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Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75)

 EXOS9_HUMAN             Reviewed;         439 AA.
Q06265; Q12883; Q4W5P5; Q86Y41; Q86Y48;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 3.
22-NOV-2017, entry version 171.
RecName: Full=Exosome complex component RRP45;
AltName: Full=Autoantigen PM/Scl 1;
AltName: Full=Exosome component 9;
AltName: Full=P75 polymyositis-scleroderma overlap syndrome-associated autoantigen;
AltName: Full=Polymyositis/scleroderma autoantigen 1;
AltName: Full=Polymyositis/scleroderma autoantigen 75 kDa;
Short=PM/Scl-75;
Name=EXOSC9; Synonyms=PMSCL1;
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 3).
TISSUE=Lymphoblastoma;
PubMed=2007859; DOI=10.1084/jem.173.4.941;
Alderuccio F., Chan E.K.L., Tan E.M.;
"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.";
J. Exp. Med. 173:941-952(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Stahnke G., Haubruck H.;
"Nucleotide sequence of an alternatively spliced cDNA coding for PM-
Scl-75, an autoantigen of the Polymyositis/Scleroderma overlap
syndrome.";
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND IDENTIFICATION IN THE RNA EXOSOME COMPLEX.
PubMed=12788944; DOI=10.1074/jbc.M302488200;
Raijmakers R., Egberts W.V., van Venrooij W.J., Pruijn G.J.;
"The association of the human PM/Scl-75 autoantigen with the exosome
is dependent on a newly identified N terminus.";
J. Biol. Chem. 278:30698-30704(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA
EXOSOME CORE COMPLEX.
PubMed=11719186; DOI=10.1016/S0092-8674(01)00578-5;
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.;
"AU binding proteins recruit the exosome to degrade ARE-containing
mRNAs.";
Cell 107:451-464(2001).
[7]
FUNCTION IN CYTOPLASMIC MRNA DEGRADATION, AND ARE BINDING.
PubMed=11782436; DOI=10.1093/emboj/21.1.165;
Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G.,
Lutz C.S., Wilusz J.;
"The mammalian exosome mediates the efficient degradation of mRNAs
that contain AU-rich elements.";
EMBO J. 21:165-174(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
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).
[10]
FUNCTION IN ARE-CONTAINING MRNA-BINDING.
PubMed=16912217; DOI=10.1261/rna.144606;
Anderson J.R., Mukherjee D., Muthukumaraswamy K., Moraes K.C.,
Wilusz C.J., Wilusz J.;
"Sequence-specific RNA binding mediated by the RNase PH domain of
components of the exosome.";
RNA 12:1810-1816(2006).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND
SER-394, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-297, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 AND
SER-394, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
INTERACTION WITH SETX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
388-PRO--LEU-391; 390-ILE-LEU-391 AND 395-GLU--GLU-398.
PubMed=24105744; DOI=10.1101/gad.224923.113;
Richard P., Feng S., Manley J.L.;
"A SUMO-dependent interaction between Senataxin and the exosome,
disrupted in the neurodegenerative disease AOA2, targets the exosome
to sites of transcription-induced DNA damage.";
Genes Dev. 27:2227-2232(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-306, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-346,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-411 (ISOFORM
2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-327
(ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, 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-297, 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]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, 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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297 AND LYS-419, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297 AND LYS-419, 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]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY,
AND RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
Liu Q., Greimann J.C., Lima C.D.;
"Reconstitution, activities, and structure of the eukaryotic RNA
exosome.";
Cell 127:1223-1237(2006).
[30]
ERRATUM.
Liu Q., Greimann J.C., Lima C.D.;
Cell 131:188-189(2007).
-!- 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.
{ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:16455498,
ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}.
-!- SUBUNIT: 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 (PubMed:11719186,
PubMed:12788944, PubMed:20531389). Interacts (via C-terminus
region) with SETX (via N-terminus domain); the interaction
enhances SETX sumoylation (PubMed:24105744).
{ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:12788944,
ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:24105744}.
