Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Exosome complex component CSL4 (Exosome component 1)

 EXOS1_HUMAN             Reviewed;         195 AA.
Q9Y3B2; B2R9B3; Q5JTH3;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 159.
RecName: Full=Exosome complex component CSL4;
AltName: Full=Exosome component 1;
Name=EXOSC1; Synonyms=CSL4; ORFNames=CGI-108;
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 MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[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=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[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]
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).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC5; EXOSC7 AND EXOSC10.
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]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, 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).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, 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).
[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]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-98, 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).
[17]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), 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).
[18]
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. EXOSC1 as peripheral part of the Exo-9 complex
stabilizes the hexameric ring of RNase PH-domain subunits through
contacts with EXOSC6 and EXOSC8.
-!- 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
EXOSC5, EXOSC7 and EXOSC10. Interacts with DDX60.
{ECO:0000269|PubMed:11719186, ECO:0000269|PubMed:11812149,
ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:21791617}.
-!- INTERACTION:
Q9NPD3:EXOSC4; NbExp=7; IntAct=EBI-371892, EBI-371823;
Q9NQT4:EXOSC5; NbExp=25; IntAct=EBI-371892, EBI-371876;
Q15024:EXOSC7; NbExp=8; IntAct=EBI-371892, EBI-371841;
Q96B26:EXOSC8; NbExp=5; IntAct=EBI-371892, EBI-371922;
Q49A26-4:GLYR1; NbExp=4; IntAct=EBI-371892, EBI-12143817;
Q719H9:KCTD1; NbExp=5; IntAct=EBI-371892, EBI-9027502;
Q9P286:PAK5; NbExp=3; IntAct=EBI-371892, EBI-741896;
Q04864:REL; NbExp=3; IntAct=EBI-371892, EBI-307352;
Q04864-2:REL; NbExp=4; IntAct=EBI-371892, EBI-10829018;
P15884:TCF4; NbExp=3; IntAct=EBI-371892, EBI-533224;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11812149}. Nucleus
{ECO:0000305|PubMed:11812149}. Cytoplasm
{ECO:0000305|PubMed:11812149}.
-!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF151866; AAD34103.1; -; mRNA.
EMBL; AK313717; BAG36460.1; -; mRNA.
EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49936.1; -; Genomic_DNA.
EMBL; BC022067; AAH22067.1; -; mRNA.
CCDS; CCDS7459.1; -.
RefSeq; NP_001305291.1; NM_001318362.1.
RefSeq; NP_001305292.1; NM_001318363.1.
RefSeq; NP_001305293.1; NM_001318364.1.
RefSeq; NP_001305294.1; NM_001318365.1.
RefSeq; NP_001305295.1; NM_001318366.1.
RefSeq; NP_057130.1; NM_016046.4.
UniGene; Hs.632089; -.
PDB; 2NN6; X-ray; 3.35 A; I=1-195.
PDBsum; 2NN6; -.
ProteinModelPortal; Q9Y3B2; -.
BioGrid; 119220; 61.
CORUM; Q9Y3B2; -.
DIP; DIP-31261N; -.
IntAct; Q9Y3B2; 59.
MINT; MINT-3085607; -.
STRING; 9606.ENSP00000359939; -.
iPTMnet; Q9Y3B2; -.
PhosphoSitePlus; Q9Y3B2; -.
BioMuta; EXOSC1; -.
DMDM; 14285410; -.
EPD; Q9Y3B2; -.
MaxQB; Q9Y3B2; -.
PaxDb; Q9Y3B2; -.
PeptideAtlas; Q9Y3B2; -.
PRIDE; Q9Y3B2; -.
DNASU; 51013; -.
Ensembl; ENST00000370902; ENSP00000359939; ENSG00000171311.
GeneID; 51013; -.
KEGG; hsa:51013; -.
UCSC; uc001kni.4; human.
CTD; 51013; -.
DisGeNET; 51013; -.
EuPathDB; HostDB:ENSG00000171311.12; -.
GeneCards; EXOSC1; -.
HGNC; HGNC:17286; EXOSC1.
HPA; HPA038370; -.
MIM; 606493; gene.
neXtProt; NX_Q9Y3B2; -.
OpenTargets; ENSG00000171311; -.
PharmGKB; PA134900737; -.
eggNOG; KOG3409; Eukaryota.
eggNOG; COG1096; LUCA.
GeneTree; ENSGT00390000015287; -.
HOGENOM; HOG000177330; -.
HOVERGEN; HBG051516; -.
InParanoid; Q9Y3B2; -.
KO; K07573; -.
OMA; KPGFHLT; -.
OrthoDB; EOG091G0NLQ; -.
PhylomeDB; Q9Y3B2; -.
TreeFam; TF316607; -.
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; EXOSC1; human.
EvolutionaryTrace; Q9Y3B2; -.
GeneWiki; Exosome_component_1; -.
GenomeRNAi; 51013; -.
PRO; PR:Q9Y3B2; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000171311; -.
CleanEx; HS_EXOSC1; -.
ExpressionAtlas; Q9Y3B2; baseline and differential.
Genevisible; Q9Y3B2; HS.
GO; GO:0005737; C:cytoplasm; 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:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
InterPro; IPR019495; EXOSC1.
InterPro; IPR025721; Exosome_cplx_N_dom.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
Pfam; PF14382; ECR1_N; 1.
Pfam; PF10447; EXOSC1; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Exosome; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
CHAIN 1 195 Exosome complex component CSL4.
/FTId=PRO_0000087127.
DOMAIN 66 147 S1 motif.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
STRAND 13 16 {ECO:0000244|PDB:2NN6}.
TURN 17 19 {ECO:0000244|PDB:2NN6}.
STRAND 23 25 {ECO:0000244|PDB:2NN6}.
STRAND 27 29 {ECO:0000244|PDB:2NN6}.
STRAND 32 34 {ECO:0000244|PDB:2NN6}.
STRAND 41 45 {ECO:0000244|PDB:2NN6}.
STRAND 49 52 {ECO:0000244|PDB:2NN6}.
STRAND 70 78 {ECO:0000244|PDB:2NN6}.
STRAND 80 93 {ECO:0000244|PDB:2NN6}.
STRAND 103 106 {ECO:0000244|PDB:2NN6}.
HELIX 107 109 {ECO:0000244|PDB:2NN6}.
HELIX 118 120 {ECO:0000244|PDB:2NN6}.
STRAND 124 135 {ECO:0000244|PDB:2NN6}.
STRAND 142 145 {ECO:0000244|PDB:2NN6}.
STRAND 148 150 {ECO:0000244|PDB:2NN6}.
STRAND 159 161 {ECO:0000244|PDB:2NN6}.
STRAND 165 168 {ECO:0000244|PDB:2NN6}.
STRAND 171 173 {ECO:0000244|PDB:2NN6}.
TURN 175 178 {ECO:0000244|PDB:2NN6}.
SEQUENCE 195 AA; 21452 MW; E9C3B0A66F911195 CRC64;
MAPPVRYCIP GERLCNLEEG SPGSGTYTRH GYIFSSLAGC LMKSSENGAL PVVSVVRETE
SQLLPDVGAI VTCKVSSINS RFAKVHILYV GSMPLKNSFR GTIRKEDVRA TEKDKVEIYK
SFRPGDIVLA KVISLGDAQS NYLLTTAENE LGVVVAHSES GIQMVPISWC EMQCPKTHTK
EFRKVARVQP EFLQT


Related products :

Catalog number Product name Quantity
EIAAB13482 CGI-108,CSL4,EXOSC1,Exosome complex component CSL4,Exosome component 1,Homo sapiens,Human
EIAAB13481 Csl4,Exosc1,Exosome complex component CSL4,Exosome component 1,Mouse,Mus musculus
TBC31_MOUSE Mouse ELISA Kit FOR Exosome complex component CSL4 96T
E0625r Mouse ELISA Kit FOR Exosome complex component CSL4 96T
EIAAB13498 Bos taurus,Bovine,EXOSC8,Exosome complex component RRP43,Exosome component 8,Ribosomal RNA-processing protein 43
CSB-EL007888MO Mouse Exosome complex component CSL4(EXOSC1) ELISA kit 96T
CSB-EL007888HU Human Exosome complex component CSL4(EXOSC1) ELISA kit 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-EL007888HU Human Exosome complex component CSL4(EXOSC1) ELISA kit SpeciesHuman 96T
CSB-EL007888MO Mouse Exosome complex component CSL4(EXOSC1) ELISA kit SpeciesMouse 96T
EXOS1_MOUSE ELISA Kit FOR Exosome complex component CSL4; organism: Mouse; gene name: Exosc1 96T
EIAAB13496 EXOSC7,Exosome complex component RRP42,Exosome component 7,Homo sapiens,Human,KIAA0116,p8,Ribosomal RNA-processing protein 42,RRP42
EIAAB13494 EXOSC6,Exosome complex component MTR3,Exosome component 6,hMtr3,Homo sapiens,Human,mRNA transport regulator 3 homolog,MTR3,p11
EIAAB13490 EXOSC4,Exosome complex component RRP41,Exosome component 4,Homo sapiens,Human,p12A,Ribosomal RNA-processing protein 41,RRP41,SKI6
EIAAB13493 D7Wsu180e,Exosc5,Exosome complex component RRP46,Exosome component 5,Mouse,Mus musculus,Ribosomal RNA-processing protein 46,Rrp46
EIAAB13495 Exosc6,Exosome complex component MTR3,Exosome component 6,Mouse,mRNA transport regulator 3 homolog,Mtr3,Mus musculus
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
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
EIAAB13484 Bos taurus,Bovine,EXOSC2,Exosome complex component RRP4,Exosome component 2,Ribosomal RNA-processing protein 4,RRP4
EIAAB13499 Exosc8,Exosome complex component RRP43,Exosome component 8,Mouse,Mus musculus,Ribosomal RNA-processing protein 43,Rrp43
EIAAB13489 Bos taurus,Bovine,EXOSC4,Exosome complex component RRP41,Exosome component 4,Ribosomal RNA-processing protein 41,RRP41


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur