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Exosome complex component RRP41 (Exosome component 4) (Ribosomal RNA-processing protein 41) (p12A)

 EXOS4_HUMAN             Reviewed;         245 AA.
Q9NPD3;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 165.
RecName: Full=Exosome complex component RRP41;
AltName: Full=Exosome component 4;
AltName: Full=Ribosomal RNA-processing protein 41;
AltName: Full=p12A;
Name=EXOSC4; Synonyms=RRP41, SKI6;
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 [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[5]
PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[6]
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).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
INTERACTION WITH DDX60.
PubMed=21791617; DOI=10.1128/MCB.01368-10;
Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
"DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting
RIG-I-like receptor-mediated signaling.";
Mol. Cell. Biol. 31:3802-3819(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[19]
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).
[20]
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. EXOSC4 binds to ARE-containing RNAs.
{ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563,
ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:20368444,
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
DDX60. {ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:20531389,
ECO:0000269|PubMed:21791617}.
-!- INTERACTION:
Q9Y3B2:EXOSC1; NbExp=7; IntAct=EBI-371823, EBI-371892;
Q01780:EXOSC10; NbExp=4; IntAct=EBI-371823, EBI-358236;
Q13868:EXOSC2; NbExp=8; IntAct=EBI-371823, EBI-301735;
Q9NQT5:EXOSC3; NbExp=5; IntAct=EBI-371823, EBI-371866;
Q15024:EXOSC7; NbExp=5; IntAct=EBI-371823, EBI-371841;
Q06265:EXOSC9; NbExp=6; IntAct=EBI-371823, EBI-347966;
P56282:POLE2; NbExp=4; IntAct=EBI-371823, EBI-713847;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}.
Nucleus, nucleolus {ECO:0000269|PubMed:17545563}. Nucleus
{ECO:0000269|PubMed:17545563}.
-!- 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; AF281133; AAF82134.1; -; mRNA.
EMBL; AK000598; BAA91279.1; -; mRNA.
EMBL; AC109322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002777; AAH02777.1; -; mRNA.
CCDS; CCDS6414.1; -.
RefSeq; NP_061910.1; NM_019037.2.
UniGene; Hs.632041; -.
PDB; 2NN6; X-ray; 3.35 A; B=2-245.
PDBsum; 2NN6; -.
ProteinModelPortal; Q9NPD3; -.
BioGrid; 120007; 95.
CORUM; Q9NPD3; -.
DIP; DIP-31165N; -.
IntAct; Q9NPD3; 69.
MINT; Q9NPD3; -.
STRING; 9606.ENSP00000315476; -.
iPTMnet; Q9NPD3; -.
PhosphoSitePlus; Q9NPD3; -.
BioMuta; EXOSC4; -.
DMDM; 14285756; -.
SWISS-2DPAGE; Q9NPD3; -.
EPD; Q9NPD3; -.
MaxQB; Q9NPD3; -.
PaxDb; Q9NPD3; -.
PeptideAtlas; Q9NPD3; -.
PRIDE; Q9NPD3; -.
DNASU; 54512; -.
Ensembl; ENST00000316052; ENSP00000315476; ENSG00000178896.
GeneID; 54512; -.
KEGG; hsa:54512; -.
UCSC; uc003zau.4; human.
CTD; 54512; -.
EuPathDB; HostDB:ENSG00000178896.6; -.
GeneCards; EXOSC4; -.
HGNC; HGNC:18189; EXOSC4.
HPA; HPA024792; -.
MIM; 606491; gene.
neXtProt; NX_Q9NPD3; -.
OpenTargets; ENSG00000178896; -.
PharmGKB; PA134867931; -.
eggNOG; KOG1068; Eukaryota.
eggNOG; COG0689; LUCA.
GeneTree; ENSGT00550000074804; -.
HOGENOM; HOG000229515; -.
HOVERGEN; HBG051519; -.
InParanoid; Q9NPD3; -.
KO; K11600; -.
OMA; VINCQYS; -.
PhylomeDB; Q9NPD3; -.
TreeFam; TF313915; -.
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.
ChiTaRS; EXOSC4; human.
EvolutionaryTrace; Q9NPD3; -.
GeneWiki; Exosome_component_4; -.
GenomeRNAi; 54512; -.
PRO; PR:Q9NPD3; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000178896; -.
CleanEx; HS_EXOSC4; -.
ExpressionAtlas; Q9NPD3; baseline and differential.
Genevisible; Q9NPD3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; NAS:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
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; TAS:Reactome.
GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
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:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
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; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Exosome; Nucleus; Reference proteome;
RNA-binding; rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 245 Exosome complex component RRP41.
/FTId=PRO_0000139958.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
STRAND 14 17 {ECO:0000244|PDB:2NN6}.
STRAND 25 30 {ECO:0000244|PDB:2NN6}.
STRAND 32 45 {ECO:0000244|PDB:2NN6}.
STRAND 47 57 {ECO:0000244|PDB:2NN6}.
STRAND 60 62 {ECO:0000244|PDB:2NN6}.
STRAND 72 78 {ECO:0000244|PDB:2NN6}.
TURN 80 82 {ECO:0000244|PDB:2NN6}.
STRAND 83 85 {ECO:0000244|PDB:2NN6}.
TURN 89 91 {ECO:0000244|PDB:2NN6}.
HELIX 94 109 {ECO:0000244|PDB:2NN6}.
HELIX 113 115 {ECO:0000244|PDB:2NN6}.
STRAND 119 129 {ECO:0000244|PDB:2NN6}.
HELIX 134 148 {ECO:0000244|PDB:2NN6}.
STRAND 158 165 {ECO:0000244|PDB:2NN6}.
STRAND 168 172 {ECO:0000244|PDB:2NN6}.
HELIX 175 178 {ECO:0000244|PDB:2NN6}.
STRAND 185 189 {ECO:0000244|PDB:2NN6}.
TURN 191 193 {ECO:0000244|PDB:2NN6}.
STRAND 198 201 {ECO:0000244|PDB:2NN6}.
HELIX 210 239 {ECO:0000244|PDB:2NN6}.
SEQUENCE 245 AA; 26383 MW; 7A24E97897DAF313 CRC64;
MAGLELLSDQ GYRVDGRRAG ELRKIQARMG VFAQADGSAY IEQGNTKALA VVYGPHEIRG
SRARALPDRA LVNCQYSSAT FSTGERKRRP HGDRKSCEMG LQLRQTFEAA ILTQLHPRSQ
IDIYVQVLQA DGGTYAACVN AATLAVLDAG IPMRDFVCAC SAGFVDGTAL ADLSHVEEAA
GGPQLALALL PASGQIALLE MDARLHEDHL ERVLEAAAQA ARDVHTLLDR VVRQHVREAS
ILLGD


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EIAAB13491 Exosc4,Exosome complex component RRP41,Exosome component 4,Mouse,Mus musculus,Ribosomal RNA-processing protein 41,Rrp41
EIAAB13498 Bos taurus,Bovine,EXOSC8,Exosome complex component RRP43,Exosome component 8,Ribosomal RNA-processing protein 43
EIAAB13496 EXOSC7,Exosome complex component RRP42,Exosome component 7,Homo sapiens,Human,KIAA0116,p8,Ribosomal RNA-processing protein 42,RRP42
EIAAB13493 D7Wsu180e,Exosc5,Exosome complex component RRP46,Exosome component 5,Mouse,Mus musculus,Ribosomal RNA-processing protein 46,Rrp46
EIAAB13485 EXOSC2,Exosome complex component RRP4,Exosome component 2,Homo sapiens,Human,Ribosomal RNA-processing protein 4,RRP4
EIAAB13488 CGI-102,EXOSC3,Exosome complex component RRP40,Exosome component 3,Homo sapiens,Human,p10,Ribosomal RNA-processing protein 40,RRP40
EIAAB13486 Bos taurus,Bovine,EXOSC3,Exosome complex component RRP40,Exosome component 3,Ribosomal RNA-processing protein 40,RRP40
EIAAB13484 Bos taurus,Bovine,EXOSC2,Exosome complex component RRP4,Exosome component 2,Ribosomal RNA-processing protein 4,RRP4
EIAAB13483 Exosc2,Exosome complex component RRP4,Exosome component 2,Mouse,Mus musculus,Ribosomal RNA-processing protein 4,Rrp4
EIAAB13487 Exosc3,Exosome complex component RRP40,Exosome component 3,Mouse,Mus musculus,Ribosomal RNA-processing protein 40,Rrp40
EIAAB13499 Exosc8,Exosome complex component RRP43,Exosome component 8,Mouse,Mus musculus,Ribosomal RNA-processing protein 43,Rrp43
EIAAB13492 Chronic myelogenous leukemia tumor antigen 28,CML28,EXOSC5,Exosome complex component RRP46,Exosome component 5,Homo sapiens,Human,p12B,Ribosomal RNA-processing protein 46,RRP46
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
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
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
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
EXOS4_HUMAN Human ELISA Kit FOR Exosome complex component RRP41 96T
EIAAB13504 Exosc9,Exosome complex component RRP45,Exosome component 9,Rat,Rattus norvegicus
EIAAB13501 Bos taurus,Bovine,EXOSC9,Exosome complex component RRP45,Exosome component 9
CSB-EL007892HU Human Exosome complex component RRP41(EXOSC4) ELISA kit 96T


 

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