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Exosome complex component RRP46 (Chronic myelogenous leukemia tumor antigen 28) (Exosome component 5) (Ribosomal RNA-processing protein 46) (p12B)

 EXOS5_HUMAN             Reviewed;         235 AA.
Q9NQT4; Q32Q81; Q8NG16; Q96I89;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=Exosome complex component RRP46;
AltName: Full=Chronic myelogenous leukemia tumor antigen 28;
AltName: Full=Exosome component 5;
AltName: Full=Ribosomal RNA-processing protein 46;
AltName: Full=p12B;
Name=EXOSC5; Synonyms=CML28, RRP46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
PubMed=11110791; DOI=10.1074/jbc.M007603200;
Brouwer R., Allmang C., Raijmakers R., van Aarssen Y., Egberts W.V.,
Petfalski E., van Venrooij W.J., Tollervey D., Pruijn G.J.M.;
"Three novel components of the human exosome.";
J. Biol. Chem. 276:6177-6184(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12359762;
Yang X.-F., Wu C.J., Chen L., Alyea E.P., Canning C., Kantoff P.,
Soiffer R.J., Dranoff G., Ritz J.;
"CML28 is a broadly immunogenic antigen, which is overexpressed in
tumor cells.";
Cancer Res. 62:5517-5522(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-5.
TISSUE=B-cell;
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).
[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.
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]
SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC1.
PubMed=11812149; DOI=10.1006/jmbi.2001.5265;
Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions of hCsl4p with other human exosome
subunits.";
J. Mol. Biol. 315:809-818(2002).
[9]
INTERACTION WITH ZC3HAV1.
PubMed=17185417; DOI=10.1073/pnas.0607063104;
Guo X., Ma J., Sun J., Gao G.;
"The zinc-finger antiviral protein recruits the RNA processing exosome
to degrade the target mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 104:151-156(2007).
[10]
INTERACTION WITH DDX17.
PubMed=18334637; DOI=10.1073/pnas.0712276105;
Chen G., Guo X., Lv F., Xu Y., Gao G.;
"p72 DEAD box RNA helicase is required for optimal function of the
zinc-finger antiviral protein.";
Proc. Natl. Acad. Sci. U.S.A. 105:4352-4357(2008).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, 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).
[13]
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).
[14]
FUNCTION IN DEAMINATION OF TRANSCRIBED DNA SUBSTRATE.
PubMed=21255825; DOI=10.1016/j.cell.2011.01.001;
Basu U., Meng F.L., Keim C., Grinstein V., Pefanis E., Eccleston J.,
Zhang T., Myers D., Wasserman C.R., Wesemann D.R., Januszyk K.,
Gregory R.I., Deng H., Lima C.D., Alt F.W.;
"The RNA exosome targets the AID cytidine deaminase to both strands of
transcribed duplex DNA substrates.";
Cell 144:353-363(2011).
[15]
INTERACTION WITH GTPBP1.
PubMed=21515746; DOI=10.1096/fj.10-178715;
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
Chung S.J., Senju S., Nishimura Y., Kim K.T.;
"Modulation of exosome-mediated mRNA turnover by interaction of GTP-
binding protein 1 (GTPBP1) with its target mRNAs.";
FASEB J. 25:2757-2769(2011).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, 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).
[18]
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).
[19]
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. {ECO:0000269|PubMed:11782436,
ECO:0000269|PubMed:21255825}.
-!- 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. Interacts with
EXOSC1. Interacts with GTPBP1. Interacts with ZC3HAV1. Interacts
with DDX17 only in the presence of ZC3HAV1 in an RNA-independent
manner. {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:11812149,
ECO:0000269|PubMed:17185417, ECO:0000269|PubMed:18334637,
ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21515746}.