-!- INTERACTION:
Q9NPD3:EXOSC4; NbExp=5; IntAct=EBI-347966, EBI-371823;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
{ECO:0000269|PubMed:24105744}. Nucleus, nucleolus
{ECO:0000269|PubMed:24105744}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:24105744}. Note=Colocalizes with SETX in
nuclear foci upon induction of transcription-related DNA damage at
the S phase (PubMed:24105744). {ECO:0000269|PubMed:24105744}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleolus.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Note=Excluded from the
nucleolus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=PM/SCL-75c-alpha;
IsoId=Q06265-1; Sequence=Displayed;
Name=2; Synonyms=PM/SCL-75c-beta;
IsoId=Q06265-2; Sequence=VSP_025556;
Note=Contains a phosphoserine at position 409. Contains a
phosphoserine at position 411. {ECO:0000244|PubMed:24275569};
Name=3; Synonyms=PM/SCL-75a-alpha;
IsoId=Q06265-3; Sequence=VSP_025555;
Name=4; Synonyms=PM/SCL-75a-beta;
IsoId=Q06265-4; Sequence=VSP_025555, VSP_025556;
Note=Contains a phosphoserine at position 325. Contains a
phosphoserine at position 327. {ECO:0000244|PubMed:24275569};
-!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
-!- CAUTION: The six exosome core subunits containing a RNase PH-
domain are not phosphorolytically active. {ECO:0000305}.
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EMBL; M58460; AAA58384.1; -; mRNA.
EMBL; U09215; AAA18832.1; -; mRNA.
EMBL; AJ505989; CAD44530.1; -; mRNA.
EMBL; AJ517294; CAD56889.1; -; mRNA.
EMBL; AC079341; AAY40968.1; -; Genomic_DNA.
CCDS; CCDS34057.1; -. [Q06265-2]
CCDS; CCDS3722.2; -. [Q06265-1]
PIR; G01425; G01425.
RefSeq; NP_001029366.1; NM_001034194.1. [Q06265-2]
RefSeq; NP_005024.2; NM_005033.2. [Q06265-1]
UniGene; Hs.91728; -.
PDB; 2NN6; X-ray; 3.35 A; A=1-302.
PDBsum; 2NN6; -.
ProteinModelPortal; Q06265; -.
SMR; Q06265; -.
BioGrid; 111402; 50.
CORUM; Q06265; -.
DIP; DIP-31286N; -.
IntAct; Q06265; 40.
MINT; MINT-1036055; -.
STRING; 9606.ENSP00000368984; -.
iPTMnet; Q06265; -.
PhosphoSitePlus; Q06265; -.
BioMuta; EXOSC9; -.
DMDM; 147744559; -.
EPD; Q06265; -.
MaxQB; Q06265; -.
PaxDb; Q06265; -.
PeptideAtlas; Q06265; -.
PRIDE; Q06265; -.
Ensembl; ENST00000243498; ENSP00000243498; ENSG00000123737. [Q06265-1]
Ensembl; ENST00000379663; ENSP00000368984; ENSG00000123737. [Q06265-2]
GeneID; 5393; -.
KEGG; hsa:5393; -.
UCSC; uc003idz.4; human. [Q06265-1]
CTD; 5393; -.
DisGeNET; 5393; -.
EuPathDB; HostDB:ENSG00000123737.12; -.
GeneCards; EXOSC9; -.
HGNC; HGNC:9137; EXOSC9.
HPA; CAB070171; -.
HPA; HPA041838; -.
HPA; HPA048257; -.
MIM; 606180; gene.
neXtProt; NX_Q06265; -.
OpenTargets; ENSG00000123737; -.
PharmGKB; PA33463; -.
eggNOG; KOG1614; Eukaryota.
eggNOG; COG2123; LUCA.
GeneTree; ENSGT00530000063093; -.
HOGENOM; HOG000229504; -.
HOVERGEN; HBG051523; -.
InParanoid; Q06265; -.
KO; K03678; -.
OMA; MFMNSNL; -.
OrthoDB; EOG091G08FZ; -.
PhylomeDB; Q06265; -.
TreeFam; TF300092; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
SIGNOR; Q06265; -.
EvolutionaryTrace; Q06265; -.
GeneWiki; Exosome_component_9; -.
GenomeRNAi; 5393; -.
PRO; PR:Q06265; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000123737; -.
CleanEx; HS_EXOSC9; -.
ExpressionAtlas; Q06265; baseline and differential.
Genevisible; Q06265; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; NAS:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IMP:UniProtKB.
GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:UniProtKB.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
CDD; cd11368; RNase_PH_RRP45; 1.
Gene3D; 3.30.230.70; -; 1.
InterPro; IPR001247; ExoRNase_PH_dom1.
InterPro; IPR015847; ExoRNase_PH_dom2.
InterPro; IPR036345; ExoRNase_PH_dom2_sf.
InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR033100; Rrp45.
Pfam; PF01138; RNase_PH; 1.
Pfam; PF03725; RNase_PH_C; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF55666; SSF55666; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Exosome; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding; rRNA processing;
Ubl conjugation.
CHAIN 1 439 Exosome complex component RRP45.
/FTId=PRO_0000139971.
REGION 1 268 ARE binding.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 297 297 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 84 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:2007859,
ECO:0000303|Ref.2}.
/FTId=VSP_025555.
VAR_SEQ 385 385 Q -> QELGFHHVGQTGLEFLTS (in isoform 2 and
isoform 4). {ECO:0000303|PubMed:12788944,
ECO:0000303|Ref.2}.
/FTId=VSP_025556.
VARIANT 366 366 I -> V (in dbSNP:rs1803183).
/FTId=VAR_051867.
VARIANT 425 425 S -> T (in dbSNP:rs1051881).
/FTId=VAR_014924.
MUTAGEN 388 391 PIIL->EECP: Abolishes interaction with
SETX. {ECO:0000269|PubMed:24105744}.
MUTAGEN 388 391 Missing: Abolishes interaction with SETX.
{ECO:0000269|PubMed:24105744}.
MUTAGEN 390 391 Missing: Abolishes interaction with SETX.
{ECO:0000269|PubMed:24105744}.
MUTAGEN 395 398 EEEE->AAAA: Abolishes interaction with
SETX. {ECO:0000269|PubMed:24105744}.
MUTAGEN 395 398 Missing: Abolishes interaction with SETX.
{ECO:0000269|PubMed:24105744}.
HELIX 8 19 {ECO:0000244|PDB:2NN6}.
STRAND 36 39 {ECO:0000244|PDB:2NN6}.
STRAND 45 52 {ECO:0000244|PDB:2NN6}.
STRAND 54 59 {ECO:0000244|PDB:2NN6}.
STRAND 62 64 {ECO:0000244|PDB:2NN6}.
TURN 69 72 {ECO:0000244|PDB:2NN6}.
STRAND 76 82 {ECO:0000244|PDB:2NN6}.
TURN 84 86 {ECO:0000244|PDB:2NN6}.
STRAND 92 94 {ECO:0000244|PDB:2NN6}.
HELIX 96 99 {ECO:0000244|PDB:2NN6}.
HELIX 101 113 {ECO:0000244|PDB:2NN6}.
STRAND 118 121 {ECO:0000244|PDB:2NN6}.
TURN 125 127 {ECO:0000244|PDB:2NN6}.
STRAND 128 138 {ECO:0000244|PDB:2NN6}.
HELIX 146 159 {ECO:0000244|PDB:2NN6}.
HELIX 176 179 {ECO:0000244|PDB:2NN6}.
STRAND 191 198 {ECO:0000244|PDB:2NN6}.
TURN 200 202 {ECO:0000244|PDB:2NN6}.
STRAND 203 208 {ECO:0000244|PDB:2NN6}.
HELIX 211 216 {ECO:0000244|PDB:2NN6}.
STRAND 220 226 {ECO:0000244|PDB:2NN6}.
TURN 227 229 {ECO:0000244|PDB:2NN6}.
STRAND 230 238 {ECO:0000244|PDB:2NN6}.
HELIX 244 277 {ECO:0000244|PDB:2NN6}.
HELIX 287 290 {ECO:0000244|PDB:2NN6}.
STRAND 291 298 {ECO:0000244|PDB:2NN6}.
SEQUENCE 439 AA; 48949 MW; 7E27322F094ED3F3 CRC64;
MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIRISFG TDYGCCIVEL GKTRVLGQVS
CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLMERCL RNSKCIDTES
LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGD EVTLYTPEER
DPVPLSIHHM PICVSFAFFQ QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI
MLLKDQVLRC SKIAGVKVAE ITELILKALE NDQKVRKEGG KFGFAESIAN QRITAFKMEK
APIDTSDVEE KAEEIIAEAE PPSEVVSTPV LWTPGTAQIG EGVENSWGDL EDSEKEDDEG
GGDQAIILDG IKMDTGVEVS DIGSQDAPII LSDSEEEEMI ILEPDKNPKK IRTQTTSAKQ
EKAPSKKPVK RRKKKRAAN


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