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Translation initiation factor IF-2

 IF2_ECOLI               Reviewed;         890 AA.
P0A705; O32548; O32549; O32550; O34379; O34415; O34603; P02995;
Q2M942; Q9EUZ4; Q9EUZ5; Q9EUZ6; Q9EUZ8; Q9EUZ9; Q9EV00;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
31-JAN-2018, entry version 119.
RecName: Full=Translation initiation factor IF-2;
Name=infB; Synonyms=gicD, ssyG; OrderedLocusNames=b3168, JW3137;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6096856; DOI=10.1073/pnas.81.24.7787;
Sacerdot C., Dessen P., Hershey J.W.B., Plumbridge J.A.,
Grunberg-Manago M.;
"Sequence of the initiation factor IF2 gene: unusual protein features
and homologies with elongation factors.";
Proc. Natl. Acad. Sci. U.S.A. 81:7787-7791(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Various clinical strains;
PubMed=9428651; DOI=10.1016/S0014-5793(97)01472-5;
Steffensen S.A.D.A., Poulsen A.B., Mortensen K.K.,
Sperling-Petersen H.U.;
"E. coli translation initiation factor IF2--an extremely conserved
protein. Comparative sequence analysis of the infB gene in clinical
isolates of E. coli.";
FEBS Lett. 419:281-284(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IQ489, and IQ490;
Hedegaard J., Kristensen J.E., Nakamura Y., Sperling-Petersen H.U.,
Mortensen K.K.;
"Sequence of the infB gene from Escherichia coli strain IQ489 and
IQ490.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=6326058; DOI=10.1093/nar/12.7.3333;
Ishii S., Ihara M., Maekawa T., Nakamura Y., Uchida H., Imamoto F.;
"The nucleotide sequence of the cloned nusA gene and its flanking
region of Escherichia coli.";
Nucleic Acids Res. 12:3333-3342(1984).
[7]
PROTEIN SEQUENCE OF 1-11 AND 159-174 (ISOFORMS ALPHA AND BETA).
PubMed=3894004;
Plumbridge J.A., Deville F., Sacerdot C., Petersen H.U.,
Cenatiempo Y., Cozzone A., Grunberg-Manago M., Hershey J.W.;
"Two translational initiation sites in the infB gene are used to
express initiation factor IF2 alpha and IF2 beta in Escherichia
coli.";
EMBO J. 4:223-229(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 864-890, INDUCTION, AND OPERON.
STRAIN=K12;
PubMed=2849753; DOI=10.1093/nar/16.22.10803;
Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M.,
Hershey J.W.B.;
"The existence of two genes between infB and rpsO in the Escherichia
coli genome: DNA sequencing and S1 nuclease mapping.";
Nucleic Acids Res. 16:10803-10816(1988).
[9]
PROTEIN SEQUENCE OF 159-174 AND 166-174 (ISOFORMS BETA AND BETA'),
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1764105; DOI=10.1016/0006-291X(91)92118-4;
Nyengaard N.R., Mortensen K.K., Lassen S.F., Hershey J.W.B.,
Sperling-Petersen H.U.;
"Tandem translation of E. coli initiation factor IF2 beta:
purification and characterization in vitro of two active forms.";
Biochem. Biophys. Res. Commun. 181:1572-1579(1991).
[10]
PROTEIN SEQUENCE OF 159-169 AND 166-171 (ISOFORMS BETA AND BETA'),
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-158 AND
MET-165.
PubMed=1374802; DOI=10.1016/0022-2836(92)91026-L;
Sacerdot C., Vachon G., Laalami S., Morel-Deville F., Cenatiempo Y.,
Grunberg-Manago M.;
"Both forms of translational initiation factor IF2 (alpha and beta)
are required for maximal growth of Escherichia coli. Evidence for two
translational initiation codons for IF2 beta.";
J. Mol. Biol. 225:67-80(1992).
[11]
PROTEIN SEQUENCE OF 290-304, FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=2444251; DOI=10.1021/bi00390a028;
Cenatiempo Y., Deville F., Dondon J., Grunberg-Manago M., Sacerdot C.,
Hershey J.W., Hansen H.F., Petersen H.U., Clark B.F., Kjeldgaard M.;
"The protein synthesis initiation factor 2 G-domain. Study of a
functionally active C-terminal 65-kilodalton fragment of IF2 from
Escherichia coli.";
Biochemistry 26:5070-5076(1987).
[12]
DOMAIN STRUCTURE, AND REVIEW.
PubMed=1805969; DOI=10.1016/0300-9084(91)90191-3;
Laalami S., Sacerdot C., Vachon G., Mortensen K.,
Sperling-Petersen H.U., Cenatiempo Y., Grunberg-Manago M.;
"Structural and functional domains of E coli initiation factor IF2.";
Biochimie 73:1557-1566(1991).
[13]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[14]
PARTIALLY SUPPRESSES A RSGA MUTANT.
STRAIN=K12;
PubMed=18223068; DOI=10.1128/JB.01744-07;
Campbell T.L., Brown E.D.;
"Genetic interaction screens with ordered overexpression and deletion
clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome
biogenesis.";
J. Bacteriol. 190:2537-2545(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-808, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[16]
FUNCTION, AND SUBUNIT.
PubMed=20224578; DOI=10.1038/embor.2010.12;
Milon P., Carotti M., Konevega A.L., Wintermeyer W., Rodnina M.V.,
Gualerzi C.O.;
"The ribosome-bound initiation factor 2 recruits initiator tRNA to the
30S initiation complex.";
EMBO Rep. 11:312-316(2010).
[17]
FUNCTION, AND SUBUNIT.
PubMed=22562136; DOI=10.1038/nsmb.2285;
Milon P., Maracci C., Filonava L., Gualerzi C.O., Rodnina M.V.;
"Real-time assembly landscape of bacterial 30S translation initiation
complex.";
Nat. Struct. Mol. Biol. 19:609-615(2012).
[18]
REVIEW.
PubMed=22515367; DOI=10.3109/10409238.2012.678284;
Milon P., Rodnina M.V.;
"Kinetic control of translation initiation in bacteria.";
Crit. Rev. Biochem. Mol. Biol. 47:334-348(2012).
[19]
STRUCTURE BY NMR OF 2-50.
STRAIN=K12;
PubMed=12600987; DOI=10.1074/jbc.M212960200;
Laursen B.S., Mortensen K.K., Sperling-Petersen H.U., Hoffman D.W.;
"A conserved structural motif at the N terminus of bacterial
translation initiation factor IF2.";
J. Biol. Chem. 278:16320-16328(2003).
[20]
MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS), AND SUBUNIT.
PubMed=21750663; DOI=10.1371/journal.pbio.1001095;
Julian P., Milon P., Agirrezabala X., Lasso G., Gil D., Rodnina M.V.,
Valle M.;
"The cryo-EM structure of a complete 30S translation initiation
complex from Escherichia coli.";
PLoS Biol. 9:E1001095-E1001095(2011).
-!- FUNCTION: One of the essential components for the initiation of
protein synthesis. May protect N-formylmethionyl-tRNA(fMet) from
spontaneous hydrolysis. Promotes N-formylmethionyl-tRNA(fMet)
binding to the 30S pre-initiation complex (PIC) (PubMed:1764105,
PubMed:20224578). Also involved in the hydrolysis of GTP during
the formation of the 70S ribosomal complex. Upon addition of the
50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving
the mature 70S translation initation complex.
{ECO:0000269|PubMed:1764105, ECO:0000269|PubMed:20224578,
ECO:0000269|PubMed:22562136, ECO:0000269|PubMed:2444251}.