-!- INTERACTION:
Q13490:BIRC2; NbExp=5; IntAct=EBI-371876, EBI-514538;
Q96GS4:BORCS6; NbExp=4; IntAct=EBI-371876, EBI-10193358;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-371876, EBI-739580;
Q96D03:DDIT4L; NbExp=4; IntAct=EBI-371876, EBI-742054;
Q8NF50-2:DOCK8; NbExp=3; IntAct=EBI-371876, EBI-10174653;
Q9Y3B2:EXOSC1; NbExp=25; IntAct=EBI-371876, EBI-371892;
Q01780:EXOSC10; NbExp=3; IntAct=EBI-371876, EBI-358236;
Q9NQT5:EXOSC3; NbExp=8; IntAct=EBI-371876, EBI-371866;
Q96B26:EXOSC8; NbExp=14; IntAct=EBI-371876, EBI-371922;
A0A0C3SFZ9:FCHO1; NbExp=4; IntAct=EBI-371876, EBI-11977403;
O14526:FCHO1; NbExp=3; IntAct=EBI-371876, EBI-719823;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-371876, EBI-618309;
Q9UKT9:IKZF3; NbExp=7; IntAct=EBI-371876, EBI-747204;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-371876, EBI-10171552;
Q04864:REL; NbExp=3; IntAct=EBI-371876, EBI-307352;
Q13829:TNFAIP1; NbExp=5; IntAct=EBI-371876, EBI-2505861;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-371876, EBI-2130429;
Q8K3Y6:Zc3hav1 (xeno); NbExp=6; IntAct=EBI-371876, EBI-8860250;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11812149}. Cytoplasm
{ECO:0000305|PubMed:11812149}. Nucleus
{ECO:0000305|PubMed:11812149}.
-!- TISSUE SPECIFICITY: Highly expressed in a variety of hematopoietic
and epithelial tumor cell lines, but not in normal hematopoietic
tissues or other normal tissue, with the exception of testis.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAM75154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF281134; AAF82135.1; -; mRNA.
EMBL; AF285785; AAM75154.1; ALT_INIT; mRNA.
EMBL; AC011462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007742; AAH07742.1; -; mRNA.
EMBL; BC107696; AAI07697.1; -; mRNA.
CCDS; CCDS12580.1; -.
RefSeq; NP_064543.3; NM_020158.3.
UniGene; Hs.283741; -.
PDB; 2NN6; X-ray; 3.35 A; D=1-235.
PDBsum; 2NN6; -.
ProteinModelPortal; Q9NQT4; -.
SMR; Q9NQT4; -.
BioGrid; 121243; 74.
CORUM; Q9NQT4; -.
DIP; DIP-29846N; -.
IntAct; Q9NQT4; 82.
MINT; MINT-1479651; -.
STRING; 9606.ENSP00000221233; -.
iPTMnet; Q9NQT4; -.
PhosphoSitePlus; Q9NQT4; -.
BioMuta; EXOSC5; -.
DMDM; 14285757; -.
EPD; Q9NQT4; -.
MaxQB; Q9NQT4; -.
PaxDb; Q9NQT4; -.
PeptideAtlas; Q9NQT4; -.
PRIDE; Q9NQT4; -.
DNASU; 56915; -.
Ensembl; ENST00000221233; ENSP00000221233; ENSG00000077348.
GeneID; 56915; -.
KEGG; hsa:56915; -.
UCSC; uc002oqo.4; human.
CTD; 56915; -.
DisGeNET; 56915; -.
EuPathDB; HostDB:ENSG00000077348.8; -.
GeneCards; EXOSC5; -.
HGNC; HGNC:24662; EXOSC5.
HPA; HPA053150; -.
HPA; HPA055677; -.
MIM; 606492; gene.
neXtProt; NX_Q9NQT4; -.
OpenTargets; ENSG00000077348; -.
PharmGKB; PA134890468; -.
eggNOG; KOG1069; Eukaryota.
eggNOG; COG0689; LUCA.
GeneTree; ENSGT00550000075002; -.
HOGENOM; HOG000229515; -.
HOVERGEN; HBG051520; -.
InParanoid; Q9NQT4; -.
KO; K12590; -.
OMA; CNYRPKA; -.
OrthoDB; EOG091G0N6V; -.
PhylomeDB; Q9NQT4; -.
TreeFam; TF315920; -.
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.
EvolutionaryTrace; Q9NQT4; -.
GeneWiki; Exosome_component_5; -.
GenomeRNAi; 56915; -.
PRO; PR:Q9NQT4; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000077348; -.
CleanEx; HS_EXOSC5; -.
ExpressionAtlas; Q9NQT4; baseline and differential.
Genevisible; Q9NQT4; HS.
GO; GO:0005737; C:cytoplasm; NAS: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:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0035327; C:transcriptionally active chromatin; IMP:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; NAS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IMP:MGI.
