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Exosome complex component RRP43 (Exosome component 8) (Opa-interacting protein 2) (OIP-2) (Ribosomal RNA-processing protein 43) (p9)

 EXOS8_HUMAN             Reviewed;         276 AA.
Q96B26; O43480; Q5TBA5;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=Exosome complex component RRP43;
AltName: Full=Exosome component 8;
AltName: Full=Opa-interacting protein 2;
Short=OIP-2;
AltName: Full=Ribosomal RNA-processing protein 43;
AltName: Full=p9;
Name=EXOSC8; Synonyms=OIP2, RRP43;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[2]
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-276.
PubMed=9466265; DOI=10.1046/j.1365-2958.1998.00670.x;
Williams J.M., Chen G.-C., Zhu L., Rest R.F.;
"Using the yeast two-hybrid system to identify human epithelial cell
proteins that bind gonococcal Opa proteins: intracellular gonococci
bind pyruvate kinase via their Opa proteins and require host pyruvate
for growth.";
Mol. Microbiol. 27:171-186(1998).
[5]
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).
[6]
PROTEIN INTERACTION.
PubMed=12419256; DOI=10.1016/S0022-2836(02)00947-6;
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions between human exosome components support
the assembly of RNase PH-type subunits into a six-membered PNPase-like
ring.";
J. Mol. Biol. 323:653-663(2002).
[7]
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).
[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]
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).
[11]
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).
[12]
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).
[13]
INVOLVEMENT IN PCH1C, AND VARIANTS PCH1C VAL-2 AND THR-272.
PubMed=24989451; DOI=10.1038/ncomms5287;
Boczonadi V., Muller J.S., Pyle A., Munkley J., Dor T., Quartararo J.,
Ferrero I., Karcagi V., Giunta M., Polvikoski T., Birchall D.,
Princzinger A., Cinnamon Y., Lutzkendorf S., Piko H., Reza M.,
Florez L., Santibanez-Koref M., Griffin H., Schuelke M., Elpeleg O.,
Kalaydjieva L., Lochmuller H., Elliott D.J., Chinnery P.F.,
Edvardson S., Horvath R.;
"EXOSC8 mutations alter mRNA metabolism and cause hypomyelination with
spinal muscular atrophy and cerebellar hypoplasia.";
Nat. Commun. 5:4287-4287(2014).
[14]
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).
[15]
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. EXOSC8 binds to ARE-containing RNAs.
{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. Binds outer
membrane protein opap from Neisseria gonorrhoeae.
{ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:20531389}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-371922, EBI-371922;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-371922, EBI-8637627;
P15336:ATF2; NbExp=3; IntAct=EBI-371922, EBI-1170906;
Q86Y22:COL23A1; NbExp=3; IntAct=EBI-371922, EBI-373279;
P20674:COX5A; NbExp=3; IntAct=EBI-371922, EBI-715032;
Q9BVJ7:DUSP23; NbExp=10; IntAct=EBI-371922, EBI-724940;
Q9Y3B2:EXOSC1; NbExp=5; IntAct=EBI-371922, EBI-371892;
Q9NQT5:EXOSC3; NbExp=3; IntAct=EBI-371922, EBI-371866;
Q9NQT4:EXOSC5; NbExp=14; IntAct=EBI-371922, EBI-371876;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-371922, EBI-6658203;
Q14331:FRG1; NbExp=3; IntAct=EBI-371922, EBI-2515248;
Q8TBB1:LNX1; NbExp=8; IntAct=EBI-371922, EBI-739832;
Q8WVZ3:MORN4; NbExp=3; IntAct=EBI-371922, EBI-10277137;
Q01804:OTUD4; NbExp=5; IntAct=EBI-371922, EBI-1054396;
Q9Y272:RASD1; NbExp=4; IntAct=EBI-371922, EBI-740818;
Q04864:REL; NbExp=3; IntAct=EBI-371922, EBI-307352;
Q5TAL4:SNRPC; NbExp=3; IntAct=EBI-371922, EBI-10246938;
Q15560:TCEA2; NbExp=3; IntAct=EBI-371922, EBI-710310;
Q86VL0:TCEA2; NbExp=3; IntAct=EBI-371922, EBI-10259904;
Q01664:TFAP4; NbExp=5; IntAct=EBI-371922, EBI-2514218;
Q9BRA2:TXNDC17; NbExp=5; IntAct=EBI-371922, EBI-1055906;
O14530:TXNDC9; NbExp=5; IntAct=EBI-371922, EBI-707554;
Q06250:WT1-AS; NbExp=4; IntAct=EBI-371922, EBI-10223946;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}.
Nucleus {ECO:0000269|PubMed:17545563}. Nucleus, nucleolus
{ECO:0000250}.
-!- DISEASE: Pontocerebellar hypoplasia 1C (PCH1C) [MIM:616081]: A
severe autosomal recessive neurodegenerative disease characterized
by cerebellar and corpus callosum hypoplasia, abnormal myelination
of the central nervous system, and spinal motor neuron disease.
Affected individuals manifest failure to thrive, severe muscle
weakness, spasticity and psychomotor retardation. Vision and
hearing are impaired. {ECO:0000269|PubMed:24989451}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. EXOSC8 dysfunction causes myelin disruption through an
imbalanced supply of myelin proteins due to dysregulation of their
ARE-containing mRNAs (PubMed:24989451).
{ECO:0000269|PubMed:24989451}.
-!- 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=CAI14013.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAX08581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL138706; CAI14013.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471075; EAX08581.1; ALT_SEQ; Genomic_DNA.
EMBL; BC020773; AAH20773.1; -; mRNA.
EMBL; AF025438; AAC39558.1; -; mRNA.
CCDS; CCDS31958.1; -.
RefSeq; NP_852480.1; NM_181503.2.
UniGene; Hs.294041; -.
PDB; 2NN6; X-ray; 3.35 A; C=1-276.
PDBsum; 2NN6; -.
ProteinModelPortal; Q96B26; -.
SMR; Q96B26; -.
BioGrid; 116468; 68.
CORUM; Q96B26; -.
DIP; DIP-31133N; -.
IntAct; Q96B26; 80.
MINT; MINT-4536555; -.
STRING; 9606.ENSP00000374354; -.
iPTMnet; Q96B26; -.
PhosphoSitePlus; Q96B26; -.
BioMuta; EXOSC8; -.
DMDM; 21759409; -.
SWISS-2DPAGE; Q96B26; -.
EPD; Q96B26; -.
MaxQB; Q96B26; -.
PaxDb; Q96B26; -.
PeptideAtlas; Q96B26; -.
PRIDE; Q96B26; -.
TopDownProteomics; Q96B26; -.
DNASU; 11340; -.
Ensembl; ENST00000389704; ENSP00000374354; ENSG00000120699.
GeneID; 11340; -.
KEGG; hsa:11340; -.
UCSC; uc001uwa.5; human.
CTD; 11340; -.
DisGeNET; 11340; -.
EuPathDB; HostDB:ENSG00000120699.12; -.
GeneCards; EXOSC8; -.
HGNC; HGNC:17035; EXOSC8.
HPA; CAB034240; -.
HPA; HPA039702; -.
HPA; HPA043942; -.
MalaCards; EXOSC8; -.
MIM; 606019; gene.
MIM; 616081; phenotype.
neXtProt; NX_Q96B26; -.
OpenTargets; ENSG00000120699; -.
Orphanet; 2254; Pontocerebellar hypoplasia type 1.
PharmGKB; PA134922251; -.
eggNOG; KOG1613; Eukaryota.
eggNOG; COG2123; LUCA.
GeneTree; ENSGT00530000063093; -.
HOGENOM; HOG000229504; -.
HOVERGEN; HBG051522; -.
InParanoid; Q96B26; -.
KO; K12586; -.
OMA; NPFDAAW; -.
OrthoDB; EOG091G0JEJ; -.
PhylomeDB; Q96B26; -.
TreeFam; TF320415; -.
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; Q96B26; -.
GeneWiki; Exosome_component_8; -.
GenomeRNAi; 11340; -.
PRO; PR:Q96B26; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000120699; -.
CleanEx; HS_EXOSC8; -.
ExpressionAtlas; Q96B26; baseline and differential.
Genevisible; Q96B26; 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:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IBA:GO_Central.
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:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
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.
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.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR033196; Rrp43.
PANTHER; PTHR11097:SF9; PTHR11097:SF9; 1.
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; Complete proteome; Cytoplasm;
Disease mutation; Exosome; Neurodegeneration; Nucleus;
Reference proteome; RNA-binding; rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 276 Exosome complex component RRP43.
/FTId=PRO_0000139967.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
VARIANT 2 2 A -> V (in PCH1C; dbSNP:rs606231285).
{ECO:0000269|PubMed:24989451}.
/FTId=VAR_072558.
VARIANT 272 272 S -> T (in PCH1C; dbSNP:rs36027220).
{ECO:0000269|PubMed:24989451}.
/FTId=VAR_072559.
CONFLICT 265 276 LMDEVIKSMKPK -> TDG (in Ref. 4;
AAC39558). {ECO:0000305}.
HELIX 11 19 {ECO:0000244|PDB:2NN6}.
STRAND 37 39 {ECO:0000244|PDB:2NN6}.
STRAND 43 53 {ECO:0000244|PDB:2NN6}.
STRAND 56 66 {ECO:0000244|PDB:2NN6}.
STRAND 71 73 {ECO:0000244|PDB:2NN6}.
STRAND 80 84 {ECO:0000244|PDB:2NN6}.
STRAND 87 89 {ECO:0000244|PDB:2NN6}.
STRAND 95 97 {ECO:0000244|PDB:2NN6}.
HELIX 100 116 {ECO:0000244|PDB:2NN6}.
HELIX 121 124 {ECO:0000244|PDB:2NN6}.
STRAND 126 128 {ECO:0000244|PDB:2NN6}.
STRAND 133 143 {ECO:0000244|PDB:2NN6}.
HELIX 150 161 {ECO:0000244|PDB:2NN6}.
STRAND 172 175 {ECO:0000244|PDB:2NN6}.
STRAND 194 200 {ECO:0000244|PDB:2NN6}.
TURN 202 204 {ECO:0000244|PDB:2NN6}.
STRAND 207 209 {ECO:0000244|PDB:2NN6}.
TURN 212 216 {ECO:0000244|PDB:2NN6}.
STRAND 219 226 {ECO:0000244|PDB:2NN6}.
STRAND 232 238 {ECO:0000244|PDB:2NN6}.
HELIX 245 267 {ECO:0000244|PDB:2NN6}.
TURN 268 273 {ECO:0000244|PDB:2NN6}.
SEQUENCE 276 AA; 30040 MW; FC8F5BAE74A1FF55 CRC64;
MAAGFKTVEP LEYYRRFLKE NCRPDGRELG EFRTTTVNIG SISTADGSAL VKLGNTTVIC
GVKAEFAAPS TDAPDKGYVV PNVDLPPLCS SRFRSGPPGE EAQVASQFIA DVIENSQIIQ
KEDLCISPGK LVWVLYCDLI CLDYDGNILD ACTFALLAAL KNVQLPEVTI NEETALAEVN
LKKKSYLNIR THPVATSFAV FDDTLLIVDP TGEEEHLATG TLTIVMDEEG KLCCLHKPGG
SGLTGAKLQD CMSRAVTRHK EVKKLMDEVI KSMKPK


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EIAAB13496 EXOSC7,Exosome complex component RRP42,Exosome component 7,Homo sapiens,Human,KIAA0116,p8,Ribosomal RNA-processing protein 42,RRP42
EIAAB13490 EXOSC4,Exosome complex component RRP41,Exosome component 4,Homo sapiens,Human,p12A,Ribosomal RNA-processing protein 41,RRP41,SKI6
EIAAB13488 CGI-102,EXOSC3,Exosome complex component RRP40,Exosome component 3,Homo sapiens,Human,p10,Ribosomal RNA-processing protein 40,RRP40
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
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
EIAAB13487 Exosc3,Exosome complex component RRP40,Exosome component 3,Mouse,Mus musculus,Ribosomal RNA-processing protein 40,Rrp40
EIAAB13489 Bos taurus,Bovine,EXOSC4,Exosome complex component RRP41,Exosome component 4,Ribosomal RNA-processing protein 41,RRP41
EIAAB13483 Exosc2,Exosome complex component RRP4,Exosome component 2,Mouse,Mus musculus,Ribosomal RNA-processing protein 4,Rrp4
EIAAB13491 Exosc4,Exosome complex component RRP41,Exosome component 4,Mouse,Mus musculus,Ribosomal RNA-processing protein 41,Rrp41
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
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
20-372-60232 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
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
EXOS8_HUMAN Human ELISA Kit FOR Exosome complex component RRP43 96T
EXOS8_BOVIN Bovine ELISA Kit FOR Exosome complex component RRP43 96T
EIAAB13501 Bos taurus,Bovine,EXOSC9,Exosome complex component RRP45,Exosome component 9
EIAAB13504 Exosc9,Exosome complex component RRP45,Exosome component 9,Rat,Rattus norvegicus


 

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