-!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
complex which assembles on the 30S ribosome in the order IF-2 and
IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can
occur at any time during PIC assembly.
{ECO:0000269|PubMed:20224578, ECO:0000269|PubMed:21750663,
ECO:0000269|PubMed:22562136}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1764105}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=Alpha {ECO:0000269|PubMed:3894004};
IsoId=P0A705-1; Sequence=Displayed;
Note=Isoform alpha is approximately 2-fold more abundant than
the combined beta isoforms. Optimal growth requires both alpha
and beta IF2. {ECO:0000305|PubMed:1374802};
Name=Beta {ECO:0000269|PubMed:1374802, ECO:0000269|PubMed:1764105,
ECO:0000269|PubMed:3894004};
IsoId=P0A705-2; Sequence=VSP_018758, VSP_018759;
Note=Also called beta1. {ECO:0000305|PubMed:1374802};
Name=Beta' {ECO:0000269|PubMed:1374802,
ECO:0000269|PubMed:1764105};
IsoId=P0A705-3; Sequence=VSP_018760;
Note=Also called beta2. {ECO:0000305|PubMed:1374802};
-!- INDUCTION: Part of the metY operon that extends to pnp
(PubMed:2849753). {ECO:0000269|PubMed:2849753}.
-!- PTM: A proteolyzed form, called IF2 gamma (begins with residue
290), can be detected during purification which has all the
activities expected for this protein, although it is slightly less
efficient than full-length protein. It is not clear if it exists
in vivo. {ECO:0000269|PubMed:2444251}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. The C-
terminal region (residues 165-890) is sufficient for growth at 42
degrees Celsius, although it grows more slowly at 37 degrees and
is cold-sensitive at 30 degrees Celsius (PubMed:1374802).
{ECO:0000269|PubMed:1374802}.
-!- MISCELLANEOUS: When overexpressed partially suppresses the slow
growth and decreased 70S ribosome phenotype of an rsgA knockout;
RsgA may be involved in 30S ribosomal subunit biogenesis.
{ECO:0000269|PubMed:18223068}.
-!- MISCELLANEOUS: Silent mutations of codon 158, which no longer
function as alternative start codons, decrease beta isoform
expression to 31 to 50%, the strongest mutation is GUG to GUC.
{ECO:0000269|PubMed:1374802}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. IF-2
subfamily. {ECO:0000305}.
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EMBL; X00513; CAA25201.1; -; Genomic_DNA.
EMBL; X00513; CAA25202.1; -; Genomic_DNA.
EMBL; U18997; AAA57971.1; -; Genomic_DNA.
EMBL; U00096; AAC76202.1; -; Genomic_DNA.
EMBL; AP009048; BAE77214.1; -; Genomic_DNA.
EMBL; AJ002537; CAA05529.1; -; Genomic_DNA.
EMBL; AJ002537; CAA05530.1; -; Genomic_DNA.
EMBL; AJ002537; CAA05531.1; -; Genomic_DNA.
EMBL; AJ002538; CAA05532.1; -; Genomic_DNA.
EMBL; AJ002538; CAA05533.1; -; Genomic_DNA.
EMBL; AJ002538; CAA05534.1; -; Genomic_DNA.
EMBL; AJ002539; CAA05535.1; -; Genomic_DNA.
EMBL; AJ002539; CAA05536.1; -; Genomic_DNA.
EMBL; AJ002539; CAA05537.1; -; Genomic_DNA.
EMBL; AJ002540; CAA05538.1; -; Genomic_DNA.
EMBL; AJ002540; CAA05539.1; -; Genomic_DNA.
EMBL; AJ002540; CAA05540.1; -; Genomic_DNA.
EMBL; AJ002541; CAA05541.1; -; Genomic_DNA.
EMBL; AJ002541; CAA05542.1; -; Genomic_DNA.
EMBL; AJ002541; CAA05543.1; -; Genomic_DNA.
EMBL; AJ002542; CAA05544.1; -; Genomic_DNA.
EMBL; AJ002542; CAA05545.1; -; Genomic_DNA.
EMBL; AJ002542; CAA05546.1; -; Genomic_DNA.
EMBL; AJ002402; CAA05386.1; -; Genomic_DNA.
EMBL; AJ002403; CAA05387.1; -; Genomic_DNA.
EMBL; AJ002404; CAA05388.1; -; Genomic_DNA.
EMBL; AJ002405; CAA05389.1; -; Genomic_DNA.
EMBL; AJ002406; CAA05390.1; -; Genomic_DNA.
EMBL; AJ002407; CAA05391.1; -; Genomic_DNA.
EMBL; AJ002408; CAA05392.1; -; Genomic_DNA.
EMBL; AJ002409; CAA05393.1; -; Genomic_DNA.
EMBL; AJ002410; CAA05394.1; -; Genomic_DNA.
EMBL; AJ002411; CAA05395.1; -; Genomic_DNA.
EMBL; AJ002412; CAA05396.1; -; Genomic_DNA.
EMBL; AJ002413; CAA05397.1; -; Genomic_DNA.
EMBL; AJ132861; CAC20126.1; -; Genomic_DNA.
EMBL; AJ132861; CAC20127.1; -; Genomic_DNA.
EMBL; AJ132861; CAC20128.1; -; Genomic_DNA.
EMBL; AJ132862; CAC20130.1; -; Genomic_DNA.
EMBL; AJ132862; CAC20131.1; -; Genomic_DNA.
EMBL; AJ132862; CAC20132.1; -; Genomic_DNA.
EMBL; X13775; CAA32019.1; -; Genomic_DNA.
PIR; D65107; FIEC2.
RefSeq; NP_417637.1; NC_000913.3.
RefSeq; WP_000133044.1; NZ_LN832404.1.
PDB; 1ND9; NMR; -; A=2-50.
PDB; 1ZO1; EM; 13.80 A; I=388-888.
PDB; 3JCJ; EM; 3.70 A; f=1-890.
PDB; 3JCN; EM; 4.60 A; b=1-890.
PDB; 5ME0; EM; 13.50 A; W=1-890.
PDB; 5ME1; EM; 13.50 A; W=1-890.
PDBsum; 1ND9; -.
PDBsum; 1ZO1; -.
PDBsum; 3JCJ; -.
PDBsum; 3JCN; -.
PDBsum; 5ME0; -.
PDBsum; 5ME1; -.
ProteinModelPortal; P0A705; -.
SMR; P0A705; -.
DIP; DIP-36182N; -.
IntAct; P0A705; 51.
MINT; MINT-1235405; -.
STRING; 316385.ECDH10B_3342; -.
iPTMnet; P0A705; -.
EPD; P0A705; -.
PaxDb; P0A705; -.
PRIDE; P0A705; -.
EnsemblBacteria; AAC76202; AAC76202; b3168.
EnsemblBacteria; BAE77214; BAE77214; BAE77214.
GeneID; 947684; -.
KEGG; ecj:JW3137; -.
KEGG; eco:b3168; -.
PATRIC; fig|511145.12.peg.3263; -.
EchoBASE; EB0500; -.
EcoGene; EG10505; infB.
eggNOG; ENOG4107QHU; Bacteria.
eggNOG; COG0532; LUCA.
InParanoid; P0A705; -.
KO; K02519; -.
PhylomeDB; P0A705; -.
BioCyc; EcoCyc:EG10505-MONOMER; -.
EvolutionaryTrace; P0A705; -.
PRO; PR:P0A705; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
GO; GO:0003743; F:translation initiation factor activity; IDA:EcoliWiki.
GO; GO:0006413; P:translational initiation; IDA:EcoCyc.
Gene3D; 3.40.50.10050; -; 1.
HAMAP; MF_00100_B; IF_2_B; 1.
InterPro; IPR009061; DNA-bd_dom_put_sf.
InterPro; IPR013575; IF2_assoc_dom_bac.
InterPro; IPR006847; IF2_N.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR000178; TF_IF2_bacterial-like.
InterPro; IPR015760; TIF_IF2.
InterPro; IPR023115; TIF_IF2_dom3.
InterPro; IPR036925; TIF_IF2_dom3_sf.
InterPro; IPR009000; Transl_B-barrel_sf.
PANTHER; PTHR43381; PTHR43381; 1.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF11987; IF-2; 1.
Pfam; PF08364; IF2_assoc; 1.
Pfam; PF04760; IF2_N; 2.
SUPFAM; SSF46955; SSF46955; 1.
SUPFAM; SSF50447; SSF50447; 2.
SUPFAM; SSF52156; SSF52156; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00487; IF-2; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51722; G_TR_2; 1.
PROSITE; PS01176; IF2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation; Complete proteome;
Cytoplasm; Direct protein sequencing; GTP-binding; Initiation factor;
Nucleotide-binding; Protein biosynthesis; Reference proteome.
CHAIN 1 890 Translation initiation factor IF-2.
/FTId=PRO_0000238785.
DOMAIN 389 558 tr-type G.
NP_BIND 398 405 GTP. {ECO:0000250}.
NP_BIND 444 448 GTP. {ECO:0000250}.
NP_BIND 498 501 GTP. {ECO:0000250}.
REGION 1 103 1.
REGION 104 287 2.
REGION 288 391 3.
REGION 398 405 G1. {ECO:0000250}.
REGION 423 427 G2. {ECO:0000250}.
REGION 444 447 G3. {ECO:0000250}.
REGION 498 501 G4. {ECO:0000250}.
REGION 534 536 G5. {ECO:0000250}.
REGION 541 668 5.
REGION 669 890 6.
COMPBIAS 167 214 Ala/Arg/Glu/Lys-rich.
MOD_RES 808 808 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
VAR_SEQ 1 164 Missing (in isoform Beta').
{ECO:0000269|PubMed:1374802,
ECO:0000269|PubMed:1764105, ECO:0000305}.
/FTId=VSP_018760.
VAR_SEQ 1 157 Missing (in isoform Beta).
{ECO:0000269|PubMed:1374802,
ECO:0000269|PubMed:1764105,
ECO:0000269|PubMed:3894004, ECO:0000305}.
/FTId=VSP_018758.
VAR_SEQ 158 158 V -> M (in isoform Beta).
{ECO:0000305|PubMed:1764105,
ECO:0000305|PubMed:3894004}.
/FTId=VSP_018759.
VARIANT 409 409 D -> E (in strain: IQ489).
VARIANT 423 423 G -> GG (in strain: IQ490).
VARIANT 432 432 H -> Q (in strain: ECOAU9326).
VARIANT 490 490 Q -> G (in strain: ECOAU9302, ECOAU9306,
ECOAU9307 and ECOAU9309).
VARIANT 684 684 G -> A (in strain: ECOAU9306).
MUTAGEN 158 158 V->A: Produces 35% of isoform beta (i.e.
only beta2).
{ECO:0000269|PubMed:1374802}.
MUTAGEN 158 158 V->E: Produces 70% of isoform beta (i.e.
only beta2).
{ECO:0000269|PubMed:1374802}.
MUTAGEN 158 158 V->G: Produces 66% of isoform beta (i.e.
only beta2).
{ECO:0000269|PubMed:1374802}.
MUTAGEN 165 165 M->I,T: Produces reduces amount of
isoform beta (i.e. only beta1). Reduced
growth at 37 degrees Celsius, greatly
reduced growth at 30 degrees Celsius.
Growth is more impaired; when associated
with silent V-158 GUG to GUC.
{ECO:0000269|PubMed:1374802}.
HELIX 8 13 {ECO:0000244|PDB:1ND9}.
