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Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein)

 IF4E_DROME              Reviewed;         259 AA.
P48598; A4V1Q6; Q95SV3; Q9VSX8; Q9VSX9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=Eukaryotic translation initiation factor 4E;
Short=eIF-4E;
Short=eIF4E;
AltName: Full=eIF-4F 25 kDa subunit;
AltName: Full=mRNA cap-binding protein;
Name=eIF-4E; Synonyms=Eif4e, EIF4F; ORFNames=CG4035;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), AND DEVELOPMENTAL STAGE.
PubMed=7742371;
Hernandez G., Sierra J.M.;
"Translation initiation factor eIF-4E from Drosophila: cDNA sequence
and expression of the gene.";
Biochim. Biophys. Acta 1261:427-431(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS I AND II), AND FUNCTION.
PubMed=8663200; DOI=10.1074/jbc.271.27.16393;
Lavoie C.A., Lachance P.E.D., Sonenberg N., Lasko P.;
"Alternatively spliced transcripts from the Drosophila eIF4E gene
produce two different Cap-binding proteins.";
J. Biol. Chem. 271:16393-16398(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS I AND II), TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=9065696; DOI=10.1007/s004380050365;
Hernandez G., del Corral R., Santoyo J., Campuzano S., Sierra J.M.;
"Localization, structure and expression of the gene for translation
initiation factor eIF-4E from Drosophila melanogaster.";
Mol. Gen. Genet. 253:624-633(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS I AND II).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E.,
George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M.,
Celniker S.E.;
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH CUP.
PubMed=14691132; DOI=10.1083/jcb.200309088;
Wilhelm J.E., Hilton M., Amos Q., Henzel W.J.;
"Cup is an eIF4E binding protein required for both the translational
repression of oskar and the recruitment of Barentsz.";
J. Cell Biol. 163:1197-1204(2003).
[9]
INTERACTION WITH CUP, AND MUTAGENESIS OF TRP-117.
PubMed=14723848; DOI=10.1016/S1534-5807(03)00400-3;
Nakamura A., Sato K., Hanyu-Nakamura K.;
"Drosophila Cup is an eIF4E binding protein that associates with Bruno
and regulates oskar mRNA translation in oogenesis.";
Dev. Cell 6:69-78(2004).
[10]
INTERACTION WITH CUP.
PubMed=14685270; DOI=10.1038/sj.emboj.7600026;
Nelson M.R., Leidal A.M., Smibert C.A.;
"Drosophila Cup is an eIF4E-binding protein that functions in Smaug-
mediated translational repression.";
EMBO J. 23:150-159(2004).
[11]
INTERACTION WITH MXT.
PubMed=23716590; DOI=10.1128/MCB.01354-12;
Hernandez G., Miron M., Han H., Liu N., Magescas J., Tettweiler G.,
Frank F., Siddiqui N., Sonenberg N., Lasko P.;
"Mextli is a novel eukaryotic translation initiation factor 4E-binding
protein that promotes translation in Drosophila melanogaster.";
Mol. Cell. Biol. 33:2854-2864(2013).
[12]
X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 80-259 IN COMPLEX WITH MXT,
INTERACTION WITH 4E-T; CUP; MXT AND THOR, AND MUTAGENESIS OF ILE-107;
121-ASN-HIS-122 AND ILE-123.
PubMed=26294658; DOI=10.1101/gad.269068.115;
Peter D., Weber R., Kone C., Chung M.Y., Ebertsch L., Truffault V.,
Weichenrieder O., Igreja C., Izaurralde E.;
"Mextli proteins use both canonical bipartite and novel tripartite
binding modes to form eIF4E complexes that display differential
sensitivity to 4E-BP regulation.";
Genes Dev. 29:1835-1849(2015).
-!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing
mRNA cap during an early step in the initiation of protein
synthesis and facilitates ribosome binding by inducing the
unwinding of the mRNAs secondary structures.
{ECO:0000269|PubMed:8663200}.
-!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
which varies with external and internal environmental conditions.
It is composed of at least eIF4A, eIF4E and eIF4G. eIF4E is also
known to interact with other partners (By similarity). Recruited
by cup in oocytes and in early embryos, preventing the interaction
with eIF4G. The interaction with cup therefore prevents the
translation of key transcripts such as oskar (osk) and nanos (nos)
in some regions in the early embryo (PubMed:14691132,
PubMed:14723848, PubMed:14685270, PubMed:26294658). Interacts with
mxt (PubMed:23716590, PubMed:26294658). Interacts with 4E-T and
Thor (PubMed:26294658). {ECO:0000250, ECO:0000269|PubMed:14685270,
ECO:0000269|PubMed:14691132, ECO:0000269|PubMed:14723848,
ECO:0000269|PubMed:23716590, ECO:0000269|PubMed:26294658}.
-!- INTERACTION:
Q9VMA3:cup; NbExp=6; IntAct=EBI-198574, EBI-95398;
O61380:eIF4G1; NbExp=4; IntAct=EBI-198574, EBI-182219;
P21187:pAbp; NbExp=2; IntAct=EBI-198574, EBI-103658;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=I; Synonyms=A, B, D, E, F, G;
IsoId=P48598-1; Sequence=Displayed;
Name=II; Synonyms=C;
IsoId=P48598-2; Sequence=VSP_001437;
-!- TISSUE SPECIFICITY: Preferential expression in the pole cells, at
different developmental stages. {ECO:0000269|PubMed:9065696}.
-!- DEVELOPMENTAL STAGE: Throughout development.
{ECO:0000269|PubMed:7742371, ECO:0000269|PubMed:9065696}.
-!- PTM: Phosphorylation increases the ability of the protein to bind
to mRNA caps and to form the eIF4F complex. {ECO:0000250}.
-!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL25509.1; Type=Frameshift; Positions=105; Evidence={ECO:0000305};
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EMBL; U16139; AAC46603.1; -; mRNA.
EMBL; U54469; AAC03525.1; -; Genomic_DNA.
EMBL; U54469; AAC03524.1; -; Genomic_DNA.
EMBL; U63033; AAC47480.1; -; Genomic_DNA.
EMBL; U63033; AAC47479.1; -; Genomic_DNA.
EMBL; AE014296; AAF50281.1; -; Genomic_DNA.
EMBL; AE014296; AAF50282.1; -; Genomic_DNA.
EMBL; AE014296; AAF50283.1; -; Genomic_DNA.
EMBL; AE014296; AAN11963.1; -; Genomic_DNA.
EMBL; AE014296; AAN11964.1; -; Genomic_DNA.
EMBL; AE014296; AAN11965.1; -; Genomic_DNA.
EMBL; AE014296; AAN11966.1; -; Genomic_DNA.
EMBL; AY060470; AAL25509.1; ALT_FRAME; mRNA.
EMBL; BT012467; AAS93738.1; -; mRNA.
EMBL; BT044219; ACH92284.1; -; mRNA.
PIR; S55936; S55936.
RefSeq; NP_001261626.1; NM_001274697.1. [P48598-1]
RefSeq; NP_001261627.1; NM_001274698.1. [P48598-1]
RefSeq; NP_524829.1; NM_080090.3. [P48598-1]
RefSeq; NP_729480.1; NM_168333.2. [P48598-2]
RefSeq; NP_729481.1; NM_168334.1. [P48598-1]
RefSeq; NP_729482.1; NM_168335.2. [P48598-1]
RefSeq; NP_729483.1; NM_168336.2. [P48598-1]
RefSeq; NP_729484.1; NM_168337.2. [P48598-1]
RefSeq; NP_729485.1; NM_168338.2. [P48598-1]
UniGene; Dm.7012; -.
PDB; 4AXG; X-ray; 2.80 A; A/B=19-259.
PDB; 4UE8; X-ray; 1.10 A; A=80-259.
PDB; 4UE9; X-ray; 2.15 A; A=80-259.
PDB; 4UEA; X-ray; 2.62 A; A/C/E=80-259.
PDB; 4UEB; X-ray; 2.52 A; A/C/E=80-259.
PDB; 4UEC; X-ray; 2.40 A; A/C=80-259.
PDB; 5ABU; X-ray; 2.16 A; A=80-259.
PDB; 5ABV; X-ray; 2.13 A; A/C/E/G=80-259.
PDB; 5T47; X-ray; 2.20 A; A/C=80-259.
PDB; 5T48; X-ray; 2.19 A; A=80-259.
PDBsum; 4AXG; -.
PDBsum; 4UE8; -.
PDBsum; 4UE9; -.
PDBsum; 4UEA; -.
PDBsum; 4UEB; -.
PDBsum; 4UEC; -.
PDBsum; 5ABU; -.
PDBsum; 5ABV; -.
PDBsum; 5T47; -.
PDBsum; 5T48; -.
ProteinModelPortal; P48598; -.
SMR; P48598; -.
BioGrid; 69740; 44.
DIP; DIP-17448N; -.
ELM; P48598; -.
IntAct; P48598; 11.
STRING; 7227.FBpp0076215; -.
iPTMnet; P48598; -.
PaxDb; P48598; -.
PRIDE; P48598; -.
EnsemblMetazoa; FBtr0076487; FBpp0076215; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0076488; FBpp0076216; FBgn0015218. [P48598-2]
EnsemblMetazoa; FBtr0076489; FBpp0076217; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0076490; FBpp0076218; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0076491; FBpp0076219; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0076492; FBpp0076220; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0076493; FBpp0076221; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0333884; FBpp0306016; FBgn0015218. [P48598-1]
EnsemblMetazoa; FBtr0333885; FBpp0306017; FBgn0015218. [P48598-1]
GeneID; 45525; -.
KEGG; dme:Dmel_CG4035; -.
UCSC; CG4035-RB; d. melanogaster.
CTD; 45525; -.
FlyBase; FBgn0015218; eIF-4E.
eggNOG; KOG1670; Eukaryota.
eggNOG; COG5053; LUCA.
GeneTree; ENSGT00520000055549; -.
InParanoid; P48598; -.
KO; K03259; -.
OMA; HLFKHPL; -.
OrthoDB; EOG091G0IVA; -.
PhylomeDB; P48598; -.
Reactome; R-DME-110523; TOR signaling pathway.
Reactome; R-DME-1169408; ISG15 antiviral mechanism.
Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-DME-166208; mTORC1-mediated signalling.
Reactome; R-DME-429947; Deadenylation of mRNA.
Reactome; R-DME-72649; Translation initiation complex formation.
Reactome; R-DME-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
ChiTaRS; eIF-4E; fly.
GenomeRNAi; 45525; -.
PRO; PR:P48598; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0015218; -.
ExpressionAtlas; P48598; differential.
Genevisible; P48598; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; ISS:FlyBase.
GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:FlyBase.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0097482; C:muscle cell postsynaptic specialization; IDA:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0000932; C:P-body; IDA:FlyBase.
GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IPI:FlyBase.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:FlyBase.
GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
GO; GO:0002191; P:cap-dependent translational initiation; IMP:FlyBase.
GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0048136; P:male germ-line cyst formation; IMP:FlyBase.
GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
GO; GO:0010032; P:meiotic chromosome condensation; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
GO; GO:0030307; P:positive regulation of cell growth; TAS:FlyBase.
GO; GO:0001558; P:regulation of cell growth; IMP:FlyBase.
GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0016070; P:RNA metabolic process; IDA:UniProtKB.
GO; GO:0048515; P:spermatid differentiation; IMP:FlyBase.
GO; GO:0048137; P:spermatocyte division; IMP:FlyBase.
GO; GO:0006412; P:translation; IDA:FlyBase.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
Gene3D; 3.30.760.10; -; 1.
InterPro; IPR023398; TIF_eIF4e-like.
InterPro; IPR001040; TIF_eIF_4E.
InterPro; IPR019770; TIF_eIF_4E_CS.
PANTHER; PTHR11960; PTHR11960; 1.
Pfam; PF01652; IF4E; 1.
SUPFAM; SSF55418; SSF55418; 1.
PROSITE; PS00813; IF4E; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Initiation factor; Phosphoprotein; Protein biosynthesis;
Reference proteome; RNA-binding; Translation regulation.
CHAIN 1 259 Eukaryotic translation initiation factor
4E.
/FTId=PRO_0000193642.
REGION 100 101 7-methylguanosine-containing mRNA cap
binding. {ECO:0000250}.
REGION 146 147 7-methylguanosine-containing mRNA cap
binding. {ECO:0000250}.
REGION 199 204 7-methylguanosine-containing mRNA cap
binding. {ECO:0000250}.
VAR_SEQ 1 18 MQSDFHRMKNFANPKSMF -> MVVLETE (in isoform
II). {ECO:0000303|Ref.7}.
/FTId=VSP_001437.
MUTAGEN 107 107 I->A: Abolishes interaction with cup and
mxt; when associated with A-123.
{ECO:0000269|PubMed:26294658}.
MUTAGEN 117 117 W->A: Disrupts interaction with cup,
eIF4G and mxt.
{ECO:0000269|PubMed:14723848,
ECO:0000269|PubMed:26294658}.
MUTAGEN 121 122 NH->EE: Abolishes interaction with mxt,
reduces binding to Thor and 4E-T, and
does not affect interaction with cup.
{ECO:0000269|PubMed:26294658}.
MUTAGEN 123 123 I->A: Abolishes interaction with cup and
mxt; when associated with A-107.
{ECO:0000269|PubMed:26294658}.
STRAND 82 92 {ECO:0000244|PDB:4UE8}.
HELIX 100 102 {ECO:0000244|PDB:5ABV}.
STRAND 105 112 {ECO:0000244|PDB:4UE8}.
HELIX 113 122 {ECO:0000244|PDB:4UE8}.
HELIX 126 128 {ECO:0000244|PDB:4UE8}.
STRAND 134 139 {ECO:0000244|PDB:4UE8}.
STRAND 144 148 {ECO:0000244|PDB:4UEB}.
TURN 149 153 {ECO:0000244|PDB:4UE8}.
STRAND 155 163 {ECO:0000244|PDB:4UE8}.
HELIX 166 181 {ECO:0000244|PDB:4UE8}.
HELIX 188 190 {ECO:0000244|PDB:4UE8}.
STRAND 191 199 {ECO:0000244|PDB:4UE8}.
STRAND 202 210 {ECO:0000244|PDB:4UE8}.
HELIX 215 229 {ECO:0000244|PDB:4UE8}.
HELIX 233 235 {ECO:0000244|PDB:4UE8}.
STRAND 238 241 {ECO:0000244|PDB:4UE8}.
HELIX 242 244 {ECO:0000244|PDB:4UE8}.
STRAND 256 258 {ECO:0000244|PDB:5ABV}.
SEQUENCE 259 AA; 29224 MW; B844B2DD5738758E CRC64;
MQSDFHRMKN FANPKSMFKT SAPSTEQGRP EPPTSAAAPA EAKDVKPKED PQETGEPAGN
TATTTAPAGD DAVRTEHLYK HPLMNVWTLW YLENDRSKSW EDMQNEITSF DTVEDFWSLY
NHIKPPSEIK LGSDYSLFKK NIRPMWEDAA NKQGGRWVIT LNKSSKTDLD NLWLDVLLCL
IGEAFDHSDQ ICGAVINIRG KSNKISIWTA DGNNEEAALE IGHKLRDALR LGRNNSLQYQ
LHKDTMVKQG SNVKSIYTL


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20-372-60113 eukaryotic translation initiation factor 2. subunit 1 alpha. 35kDa. mRNA (cDNA clone MGC 1511 IMAGE 3139624). complete cds - Mouse monoclonal anti-human EIF2S1 antibody; Eukaryotic translation initiat 0.1 mg
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
EIAAB12733 Bos taurus,Bovine,eIF3 p42,eIF3 p44,eIF-3 RNA-binding subunit,eIF-3-delta,eIF3g,EIF3G,EIF3S4,Eukaryotic translation initiation factor 3 RNA-binding subunit,Eukaryotic translation initiation factor 3 s
15-288-22048F Eukaryotic translation initiation factor 4E-binding protein 2 - 4E-BP2; eIF4E-binding protein 2 Polyclonal 0.05 mg
15-288-22048F Eukaryotic translation initiation factor 4E-binding protein 2 - 4E-BP2; eIF4E-binding protein 2 Polyclonal 0.1 mg
EIAAB12730 eIF3 p42,eIF3 p44,eIF-3 RNA-binding subunit,eIF-3-delta,eIF3g,Eif3g,Eif3s4,Eukaryotic translation initiation factor 3 RNA-binding subunit,Eukaryotic translation initiation factor 3 subunit 4,Eukaryoti
EIAAB12732 eIF3 p42,eIF3 p44,eIF-3 RNA-binding subunit,eIF-3-delta,eIF3g,Eif3g,Eif3p42,Eif3s4,Eukaryotic translation initiation factor 3 RNA-binding subunit,Eukaryotic translation initiation factor 3 subunit 4,E
EIAAB12731 eIF3 p42,eIF3 p44,eIF-3 RNA-binding subunit,eIF-3-delta,eIF3g,EIF3G,EIF3S4,Eukaryotic translation initiation factor 3 RNA-binding subunit,Eukaryotic translation initiation factor 3 subunit 4,Eukaryoti
10-288-22048F Eukaryotic translation initiation factor 4E-binding protein 2 - 4E-BP2; eIF4E-binding protein 2 0.1 mg
10-288-22048F Eukaryotic translation initiation factor 4E-binding protein 2 - 4E-BP2; eIF4E-binding protein 2 0.05 mg
32-101 4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1_BP-1_PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13kDa). Binding of eIF4E 0.1 mL
32-102 4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1_BP-1_PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13kDa). Binding of eIF4E 0.1 mL
32-103 4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1_BP-1_PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13kDa). Binding of eIF4E 0.1 mg
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
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
60230 IgG,eukaryotic translation initiation factor 3, subunit 12 (EIF3S12), mRNA 0.1 mg
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
EIAAB12737 eIF3 p40 subunit,eIF-3-gamma,eIF3h,EIF3H,EIF3S3,Eukaryotic translation initiation factor 3 subunit 3,Eukaryotic translation initiation factor 3 subunit H,Homo sapiens,Human
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
GWB-8DFEE1 eukaryotic translation initiation factor 3 subunit 12 (EIF3S12) mRNA, Antibody


 

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