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Exosome complex component RRP43 (Ribosomal RNA-processing protein 43)

 RRP43_YEAST             Reviewed;         394 AA.
P25359; D6VR45; Q8NKJ5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
27-JUN-2003, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Exosome complex component RRP43;
AltName: Full=Ribosomal RNA-processing protein 43;
Name=RRP43; OrderedLocusNames=YCR035C; ORFNames=YCR35C, YCR522;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=1964349; DOI=10.1002/yea.320060609;
Thierry A., Fairhead C., Dujon B.;
"The complete sequence of the 8.2 kb segment left of MAT on chromosome
III reveals five ORFs, including a gene for a yeast ribokinase.";
Yeast 6:521-534(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[3]
SEQUENCE REVISION TO 102 AND 363.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 25-33, FUNCTION, SUBUNIT, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=9390555; DOI=10.1016/S0092-8674(00)80432-8;
Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.;
"The exosome: a conserved eukaryotic RNA processing complex containing
multiple 3'-->5' exoribonucleases.";
Cell 91:457-466(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-394.
PubMed=1776366; DOI=10.1002/yea.320070711;
Wicksteed B.L., Roberts A.B., Sagliocco F.A., Brown A.J.P.;
"The complete sequence of a 7.5 kb region of chromosome III from
Saccharomyces cerevisiae that lies between CRY1 and MAT.";
Yeast 7:761-772(1991).
[7]
IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS SPECTROMETRY.
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).
[8]
FUNCTION.
PubMed=9973615; DOI=10.1093/nar/27.5.1283;
Zanchin N.I., Goldfarb D.S.;
"The exosome subunit Rrp43p is required for the efficient maturation
of 5.8S, 18S and 25S rRNA.";
Nucleic Acids Res. 27:1283-1288(1999).
[9]
FUNCTION, INTERACTION WITH RRP46, AND MUTAGENESIS OF SER-162; VAL-212;
CYS-230; ALA-246; ILE-274 AND CYS-276.
PubMed=12364597; DOI=10.1093/nar/gkf545;
Oliveira C.C., Gonzales F.A., Zanchin N.I.;
"Temperature-sensitive mutants of the exosome subunit Rrp43p show a
deficiency in mRNA degradation and no longer interact with the
exosome.";
Nucleic Acids Res. 30:4186-4198(2002).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
RECONSTITUTION OF THE RNA EXOSOME COMPLEX, AND LACK OF EXONUCLEASE
ACTIVITY.
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).
[13]
ERRATUM.
Liu Q., Greimann J.C., Lima C.D.;
Cell 131:188-189(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME
COMPLEX, AND SUBUNIT.
PubMed=17173052; DOI=10.1038/nsmb1184;
Dziembowski A., Lorentzen E., Conti E., Seraphin B.;
"A single subunit, Dis3, is essentially responsible for yeast exosome
core activity.";
Nat. Struct. Mol. Biol. 14:15-22(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[16]
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).
-!- 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 cryptic
unstable transcripts (CUTs), and of mRNAs with processing defects,
thereby limiting or excluding their export to the cytoplasm. In
the cytoplasm, the RNA exosome complex is involved in general mRNA
turnover and in RNA surveillance pathways, preventing translation
of aberrant mRNAs. 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. RRP43 is part of the hexameric
ring of RNase PH domain-containing subunits proposed to form a
central channel which threads RNA substrates for degradation.
{ECO:0000269|PubMed:12364597, ECO:0000269|PubMed:17173052,
ECO:0000269|PubMed:9390555, ECO:0000269|PubMed:9973615}.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which associates with catalytic subunits DIS3 and RRP6 in
cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9
is formed by a hexameric ring of RNase PH domain-containing
subunits and peripheral S1 domain-containing components CSL4, RRP4
and RRP40 located on the top of the ring structure. Interacts with
NIP7 and NOP8. Interacts strongly with RRP46.
{ECO:0000269|PubMed:10465791, ECO:0000269|PubMed:12364597,
ECO:0000269|PubMed:17173052, ECO:0000269|PubMed:9390555}.
-!- INTERACTION:
P53859:CSL4; NbExp=18; IntAct=EBI-1773, EBI-1731;
Q08162:DIS3; NbExp=15; IntAct=EBI-1773, EBI-1740;
P48240:MTR3; NbExp=10; IntAct=EBI-1773, EBI-1749;
P47047:MTR4; NbExp=5; IntAct=EBI-1773, EBI-11592;
Q08962:NIP7; NbExp=5; IntAct=EBI-1773, EBI-12067;
P38768:PIH1; NbExp=2; IntAct=EBI-1773, EBI-24499;
P38792:RRP4; NbExp=6; IntAct=EBI-1773, EBI-1757;
Q12277:RRP42; NbExp=4; IntAct=EBI-1773, EBI-1765;
Q05636:RRP45; NbExp=9; IntAct=EBI-1773, EBI-1810;
P53256:RRP46; NbExp=9; IntAct=EBI-1773, EBI-1842;
Q12149:RRP6; NbExp=8; IntAct=EBI-1773, EBI-1782;
P35207:SKI2; NbExp=2; IntAct=EBI-1773, EBI-1851;
P46948:SKI6; NbExp=5; IntAct=EBI-1773, EBI-1788;
Q08491:SKI7; NbExp=5; IntAct=EBI-1773, EBI-1389;
Q02821:SRP1; NbExp=2; IntAct=EBI-1773, EBI-1797;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
-!- CAUTION: According to PubMed:17173052 and PubMed:17174896, only
DIS3/RRP44 subunit of the exosome core has exonuclease activity.
{ECO:0000305}.
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EMBL; X56909; CAA40227.1; -; Genomic_DNA.
EMBL; X59720; CAC42984.1; -; Genomic_DNA.
EMBL; S78624; AAB21261.1; -; Genomic_DNA.
EMBL; BK006937; DAA07514.1; -; Genomic_DNA.
PIR; S12917; S12917.
RefSeq; NP_009964.2; NM_001178749.1.
PDB; 4IFD; X-ray; 2.80 A; C=2-394.
PDB; 4OO1; X-ray; 3.30 A; C=1-394.
PDB; 5C0W; X-ray; 4.60 A; C=1-394.
PDB; 5C0X; X-ray; 3.81 A; C=1-394.
PDB; 5G06; EM; 4.20 A; C=1-394.
PDB; 5JEA; X-ray; 2.65 A; C=1-394.
PDB; 5K36; X-ray; 3.10 A; C=1-394.
PDB; 5OKZ; X-ray; 3.20 A; C/M/W/g=1-394.
PDB; 5VZJ; X-ray; 3.30 A; C=1-394.
PDB; 6FSZ; EM; 4.60 A; CC=2-394.
PDBsum; 4IFD; -.
PDBsum; 4OO1; -.
PDBsum; 5C0W; -.
PDBsum; 5C0X; -.
PDBsum; 5G06; -.
PDBsum; 5JEA; -.
PDBsum; 5K36; -.
PDBsum; 5OKZ; -.
PDBsum; 5VZJ; -.
PDBsum; 6FSZ; -.
ProteinModelPortal; P25359; -.
SMR; P25359; -.
BioGrid; 31018; 134.
ComplexPortal; CPX-599; Nuclear/nucleolar exosome complex, DIS3-RRP6 variant.
ComplexPortal; CPX-603; Cytoplasmic exosome complex, DIS3 variant.
DIP; DIP-5485N; -.
IntAct; P25359; 31.
MINT; P25359; -.
STRING; 4932.YCR035C; -.
iPTMnet; P25359; -.
MaxQB; P25359; -.
PaxDb; P25359; -.
PRIDE; P25359; -.
EnsemblFungi; CAC42984; CAC42984; CAC42984.
EnsemblFungi; YCR035C; YCR035C; YCR035C.
GeneID; 850401; -.
KEGG; sce:YCR035C; -.
EuPathDB; FungiDB:YCR035C; -.
SGD; S000000631; RRP43.
HOGENOM; HOG000057141; -.
InParanoid; P25359; -.
KO; K12586; -.
OMA; YVLYAKI; -.
OrthoDB; EOG092C5179; -.
BioCyc; YEAST:G3O-29348-MONOMER; -.
PRO; PR:P25359; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:SGD.
GO; GO:0000176; C:nuclear exosome (RNase complex); IDA:SGD.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; IDA:SGD.
GO; GO:0017091; F:AU-rich element binding; IBA:GO_Central.
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); IMP:SGD.
GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
GO; GO:0043628; P:ncRNA 3'-end processing; IC:SGD.
GO; GO:0070651; P:nonfunctional rRNA decay; IC:SGD.
GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IC:SGD.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IMP:SGD.
GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IC:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IC:SGD.
GO; GO:0016072; P:rRNA metabolic process; IMP:UniProtKB.
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; IPR027408; PNPase/RNase_PH_dom_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR033196; Rrp43.
PANTHER; PTHR11097:SF9; PTHR11097:SF9; 1.
Pfam; PF01138; RNase_PH; 1.
SUPFAM; SSF54211; SSF54211; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Exosome; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 394 Exosome complex component RRP43.
/FTId=PRO_0000139970.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 162 162 S->F: Interaction with RRP46 abolished;
when associated with T-246.
{ECO:0000269|PubMed:12364597}.
MUTAGEN 212 212 V->A: Interaction with RRP46 abolished.
{ECO:0000269|PubMed:12364597}.
MUTAGEN 230 230 C->Y: Interaction with RRP46 abolished;
when associated with T-274 and Y-276.
{ECO:0000269|PubMed:12364597}.
MUTAGEN 246 246 A->T: Interaction with RRP46 abolished;
when associated with F-162.
{ECO:0000269|PubMed:12364597}.
MUTAGEN 274 274 I->T: Interaction with RRP46 abolished;
when associated with Y-230 and Y-276.
{ECO:0000269|PubMed:12364597}.
MUTAGEN 276 276 C->Y: Interaction with RRP46 abolished;
when associated with Y-230 and T-274.
{ECO:0000269|PubMed:12364597}.
CONFLICT 102 102 A -> S (in Ref. 1; CAA40227).
{ECO:0000305}.
CONFLICT 363 363 V -> M (in Ref. 1; CAA40227).
{ECO:0000305}.
STRAND 10 12 {ECO:0000244|PDB:4IFD}.
HELIX 19 25 {ECO:0000244|PDB:5JEA}.
HELIX 27 35 {ECO:0000244|PDB:5JEA}.
TURN 36 38 {ECO:0000244|PDB:5JEA}.
STRAND 48 50 {ECO:0000244|PDB:4IFD}.
STRAND 52 60 {ECO:0000244|PDB:5JEA}.
HELIX 61 63 {ECO:0000244|PDB:4OO1}.
STRAND 65 67 {ECO:0000244|PDB:5JEA}.
STRAND 75 82 {ECO:0000244|PDB:5JEA}.
STRAND 85 97 {ECO:0000244|PDB:5JEA}.
HELIX 103 106 {ECO:0000244|PDB:5K36}.
HELIX 109 118 {ECO:0000244|PDB:5K36}.
HELIX 124 126 {ECO:0000244|PDB:5JEA}.
STRAND 131 136 {ECO:0000244|PDB:5JEA}.
HELIX 146 161 {ECO:0000244|PDB:5JEA}.
HELIX 167 170 {ECO:0000244|PDB:5JEA}.
STRAND 175 180 {ECO:0000244|PDB:5JEA}.
TURN 181 183 {ECO:0000244|PDB:5JEA}.
STRAND 184 188 {ECO:0000244|PDB:5JEA}.
STRAND 209 221 {ECO:0000244|PDB:5JEA}.
HELIX 227 239 {ECO:0000244|PDB:5JEA}.
STRAND 242 248 {ECO:0000244|PDB:5JEA}.
STRAND 257 260 {ECO:0000244|PDB:4IFD}.
STRAND 265 268 {ECO:0000244|PDB:4IFD}.
STRAND 275 283 {ECO:0000244|PDB:5JEA}.
HELIX 288 290 {ECO:0000244|PDB:5JEA}.
STRAND 293 302 {ECO:0000244|PDB:5JEA}.
HELIX 304 306 {ECO:0000244|PDB:5JEA}.
HELIX 322 324 {ECO:0000244|PDB:5K36}.
STRAND 327 333 {ECO:0000244|PDB:5JEA}.
HELIX 338 342 {ECO:0000244|PDB:5JEA}.
STRAND 345 351 {ECO:0000244|PDB:5JEA}.
TURN 353 355 {ECO:0000244|PDB:5K36}.
STRAND 357 367 {ECO:0000244|PDB:5JEA}.
HELIX 371 390 {ECO:0000244|PDB:5JEA}.
SEQUENCE 394 AA; 44011 MW; 8801837B8184134D CRC64;
MAESTTLETI EIHPITFPPE VLARISPELS LQRHLSLGIR PCLRKYEEFR DVAIENNTLS
RYADAGNIDT KNNILGSNVL KSGKTIVITS ITGGIIEETS AAIKDLDDFG EEELFEVTKE
EDIIANYASV YPVVEVERGR VGACTDEEMT ISQKLHDSIL HSRILPKKAL KVKAGVRSAN
EDGTFSVLYP DELEDDTLNE TNLKMKRKWS YVLYAKIVVL SRTGPVFDLC WNSLMYALQS
VKLPRAFIDE RASDLRMTIR TRGRSATIRE TYEIICDQTK SVPLMINAKN IAFASNYGIV
ELDPECQLQN SDNSEEEEVD IDMDKLNTVL IADLDTEAEE TSIHSTISIL AAPSGNYKQL
TLVGGGAKIT PEMIKRSLLL SRVRADDLST RFNI


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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
EIAAB13491 Exosc4,Exosome complex component RRP41,Exosome component 4,Mouse,Mus musculus,Ribosomal RNA-processing protein 41,Rrp41
EIAAB13489 Bos taurus,Bovine,EXOSC4,Exosome complex component RRP41,Exosome component 4,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
EIAAB13497 Exosc7,Exosome complex exonuclease RRP42,Exosome component 7,Mouse,Mus musculus,Ribosomal RNA-processing protein 42,Rrp42
EXOS8_BOVIN Bovine ELISA Kit FOR Exosome complex component RRP43 96T
EXOS8_HUMAN Human ELISA Kit FOR Exosome complex component RRP43 96T
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
CSB-EL007896MO Mouse Exosome complex component RRP43(EXOSC8) ELISA kit 96T
CSB-EL007896BO Bovine Exosome complex component RRP43(EXOSC8) ELISA kit 96T


 

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