GO; GO:0045006; P:DNA deamination; IDA:UniProtKB.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IMP:UniProtKB.
GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0031125; P:rRNA 3'-end processing; IBA:GO_Central.
GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
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.
Pfam; PF01138; RNase_PH; 1.
Pfam; PF03725; RNase_PH_C; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55666; SSF55666; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Exosome; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
rRNA processing.
CHAIN 1 235 Exosome complex component RRP46.
/FTId=PRO_0000139975.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VARIANT 5 5 T -> M (in dbSNP:rs10853751).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030788.
VARIANT 33 33 C -> W (in dbSNP:rs34500671).
/FTId=VAR_051868.
STRAND 31 36 {ECO:0000244|PDB:2NN6}.
STRAND 39 49 {ECO:0000244|PDB:2NN6}.
STRAND 52 63 {ECO:0000244|PDB:2NN6}.
STRAND 74 81 {ECO:0000244|PDB:2NN6}.
STRAND 83 85 {ECO:0000244|PDB:2NN6}.
HELIX 89 105 {ECO:0000244|PDB:2NN6}.
HELIX 107 109 {ECO:0000244|PDB:2NN6}.
STRAND 111 124 {ECO:0000244|PDB:2NN6}.
HELIX 129 143 {ECO:0000244|PDB:2NN6}.
STRAND 152 159 {ECO:0000244|PDB:2NN6}.
STRAND 165 168 {ECO:0000244|PDB:2NN6}.
HELIX 171 176 {ECO:0000244|PDB:2NN6}.
STRAND 178 186 {ECO:0000244|PDB:2NN6}.
TURN 187 189 {ECO:0000244|PDB:2NN6}.
STRAND 194 200 {ECO:0000244|PDB:2NN6}.
HELIX 203 231 {ECO:0000244|PDB:2NN6}.
SEQUENCE 235 AA; 25249 MW; C3C1FCB39D85B1EE CRC64;
MEEETHTDAK IRAENGTGSS PRGPGCSLRH FACEQNLLSR PDGSASFLQG DTSVLAGVYG
PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLIRN TCEAVVLGTL HPRTSITVVL
QVVSDAGSLL ACCLNAACMA LVDAGVPMRA LFCGVACALD SDGTLVLDPT SKQEKEARAV
LTFALDSVER KLLMSSTKGL YSDTELQQCL AAAQAASQHV FRFYRESLQR RYSKS


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18-003-43636 Exosome complex exonuclease RRP42 - EC 3.1.13.-; Ribosomal RNA-processing protein 42; Exosome component 7; p8 Polyclonal 0.1 mg Protein A
18-003-44218 Exosome complex exonuclease RRP4 - EC 3.1.13.-; Ribosomal RNA-processing protein 4; Exosome component 2 Polyclonal 0.1 mg Protein A
EIAAB13500 EXOSC8,Exosome complex component RRP43,Exosome component 8,Homo sapiens,Human,OIP2,OIP-2,Opa-interacting protein 2,p9,Ribosomal RNA-processing protein 43,RRP43
18-003-43649 Exosome complex exonuclease RRP41 - EC 3.1.13.-; Ribosomal RNA-processing protein 41; Exosome component 4; p12A Polyclonal 0.1 mg Protein A
EIAAB13497 Exosc7,Exosome complex exonuclease RRP42,Exosome component 7,Mouse,Mus musculus,Ribosomal RNA-processing protein 42,Rrp42
20-372-60233 exosome component 7 (EXOSC7). mRNA - Mouse monoclonal anti-human EXOSC7 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 42; Exosome component 7; p8 Monoclonal 0.1 mg
20-372-60232 exosome component 2 (EXOSC2). mRNA - Mouse monoclonal anti-human EXOSC2 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 4; Exosome component 2 Monoclonal 0.1 mg
EXOS5_MOUSE Mouse ELISA Kit FOR Exosome complex component RRP46 96T
CSB-EL007893MO Mouse Exosome complex component RRP46(EXOSC5) ELISA kit 96T
CSB-EL007893HU Human Exosome complex component RRP46(EXOSC5) ELISA kit 96T
EIAAB13504 Exosc9,Exosome complex component RRP45,Exosome component 9,Rat,Rattus norvegicus


 

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