STRAND 14 16 {ECO:0000244|PDB:1ND9}.
HELIX 17 27 {ECO:0000244|PDB:1ND9}.
STRAND 32 35 {ECO:0000244|PDB:1ND9}.
HELIX 41 43 {ECO:0000244|PDB:1ND9}.
HELIX 44 49 {ECO:0000244|PDB:1ND9}.
SEQUENCE 890 AA; 97350 MW; 86B9F9B2AE773DDE CRC64;
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT
LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQAQR EAEEQARREA
EESAKREAQQ KAEREAAEQA KREAAEQAKR EAAEKDKVSN QQDDMTKNAQ AEKARREQEA
AELKRKAEEE ARRKLEEEAR RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE
DESDREVEGG RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE
MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV DHGKTSLLDY IRSTKVASGE
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI
EAIQHAKAAQ VPVVVAVNKI DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG
IDELLDAILL QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA REVALYRQGK
FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS VEAISDSLLK LSTDEVKVKI
IGSGVGGITE TDATLAAASN AILVGFNVRA DASARKVIEA ESLDLRYYSV IYNLIDEVKA
AMSGMLSPEL KQQIIGLAEV RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA


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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
EIAAB12703 65 kDa eukaryotic translation initiation factor 2A,CDA02,EIF2A,eIF-2A,Eukaryotic translation initiation factor 2A,Homo sapiens,Human,MSTP004,MSTP089
10-288-22403F Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.05 mg
15-288-22403A Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg
10-288-22403F Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg
18-003-43602 Eukaryotic translation initiation factor 4E type 2 - eIF4E type 2; eIF-4E type 2; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.1 mg Protein A
15-288-22403A Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation 0.05 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
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
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
EIAAB12715 eIF3 p110,eIF3c,EIF3C,EIF3S8,Eukaryotic translation initiation factor 3 subunit 8,Eukaryotic translation initiation factor 3 subunit C,Homo sapiens,Human
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
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
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
U1885r CLIA kit eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
EIAAB12739 eIF3 p36,eIF-3-beta,eIF3i,Eif3i,Eif3s2,Eukaryotic translation initiation factor 3 subunit 2,Eukaryotic translation initiation factor 3 subunit I,Rat,Rattus norvegicus
EIAAB12722 eIF3 p66,eIF3d,Eif3d,Eif3s7,eIF-3-zeta,Eukaryotic translation initiation factor 3 subunit 7,Eukaryotic translation initiation factor 3 subunit D,Mouse,Mus musculus
EIAAB12745 Bos taurus,Bovine,eIF3 p35,eIF-3-alpha,eIF3j,EIF3J,EIF3S1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J
EIAAB12740 Bos taurus,Bovine,eIF3 p36,eIF-3-beta,eIF3i,EIF3I,EIF3S2,Eukaryotic translation initiation factor 3 subunit 2,Eukaryotic translation initiation factor 3 subunit I
E1885r ELISA kit eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
EIAAB12747 eIF3 p35,eIF-3-alpha,eIF3j,Eif3j,Eif3s1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J,Mouse,Mus musculus
EIAAB12746 eIF3 p35,eIF-3-alpha,eIF3j,Eif3j,Eif3s1,Eukaryotic translation initiation factor 3 subunit 1,Eukaryotic translation initiation factor 3 subunit J,Rat,Rattus norvegicus
EIAAB12728 eIF3 p47,eIF-3-epsilon,eIF3f,Eif3f,Eif3s5,Eukaryotic translation initiation factor 3 subunit 5,Eukaryotic translation initiation factor 3 subunit F,Mouse,Mus musculus
EIAAB12717 Bos taurus,Bovine,eIF3 p110,eIF3c,EIF3C,EIF3S8,Eukaryotic translation initiation factor 3 subunit 8,Eukaryotic translation initiation factor 3 subunit C


 

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