MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Exosome component 10; 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; |
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| MyHits synonyms | EXOSX_HUMAN , Q01780 , B1AKQ0 , B1AKQ1 , Q15158 , A37BDC8F49BF2E57 |
 Legends: 1, Phosphoserine. {ECO:0000244|PubMed:23186163}; 2, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1). {ECO:0000244|PubMed:25114211}; 3, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25218447}; 4, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25772364}; 5, HRDC. {ECO:0000255|PROSITE- ProRule:PRU00328}; 6, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:1644924}; 7, iprf:HRDC [T]; 8, ismart:HRDC [T]; 9, ipfam:HRDC [T]; 10, ipfam:PMC2NT [T]; 11, ipfam:DNA_pol_A_exo1 [T]; 12, HELIX {ECO:0000244|PDB:3SAF}; 13, STRAND {ECO:0000244|PDB:3SAF}; 14, TURN {ECO:0000244|PDB:3SAF}; 15, STRAND {ECO:0000244|PDB:3SAH}; 16, STRAND {ECO:0000244|PDB:2CPR}.
| |
ID EXOSX_HUMAN Reviewed; 885 AA.
AC Q01780; B1AKQ0; B1AKQ1; Q15158;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 02-NOV-2016, entry version 179.
DE RecName: Full=Exosome component 10;
DE EC=3.1.13.-;
DE AltName: Full=Autoantigen PM/Scl 2;
DE AltName: Full=P100 polymyositis-scleroderma overlap syndrome-associated autoantigen;
DE AltName: Full=Polymyositis/scleroderma autoantigen 100 kDa;
DE Short=PM/Scl-100;
DE AltName: Full=Polymyositis/scleroderma autoantigen 2;
GN Name=EXOSC10; Synonyms=PMSCL, PMSCL2, RRP6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1383382; DOI=10.1084/jem.176.4.973;
RA Bluethner M., Bautz F.A.;
RT "Cloning and characterization of the cDNA coding for a polymyositis-
RT scleroderma overlap syndrome-related nucleolar 100-kD protein.";
RL J. Exp. Med. 176:973-980(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Thymocyte;
RX PubMed=1644924; DOI=10.1172/JCI115895;
RA Ge Q., Frank M.B., O'Brien C., Targoff I.N.;
RT "Cloning of a complementary DNA coding for the 100-kD antigenic
RT protein of the PM-Scl autoantigen.";
RL J. Clin. Invest. 90:559-570(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=11426320; DOI=10.1038/sj.gene.6363745;
RA Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C.,
RA Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S.,
RA Fujita T., Schwaeble W.;
RT "The human gene for mannan-binding lectin-associated serine protease-2
RT (MASP-2), the effector component of the lectin route of complement
RT activation, is part of a tightly linked gene cluster on chromosome
RT 1p36.2-3.";
RL Genes Immun. 2:119-127(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10465791; DOI=10.1101/gad.13.16.2148;
RA Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D.,
RA Mitchell P.;
RT "The yeast exosome and human PM-Scl are related complexes of 3'-->5'
RT exonucleases.";
RL Genes Dev. 13:2148-2158(1999).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND SUBCELLULAR LOCATION.
RX PubMed=14527413; DOI=10.1016/S1097-2765(03)00349-6;
RA Lejeune F., Li X., Maquat L.E.;
RT "Nonsense-mediated mRNA decay in mammalian cells involves decapping,
RT deadenylating, and exonucleolytic activities.";
RL Mol. Cell 12:675-687(2003).
RN [10]
RP PROTEIN INTERACTION.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [11]
RP FUNCTION IN NUCLEAR PRE-MRNA DEGRADATION.
RX PubMed=16455498; DOI=10.1016/j.molcel.2005.12.008;
RA West S., Gromak N., Norbury C.J., Proudfoot N.J.;
RT "Adenylation and exosome-mediated degradation of cotranscriptionally
RT cleaved pre-messenger RNA in human cells.";
RL Mol. Cell 21:437-443(2006).
RN [12]
RP INTERACTION WITH ALYREF.
RX PubMed=17234882; DOI=10.1101/gad.1503107;
RA Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.;
RT "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA
RT splicing and export.";
RL Genes Dev. 21:160-174(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1D AND MPHOSPH6.
RX PubMed=17412707; DOI=10.1093/nar/gkm082;
RA Schilders G., van Dijk E., Pruijn G.J.M.;
RT "C1D and hMtr4p associate with the human exosome subunit PM/Scl-100
RT and are involved in pre-rRNA processing.";
RL Nucleic Acids Res. 35:2564-2572(2007).
