463 {ECO:0000244|PDB:3SAH}.
HELIX 464 476 {ECO:0000244|PDB:3SAF}.
HELIX 490 492 {ECO:0000244|PDB:3SAF}.
HELIX 493 496 {ECO:0000244|PDB:3SAF}.
STRAND 497 500 {ECO:0000244|PDB:2CPR}.
HELIX 504 524 {ECO:0000244|PDB:3SAF}.
HELIX 528 531 {ECO:0000244|PDB:3SAF}.
HELIX 534 543 {ECO:0000244|PDB:3SAF}.
HELIX 548 552 {ECO:0000244|PDB:3SAF}.
STRAND 555 557 {ECO:0000244|PDB:3SAH}.
HELIX 560 564 {ECO:0000244|PDB:3SAF}.
HELIX 566 577 {ECO:0000244|PDB:3SAF}.
HELIX 583 586 {ECO:0000244|PDB:3SAF}.
SEQUENCE 885 AA; 100831 MW; A37BDC8F49BF2E57 CRC64;
MAPPSTREPR VLSATSATKS DGEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY
DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDANDVI
LERVGILLDE ASGVNKNQQP VLPAGLQVPK TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI
IRPQLKFREK IDNSNTPFLP KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF
IHQQRTQQVE QDMFAHPYQY ELNHFTPADA VLQKPQPQLY RPIEETPCHF ISSLDELVEL
NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY ILNESLTDPA
IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR HSLDHLLKLY CNVDSNKQYQ
LADWRIRPLP EEMLSYARDD THYLLYIYDK MRLEMWERGN GQPVQLQVVW QRSRDICLKK
FIKPIFTDES YLELYRKQKK HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI
AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE
RLENVLFGPH DCSHAPPDGY PIIPTSGSVP VQKQASLFPD EKEDNLLGTT CLIATAVITL
FNEPSAEDSK KGPLTVAQKK AQNIMESFEN PFRMFLPSLG HRAPVSQAAK FDPSTKIYEI
SNRWKLAQVQ VQKDSKEAVK KKAAEQTAAR EQAKEACKAA AEQAISVRQQ VVLENAAKKR
ERATSDPRTT EQKQEKKRLK ISKKPKDPEP PEKEFTPYDY SQSDFKAFAG NSKSKVSSQF
DPNKQTPSGK KCIAAKKIKQ SVGNKSMSFP TGKSDRGFRY NWPQR


Related products :

Catalog number Product name Quantity
EIAAB13506 Autoantigen PM_Scl 2,EXOSC10,Exosome component 10,Homo sapiens,Human,P100 polymyositis-scleroderma overlap syndrome-associated autoantigen,PM_Scl-100,PMSCL,PMSCL2,Polymyositis_scleroderma autoantigen
18-003-43549 Exosome component 10 - Polymyositis_scleroderma autoantigen 2; Autoantigen PM_Scl 2; Polymyositis_scleroderma autoantigen 100 kDa; PM_Scl-100; P100 polymyositis-scleroderma overlap syndrome-associated 0.1 mg Protein A
EIAAB13502 Autoantigen PM_Scl 1,Exosc9,Exosome complex component RRP45,Exosome component 9,Mouse,Mus musculus,P75 polymyositis-scleroderma overlap syndrome-associated autoantigen,PM_Scl-75,Pmscl1,Polymyositis_sc
EIAAB13503 Autoantigen PM_Scl 1,EXOSC9,Exosome complex component RRP45,Exosome component 9,Homo sapiens,Human,P75 polymyositis-scleroderma overlap syndrome-associated autoantigen,PM_Scl-75,PMSCL1,Polymyositis_sc
E0731h Human ELISA Kit FOR Sjoegren syndrome per scleroderma autoantigen 1 96T
TIPIN_BOVIN Human ELISA Kit FOR Sjoegren syndrome per scleroderma autoantigen 1 96T
H1041 Sjoegren syndrome scleroderma autoantigen 1 (SSSCA1), Human, ELISA Kit 96T
H1042 Sjoegren syndrome scleroderma autoantigen 1 (SSSCA1), Mouse, ELISA Kit 96T
SSA27_MOUSE ELISA Kit FOR Sjoegren syndrome per scleroderma autoantigen 1 homolog; organism: Mouse; gene name: Sssca1 96T
EIAAB13505 Autoantigen PM_Scl 2 homolog,Exosc10,Exosome component 10,Mouse,Mus musculus,Pmscl2,Polymyositis_scleroderma autoantigen 2 homolog
EIAAB44587 Cell surface receptor NYD-SP8,Homo sapiens,Human,Scleroderma-associated autoantigen,SGRG,Spermatogenesis-related gene protein,Testis-expressed protein 101,TEX101,UNQ867_PRO1884
29-224 EXOSC10 contains 1 HRDC domain and 1 3'-5' exonuclease domain. Antibodies against PM_SCL are found in patients with polymyositis and_or scleroderma. 0.1 mg
EIAAB40039 Homo sapiens,Human,NA14,Nuclear autoantigen of 14 kDa,Sjoegren syndrome nuclear autoantigen 1,SSNA1
EIAAB40006 Autoantigen p27,Homo sapiens,Human,Sjoegren syndrome_scleroderma autoantigen 1,SSSCA1
EIAAB40005 Autoantigen p27 homolog,C184l,Mouse,Mus musculus,Protein C184L,Sjoegren syndrome_scleroderma autoantigen 1 homolog,Sssca1
10-663-45671 Ku Protein (P70_P80) Human - EC 3.6.1.-; ATP-dependent DNA helicase II 80 kDa subunit; Lupus Ku autoantigen protein p86; Ku86; Ku80; 86 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA; CTC 0.005 mg
10-663-45671 Ku Protein (P70_P80) Human - EC 3.6.1.-; ATP-dependent DNA helicase II 80 kDa subunit; Lupus Ku autoantigen protein p86; Ku86; Ku80; 86 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA; CTC 1 mg
10-663-45671 Ku Protein (P70_P80) Human - EC 3.6.1.-; ATP-dependent DNA helicase II 80 kDa subunit; Lupus Ku autoantigen protein p86; Ku86; Ku80; 86 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA; CTC 0.02 mg
EIAAB12416 Autoantigen Ge-1,Autoantigen RCD-8,EDC4,Enhancer of mRNA-decapping protein 4,Hedls,HEDLS,Homo sapiens,Human,Human enhancer of decapping large subunit
ARP40462_P050 SSB (Sjogren syndrome antigen B (autoantigen La)) 50 µg
SSB SSB Gene Sjogren syndrome antigen B (autoantigen La)
GWB-104D20 SSB (Sjogren syndrome antigen B (autoantigen La))
E5507h Human Sjogren Syndrome Nuclear Autoantigen 1 ELISA 96T
201-20-5588 SSNA1{Sjogren syndrome nuclear autoantigen 1}rabbit.pAb 0.2ml
18-003-42478 ATP-dependent DNA helicase 2 subunit 1 - EC 3.6.1.-; ATP-dependent DNA helicase II 70 kDa subunit; Lupus Ku autoantigen protein p70; Ku70; 70 kDa subunit of Ku antigen; Thyroid-lupus autoantigen; TLAA 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur