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Protein argonaute-3 (Argonaute3) (hAgo3) (Argonaute RISC catalytic component 3) (Eukaryotic translation initiation factor 2C 3) (eIF-2C 3) (eIF2C 3)

 AGO3_HUMAN              Reviewed;         860 AA.
Q9H9G7; B1ALI0; Q5TA55; Q9H1U6;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
22-NOV-2017, entry version 129.
RecName: Full=Protein argonaute-3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=Argonaute3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=hAgo3;
AltName: Full=Argonaute RISC catalytic component 3;
AltName: Full=Eukaryotic translation initiation factor 2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=eIF-2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Short=eIF2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
Name=AGO3; Synonyms=EIF2C3;
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] (ISOFORM 1).
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Leukocyte;
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]
ASSOCIATION WITH MIRNA.
PubMed=15260970; DOI=10.1016/j.molcel.2004.07.007;
Meister G., Landthaler M., Patkaniowska A., Dorsett Y., Teng G.,
Tuschl T.;
"Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
siRNAs.";
Mol. Cell 15:185-197(2004).
[5]
SUBCELLULAR LOCATION.
PubMed=16081698; DOI=10.1126/science.1115079;
Pillai R.S., Bhattacharyya S.N., Artus C.G., Zoller T., Cougot N.,
Basyuk E., Bertrand E., Filipowicz W.;
"Inhibition of translational initiation by Let-7 MicroRNA in human
cells.";
Science 309:1573-1576(2005).
[6]
FUNCTION.
PubMed=18771919; DOI=10.1016/j.cub.2008.07.072;
Wu L., Fan J., Belasco J.G.;
"Importance of translation and nonnucleolytic ago proteins for on-
target RNA interference.";
Curr. Biol. 18:1327-1332(2008).
[7]
INTERACTION WITH EIF4B; IMP8; PRMT5 AND TNRC6B.
PubMed=19167051; DOI=10.1016/j.cell.2008.12.023;
Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P.,
Kremmer E., Benes V., Urlaub H., Meister G.;
"Importin 8 is a gene silencing factor that targets argonaute proteins
to distinct mRNAs.";
Cell 136:496-507(2009).
[8]
INTERACTION WITH APOBEC3F; APOBEC3G AND APOBEC3H.
PubMed=22915799; DOI=10.1128/JVI.00595-12;
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
"HIV-1 replication and APOBEC3 antiviral activity are not regulated by
P bodies.";
J. Virol. 86:11712-11724(2012).
[9]
FUNCTION, AND INTERACTION WITH EDC4.
PubMed=23064648; DOI=10.1038/nsmb.2400;
Hu Q., Tanasa B., Trabucchi M., Li W., Zhang J., Ohgi K.A., Rose D.W.,
Glass C.K., Rosenfeld M.G.;
"DICER- and AGO3-dependent generation of retinoic acid-induced DR2 Alu
RNAs regulates human stem cell proliferation.";
Nat. Struct. Mol. Biol. 19:1168-1175(2012).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, 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).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
to short RNAs such as microRNAs (miRNAs) and represses the
translation of mRNAs which are complementary to them. Lacks
endonuclease activity and does not appear to cleave target mRNAs.
Proposed to be involved in stabilization of small RNA derivates
(riRNA) derived from processed RNA polymerase III-transcribed Alu
repeats containing a DR2 retinoic acid response element (RARE) in
stem cells and in the subsequent riRNA-dependent degradation of a
subset of RNA polymerase II-transcribed coding mRNAs by recruiting
a mRNA decapping complex involving EDC4. {ECO:0000255|HAMAP-
Rule:MF_03032, ECO:0000269|PubMed:18771919,
ECO:0000269|PubMed:23064648}.
-!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5 and TNRC6B. Interacts
with APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4.
{ECO:0000255|HAMAP-Rule:MF_03032, ECO:0000269|PubMed:19167051,
ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23064648}.
-!- INTERACTION:
Q6P2E9:EDC4; NbExp=2; IntAct=EBI-2267883, EBI-1006038;
O15397:IPO8; NbExp=5; IntAct=EBI-2267883, EBI-358808;
P53041:PPP5C; NbExp=2; IntAct=EBI-2267883, EBI-716663;
Q8NDV7:TNRC6A; NbExp=3; IntAct=EBI-2267883, EBI-2269715;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03032, ECO:0000269|PubMed:16081698}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H9G7-1; Sequence=Displayed;
Name=2;
IsoId=Q9H9G7-2; Sequence=VSP_041084;
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03032}.
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EMBL; AK022827; BAB14262.1; -; mRNA.
EMBL; AL139286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025769; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS399.1; -. [Q9H9G7-1]
CCDS; CCDS400.1; -. [Q9H9G7-2]
RefSeq; NP_079128.2; NM_024852.3. [Q9H9G7-1]
RefSeq; NP_803171.1; NM_177422.2. [Q9H9G7-2]
RefSeq; XP_005270632.1; XM_005270575.3. [Q9H9G7-1]
RefSeq; XP_011539184.1; XM_011540882.2. [Q9H9G7-2]
RefSeq; XP_016856012.1; XM_017000523.1. [Q9H9G7-1]
RefSeq; XP_016856013.1; XM_017000524.1. [Q9H9G7-2]
RefSeq; XP_016856014.1; XM_017000525.1. [Q9H9G7-2]
RefSeq; XP_016856015.1; XM_017000526.1. [Q9H9G7-2]
RefSeq; XP_016856016.1; XM_017000527.1. [Q9H9G7-2]
UniGene; Hs.657659; -.
ProteinModelPortal; Q9H9G7; -.
SMR; Q9H9G7; -.
BioGrid; 128177; 69.
DIP; DIP-54486N; -.
IntAct; Q9H9G7; 57.
STRING; 9606.ENSP00000362287; -.
iPTMnet; Q9H9G7; -.
PhosphoSitePlus; Q9H9G7; -.
BioMuta; AGO3; -.
DMDM; 76803660; -.
EPD; Q9H9G7; -.
MaxQB; Q9H9G7; -.
PaxDb; Q9H9G7; -.
PeptideAtlas; Q9H9G7; -.
PRIDE; Q9H9G7; -.
DNASU; 192669; -.
Ensembl; ENST00000246314; ENSP00000246314; ENSG00000126070. [Q9H9G7-2]
Ensembl; ENST00000373191; ENSP00000362287; ENSG00000126070. [Q9H9G7-1]
GeneID; 192669; -.
KEGG; hsa:192669; -.
UCSC; uc001bzp.4; human. [Q9H9G7-1]
CTD; 192669; -.
DisGeNET; 192669; -.
EuPathDB; HostDB:ENSG00000126070.19; -.
GeneCards; AGO3; -.
HGNC; HGNC:18421; AGO3.
HPA; HPA048342; -.
HPA; HPA075436; -.
MIM; 607355; gene.
neXtProt; NX_Q9H9G7; -.
OpenTargets; ENSG00000126070; -.
PharmGKB; PA38329; -.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
InParanoid; Q9H9G7; -.
KO; K11593; -.
OMA; QPANPQY; -.
OrthoDB; EOG091G020J; -.
PhylomeDB; Q9H9G7; -.
TreeFam; TF101510; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
GenomeRNAi; 192669; -.
PRO; PR:Q9H9G7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000126070; -.
CleanEx; HS_EIF2C3; -.
ExpressionAtlas; Q9H9G7; baseline and differential.
Genevisible; Q9H9G7; HS.
GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0035198; F:miRNA binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; TAS:Reactome.
GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0072091; P:regulation of stem cell proliferation; IMP:UniProtKB.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:BHF-UCL.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03032; AGO3; 1.
InterPro; IPR028603; AGO3.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Translation regulation.
CHAIN 1 860 Protein argonaute-3.
/FTId=PRO_0000194061.
DOMAIN 236 349 PAZ. {ECO:0000255|HAMAP-Rule:MF_03032}.
DOMAIN 518 819 Piwi. {ECO:0000255|HAMAP-Rule:MF_03032}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 234 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041084.
CONFLICT 25 25 T -> A (in Ref. 1; BAB14262).
{ECO:0000305}.
SEQUENCE 860 AA; 97360 MW; 6FF1277995E5322E CRC64;
MEIGSAGPAG AQPLLMVPRR PGYGTMGKPI KLLANCFQVE IPKIDVYLYE VDIKPDKCPR
RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDVT LPGEGGKDRP
FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE LDKPISTNPV HAVDVVLRHL PSMKYTPVGR
SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
NGQTVERTVA QYFREKYTLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIKATA RSAPDRQEEI SRLVRSANYE TDPFVQEFQF KVRDEMAHVT GRVLPAPMLQ
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEILKG FTDQLRKISK
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRVGDTL
LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD
RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP
QALAKAVQIH QDTLRTMYFA


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YF-PA22643 anti-Argonaute 3 eIF2C 3 100 ug
EIAAB12703 65 kDa eukaryotic translation initiation factor 2A,CDA02,EIF2A,eIF-2A,Eukaryotic translation initiation factor 2A,Homo sapiens,Human,MSTP004,MSTP089
EIAAB12726 eIF-3 p48,eIF3e,Eif3e,Eif3s6,Eukaryotic translation initiation factor 3 subunit 6,Eukaryotic translation initiation factor 3 subunit E,Int6,Mammary tumor-associated protein INT-6,MMTV integration site
18-003-42779 Probable ATP-dependent RNA helicase DDX48 - EC 3.6.1.-; DEAD box protein 48; Eukaryotic initiation factor 4A-like NUK-34; Nuclear matrix protein 265; hNMP 265; Eukaryotic translation initiation factor 0.1 mg Protein A
EIAAB12755 EIF3EIP,eIF3l,EIF3L,EIF3S6IP,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation initiation factor 3 subunit E-interacting protein,Eukaryotic translation in
25-604 Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three su 0.05 mg
29-272 Translation initiation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three su 0.05 mg
YF-PA26955 anti-Argonaute 3 eIF2C 3 type: Primary antibodies host: Mouse 50 ul
YF-PA22643 anti-Argonaute 3 eIF2C 3 type: Primary antibodies host: Rabbit 100 ug
EIAAB12723 eIF-3 p48,eIF3e,EIF3E,EIF3S6,Eukaryotic translation initiation factor 3 subunit 6,Eukaryotic translation initiation factor 3 subunit E,Homo sapiens,Human,INT6,Viral integration site protein INT-6 homo
EIAAB12753 66 kDa tyrosine-rich heat shock protein,67 kDa polymerase-associated factor,Eif3eip,eIF3l,Eif3l,Eif3s6ip,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation
EIAAB12752 Bos taurus,Bovine,EIF3EIP,eIF3l,EIF3L,EIF3S6IP,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation initiation factor 3 subunit E-interacting protein,Eukaryo
EIAAB12749 ARG134,eIF-3 p25,eIF-3 p28,eIF3k,EIF3K,EIF3S12,Eukaryotic translation initiation factor 3 subunit 12,Eukaryotic translation initiation factor 3 subunit K,Homo sapiens,HSPC029,Human,MSTP001,Muscle-spec
EIAAB12748 eIF3 p35,eIF-3-alpha,eIF3j,EIF3J,EIF3S1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J,Homo sapiens,Human,PRO0391
EIAAB12721 eIF3 p66,eIF3d,EIF3D,EIF3S7,eIF-3-zeta,Eukaryotic translation initiation factor 3 subunit 7,Eukaryotic translation initiation factor 3 subunit D,Homo sapiens,Human
EIAAB12715 eIF3 p110,eIF3c,EIF3C,EIF3S8,Eukaryotic translation initiation factor 3 subunit 8,Eukaryotic translation initiation factor 3 subunit C,Homo sapiens,Human
EIAAB12743 eIF3 p36,eIF-3-beta,eIF3i,EIF3I,EIF3S2,Eukaryotic translation initiation factor 3 subunit 2,Eukaryotic translation initiation factor 3 subunit I,Oryctolagus cuniculus,Rabbit
EIAAB12729 eIF3 p47,eIF-3-epsilon,eIF3f,EIF3F,EIF3S5,Eukaryotic translation initiation factor 3 subunit 5,Eukaryotic translation initiation factor 3 subunit F,Homo sapiens,Human


 

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