RN [14]
RP FUNCTION IN MRNA DEGRADATION, AND SUBCELLULAR LOCATION.
RX PubMed=17545563; DOI=10.1261/rna.575107;
RA van Dijk E.L., Schilders G., Pruijn G.J.;
RT "Human cell growth requires a functional cytoplasmic exosome, which is
RT involved in various mRNA decay pathways.";
RL RNA 13:1027-1035(2007).
RN [15]
RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and
RT 3' to 5'.";
RL Genes Dev. 22:50-65(2008).
RN [16]
RP FUNCTION IN PROMPT DEGRADATION.
RX PubMed=19056938; DOI=10.1126/science.1164096;
RA Preker P., Nielsen J., Kammler S., Lykke-Andersen S.,
RA Christensen M.S., Mapendano C.K., Schierup M.H., Jensen T.H.;
RT "RNA exosome depletion reveals transcription upstream of active human
RT promoters.";
RL Science 322:1851-1854(2008).
RN [17]
RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=20531386; DOI=10.1038/emboj.2010.121;
RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A.,
RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S.,
RA Stepien P.P., Dziembowski A., Jensen T.H.;
RT "The human core exosome interacts with differentially localized
RT processive RNases: hDIS3 and hDIS3L.";
RL EMBO J. 29:2342-2357(2010).
RN [18]
RP IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20531389; DOI=10.1038/emboj.2010.122;
RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
RA Heck A.J., Raijmakers R., Pruijn G.J.;
RT "Dis3-like 1: a novel exoribonuclease associated with the human
RT exosome.";
RL EMBO J. 29:2358-2367(2010).
RN [19]
RP FUNCTION IN NUCLEAR MRNA SURVEILLANCE.
RX PubMed=20699273; DOI=10.1093/nar/gkq703;
RA de Almeida S.F., Garcia-Sacristan A., Custodio N., Carmo-Fonseca M.;
RT "A link between nuclear RNA surveillance, the human exosome and RNA
RT polymerase II transcriptional termination.";
RL Nucleic Acids Res. 38:8015-8026(2010).
RN [20]
RP FUNCTION IN RRNA MATURATION.
RX PubMed=20368444; DOI=10.1073/pnas.0910621107;
RA Slomovic S., Fremder E., Staals R.H., Pruijn G.J., Schuster G.;
RT "Addition of poly(A) and poly(A)-rich tails during RNA degradation in
RT the cytoplasm of human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7407-7412(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-583, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-826, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [26]
RP STRUCTURE BY NMR OF 483-593.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the HRDC domain of human exosome component
RT 10.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Putative catalytic component of the RNA exosome complex
CC which has 3'->5' exoribonuclease activity and participates in a
CC multitude of cellular RNA processing and degradation events. In
CC the nucleus, the RNA exosome complex is involved in proper
CC maturation of stable RNA species such as rRNA, snRNA and snoRNA,
CC in the elimination of RNA processing by-products and non-coding
CC 'pervasive' transcripts, such as antisense RNA species and
CC promoter-upstream transcripts (PROMPTs), and of mRNAs with
CC processing defects, thereby limiting or excluding their export to
CC the cytoplasm. The RNA exosome may be involved in Ig class switch
CC recombination (CSR) and/or Ig variable region somatic
CC hypermutation (SHM) by targeting AICDA deamination activity to
CC transcribed dsDNA substrates. In the cytoplasm, the RNA exosome
CC complex is involved in general mRNA turnover and specifically
CC degrades inherently unstable mRNAs containing AU-rich elements
CC (AREs) within their 3' untranslated regions, and in RNA
CC surveillance pathways, preventing translation of aberrant mRNAs.
CC It seems to be involved in degradation of histone mRNA. EXOSC10
CC has 3'-5' exonuclease activity (By similarity). EXOSC10 is
CC required for nucleolar localization of C1D and probably mediates
CC the association of SKIV2L2, C1D and MPP6 wth the RNA exosome
CC involved in the maturation of 5.8S rRNA. {ECO:0000250,
CC ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498,
CC ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563,
CC ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938,
CC ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273}.
CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically
CC inactive RNA exosome core (Exo-9) complex is believed to associate
CC with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic-
CC and nuclear-specific RNA exosome complex forms. Interacts with C1D
CC and MPHOSPH6. Interacts with ALYREF/THOC4.
CC {ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:17412707,
CC ECO:0000269|PubMed:20531389}.
CC -!- INTERACTION:
CC Q13901:C1D; NbExp=5; IntAct=EBI-358236, EBI-3844053;
CC P17844:DDX5; NbExp=3; IntAct=EBI-358236, EBI-351962;
CC Q9Y2L1:DIS3; NbExp=4; IntAct=EBI-358236, EBI-373539;
CC Q9NPD3:EXOSC4; NbExp=4; IntAct=EBI-358236, EBI-371823;
CC Q9NQT4:EXOSC5; NbExp=3; IntAct=EBI-358236, EBI-371876;
CC Q99547:MPHOSPH6; NbExp=4; IntAct=EBI-358236, EBI-373187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus.
CC Note=Strongly enriched in the nucleolus and a small amount has
CC been found in cytoplasm supporting the existence of a nucleolar
CC RNA exosome complex form.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01780-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01780-2; Sequence=VSP_004362;
CC Note=No experimental confirmation available.;
CC -!- SIMILARITY: Contains 1 3'-5' exonuclease domain. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 HRDC domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00328}.
DR EMBL; X66113; CAA46904.1; -; mRNA.
DR EMBL; L01457; AAB59352.1; -; mRNA.
DR EMBL; AJ300188; CAC15569.1; -; Genomic_DNA.
DR EMBL; AL109811; CAI22106.1; -; Genomic_DNA.
DR EMBL; AL109811; CAI22107.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71679.1; -; Genomic_DNA.
DR EMBL; BC039901; AAH39901.1; -; mRNA.
DR EMBL; BC073788; AAH73788.1; -; mRNA.
DR CCDS; CCDS126.1; -. [Q01780-2]
DR CCDS; CCDS30584.1; -. [Q01780-1]
DR PIR; A43920; A43920.
DR PIR; JH0796; JH0796.
DR RefSeq; NP_001001998.1; NM_001001998.2. [Q01780-1]
DR RefSeq; NP_002676.1; NM_002685.3. [Q01780-2]
DR UniGene; Hs.632368; -.
DR PDB; 2CPR; NMR; -; A=483-593.
DR PDB; 3SAF; X-ray; 2.50 A; A/B=180-606.
DR PDB; 3SAG; X-ray; 2.70 A; A/B=180-606.
DR PDB; 3SAH; X-ray; 2.65 A; A/B=180-606.
DR PDBsum; 2CPR; -.
DR PDBsum; 3SAF; -.
DR PDBsum; 3SAG; -.
DR PDBsum; 3SAH; -.
DR ProteinModelPortal; Q01780; -.
DR SMR; Q01780; -.
DR BioGrid; 111403; 75.
DR DIP; DIP-31249N; -.
DR IntAct; Q01780; 54.
DR MINT; MINT-1143843; -.
DR STRING; 9606.ENSP00000366135; -.
DR iPTMnet; Q01780; -.
DR PhosphoSitePlus; Q01780; -.
DR SwissPalm; Q01780; -.
DR BioMuta; EXOSC10; -.
DR DMDM; 8928564; -.
DR SWISS-2DPAGE; Q01780; -.
DR EPD; Q01780; -.
DR MaxQB; Q01780; -.
DR PaxDb; Q01780; -.
DR PeptideAtlas; Q01780; -.
DR PRIDE; Q01780; -.
DR DNASU; 5394; -.
DR Ensembl; ENST00000304457; ENSP00000307307; ENSG00000171824. [Q01780-2]
DR Ensembl; ENST00000376936; ENSP00000366135; ENSG00000171824. [Q01780-1]
DR GeneID; 5394; -.
DR KEGG; hsa:5394; -.
DR UCSC; uc001asa.4; human. [Q01780-1]
DR CTD; 5394; -.
DR DisGeNET; 5394; -.
DR GeneCards; EXOSC10; -.
DR HGNC; HGNC:9138; EXOSC10.
DR HPA; CAB037141; -.
DR HPA; HPA028470; -.
DR HPA; HPA028484; -.
DR MIM; 605960; gene.
DR neXtProt; NX_Q01780; -.
DR OpenTargets; ENSG00000171824; -.
DR PharmGKB; PA33464; -.
DR eggNOG; KOG2206; Eukaryota.
DR eggNOG; COG0349; LUCA.
DR GeneTree; ENSGT00390000015408; -.
DR HOGENOM; HOG000001579; -.
DR HOVERGEN; HBG051524; -.
DR InParanoid; Q01780; -.
DR KO; K12591; -.
DR OMA; GNKSMSF; -.
DR OrthoDB; EOG091G03BH; -.
DR PhylomeDB; Q01780; -.
DR TreeFam; TF105991; -.
DR BioCyc; ZFISH:ENSG00000171824-MONOMER; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR ChiTaRS; EXOSC10; human.
DR EvolutionaryTrace; Q01780; -.
DR GeneWiki; Exosome_component_10; -.
DR GenomeRNAi; 5394; -.
DR PRO; PR:Q01780; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000171824; -.
DR CleanEx; HS_EXOSC10; -.
DR ExpressionAtlas; Q01780; baseline and differential.
DR Genevisible; Q01780; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035327; C:transcriptionally active chromatin; IMP:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; EXP:Reactome.
DR GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0071034; P:CUT catabolic process; IMP:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0071048; P:nuclear retention of unspliced pre-mRNA at the site of transcription; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; TAS:Reactome.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR InterPro; IPR010997; HRDC-like.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR012337; RNaseH-like_dom.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF08066; PMC2NT; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Exonuclease; Exosome; Hydrolase; Isopeptide bond;
KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1 885 Exosome component 10.
FT /FTId=PRO_0000087133.
FT DOMAIN 503 583 HRDC. {ECO:0000255|PROSITE-
FT ProRule:PRU00328}.
FT MOD_RES 821 821 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO1).
FT {ECO:0000244|PubMed:25114211}.
FT CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO2).
FT {ECO:0000244|PubMed:25218447}.
FT CROSSLNK 826 826 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO2).
FT {ECO:0000244|PubMed:25772364}.
FT VAR_SEQ 695 719 Missing (in isoform 2).
FT {ECO:0000303|PubMed:1644924}.
FT /FTId=VSP_004362.
FT HELIX 183 186 {ECO:0000244|PDB:3SAF}.
FT STRAND 194 196 {ECO:0000244|PDB:3SAF}.
FT HELIX 214 216 {ECO:0000244|PDB:3SAF}.
FT HELIX 218 220 {ECO:0000244|PDB:3SAF}.
FT STRAND 253 255 {ECO:0000244|PDB:3SAF}.
FT HELIX 259 263 {ECO:0000244|PDB:3SAF}.
FT HELIX 269 272 {ECO:0000244|PDB:3SAF}.
FT HELIX 283 285 {ECO:0000244|PDB:3SAF}.
FT STRAND 288 291 {ECO:0000244|PDB:3SAF}.
FT HELIX 294 304 {ECO:0000244|PDB:3SAF}.
FT STRAND 308 317 {ECO:0000244|PDB:3SAF}.
FT STRAND 325 332 {ECO:0000244|PDB:3SAF}.
FT STRAND 337 341 {ECO:0000244|PDB:3SAF}.
FT TURN 342 345 {ECO:0000244|PDB:3SAF}.
FT HELIX 346 352 {ECO:0000244|PDB:3SAF}.
FT HELIX 353 356 {ECO:0000244|PDB:3SAF}.
FT STRAND 361 367 {ECO:0000244|PDB:3SAF}.
FT HELIX 369 379 {ECO:0000244|PDB:3SAF}.
FT STRAND 384 388 {ECO:0000244|PDB:3SAF}.
FT HELIX 389 395 {ECO:0000244|PDB:3SAF}.
FT HELIX 403 411 {ECO:0000244|PDB:3SAF}.
FT TURN 418 421 {ECO:0000244|PDB:3SAF}.
FT HELIX 431 442 {ECO:0000244|PDB:3SAF}.
FT HELIX 444 458 {ECO:0000244|PDB:3SAF}.
FT STRAND 461 463 {ECO:0000244|PDB:3SAH}.
FT HELIX 464 476 {ECO:0000244|PDB:3SAF}.
FT HELIX 490 492 {ECO:0000244|PDB:3SAF}.
FT HELIX 493 496 {ECO:0000244|PDB:3SAF}.
FT STRAND 497 500 {ECO:0000244|PDB:2CPR}.
FT HELIX 504 524 {ECO:0000244|PDB:3SAF}.
FT HELIX 528 531 {ECO:0000244|PDB:3SAF}.
FT HELIX 534 543 {ECO:0000244|PDB:3SAF}.
FT HELIX 548 552 {ECO:0000244|PDB:3SAF}.
FT STRAND 555 557 {ECO:0000244|PDB:3SAH}.
FT HELIX 560 564 {ECO:0000244|PDB:3SAF}.
FT HELIX 566 577 {ECO:0000244|PDB:3SAF}.
FT HELIX 583 586 {ECO:0000244|PDB:3SAF}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 503 583 iprf:HRDC [T]
FT MYHIT 503 583 ismart:HRDC [T]
FT MYHIT 506 572 ipfam:HRDC [T]
FT MYHIT 288 456 ismart:35EXOc [T]
FT MYHIT 44 133 ipfam:PMC2NT [T]
FT MYHIT 289 455 ipfam:DNA_pol_A_exo1 [T]
SQ 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
//
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