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Translation initiation factor IF-3 [Cleaved into: Translation initiation factor IF-3, N-terminally processed; Translation initiation factor IF-3S]

 IF3_ECOLI               Reviewed;         180 AA.
P0A707; P02999; P76905;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
18-SEP-2019, entry version 124.
RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
Contains:
RecName: Full=Translation initiation factor IF-3, N-terminally processed {ECO:0000255|HAMAP-Rule:MF_00080};
Contains:
RecName: Full=Translation initiation factor IF-3S {ECO:0000255|HAMAP-Rule:MF_00080};
Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; Synonyms=fit, srjA;
OrderedLocusNames=b1718, JW5829;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PROTEIN SEQUENCE, DIFFERENT PROTEIN FORMS, SUBCELLULAR LOCATION, AND
METHYLATION AT MET-1.
STRAIN=K;
PubMed=330233; DOI=10.1016/0014-5793(77)80801-6;
Brauer D., Wittmann-Liebold B.;
"The primary structure of the initiation factor IF-3 from Escherichia
coli.";
FEBS Lett. 79:269-275(1977).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6325158; DOI=10.1002/j.1460-2075.1982.tb01166.x;
Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J.A.,
Grunberg-Manago M., Blanquet S.;
"Sequence of a 1.26-kb DNA fragment containing the structural gene for
E.coli initiation factor IF3: presence of an AUU initiator codon.";
EMBO J. 1:311-315(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Miller H.I.;
Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[5]
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).
[6]
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).
[7]
DIFFERENT PROTEIN FORMS.
STRAIN=Al9, CP78, K, and MRE600;
PubMed=330232; DOI=10.1016/0014-5793(77)80800-4;
Suryanarayana T., Subramanian A.R.;
"Separation of two forms of IF-3 in Escherichia coli by two-
dimensional gel electrophoresis.";
FEBS Lett. 79:264-268(1977).
[8]
PHOSPHORYLATION.
PubMed=1534259; DOI=10.1021/bi00135a012;
Robertson E.S., Nicholson A.W.;
"Phosphorylation of Escherichia coli translation initiation factors by
the bacteriophage T7 protein kinase.";
Biochemistry 31:4822-4827(1992).
[9]
MUTAGENESIS OF TYR-107 AND LYS-110.
PubMed=1457399; DOI=10.1021/bi00163a005;
Debellis D., Liveris D., Goss D., Ringquist S., Schwartz I.;
"Structure-function analysis of Escherichia coli translation
initiation factor IF3: tyrosine 107 and lysine 110 are required for
ribosome binding.";
Biochemistry 31:11984-11990(1992).
[10]
MECHANISM OF TRANSLATION REGULATION.
PubMed=2954162; DOI=10.1073/pnas.84.12.4022;
Butler J.S., Springer M., Grunberg-Manago M.;
"AUU-to-AUG mutation in the initiator codon of the translation
initiation factor IF3 abolishes translational autocontrol of its own
gene (infC) in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 84:4022-4025(1987).
[11]
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).
[12]
MECHANISM OF TRANSLATION REGULATION.
PubMed=16857585; DOI=10.1016/j.molcel.2006.05.030;
Antoun A., Pavlov M.Y., Lovmar M., Ehrenberg M.;
"How initiation factors maximize the accuracy of tRNA selection in
initiation of bacterial protein synthesis.";
Mol. Cell 23:183-193(2006).
[13]
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).
[14]
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).
[15]
STRUCTURE BY NMR, AND MUTAGENESIS.
PubMed=1742345; DOI=10.1016/0300-9084(91)90141-m;
Spurio R., Paci M., Pawlik R.T., la Teana A., Digiacco B.V., Pon C.L.,
Gualerzi C.O.;
"Site-directed mutagenesis and NMR spectroscopic approaches to the
elucidation of the structure-function relationships in translation
initiation factors IF1 and IF3.";
Biochimie 73:1001-1006(1991).
[16]
STRUCTURE BY NMR.
PubMed=7705354; DOI=10.1111/j.1432-1033.1995.00395.x;
Garcia C., Fortier P.-L., Blanquet S., Lallemand J.-Y., Dardel F.;
"1H and 15N resonance assignments and structure of the N-terminal
domain of Escherichia coli initiation factor 3.";
Eur. J. Biochem. 228:395-402(1995).
[17]
STRUCTURE BY NMR.
PubMed=9054966; DOI=10.1006/jmbi.1996.0756;
Moreau M., de Cock E., Fortier P.-L., Garcia C., Albaret C.,
Blanquet S., Lallemand J.-Y., Dardel F.;
"Heteronuclear NMR studies of E. coli translation initiation factor
IF3. Evidence that the inter-domain region is disordered in
solution.";
J. Mol. Biol. 266:15-22(1997).
[18]
STRUCTURE BY NMR.
PubMed=9614948; DOI=10.1006/jmbi.1998.1736;
Hua Y., Raleigh D.P.;
"On the global architecture of initiation factor IF3: a comparative
study of the linker regions from the Escherichia coli protein and the
Bacillus stearothermophilus protein.";
J. Mol. Biol. 278:871-878(1998).
[19]
STRUCTURE BY NMR OF 90-180.
de Cock E., Blanquet S., Lallemand J.-Y., Dardel F.;
Submitted (DEC-1998) to the PDB data bank.
[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.IF-3 binds to the 30S ribosomal subunit and
shifts the equilibrum between 70S ribosomes and their 50S and 30S
subunits in favor of the free subunits, thus enhancing the
availability of 30S subunits on which protein synthesis initiation
begins. {ECO:0000269|PubMed:22562136}.
-!- SUBUNIT: Monomer. 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:22562136}.
-!- INTERACTION:
P02359:rpsG; NbExp=4; IntAct=EBI-546262, EBI-543074;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:330233}.
-!- PTM: Phosphorylated on threonine residue(s).
{ECO:0000269|PubMed:1534259}.
-!- PTM: The form lacking the initiator methionine is less abundant
than the N-methylmethionine form. {ECO:0000269|PubMed:330233}.
-!- MISCELLANEOUS: A short form called IF-3S/IF-3 beta is found both
in vivo and in vitro and is probably produced by degradation of
the long form IF-3L/IF-3 alpha. The major form is the N-
methylmethionine long form. {ECO:0000269|PubMed:330233}.
-!- MISCELLANEOUS: Uses the non-canonical initiation codon AUU, which
limits its expression (PubMed:16857585).
{ECO:0000305|PubMed:16857585}.
-!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
Rule:MF_00080}.
-!- CAUTION: Was originally (PubMed:2954162) thought to control the
translation of its own gene by binding to its mRNA; it now seems
that discrimination against the AUU start codon is a kinetic
effect (PubMed:16857585). {ECO:0000305|PubMed:16857585,
ECO:0000305|PubMed:2954162}.
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EMBL; V00291; CAA23561.1; -; Genomic_DNA.
EMBL; K02844; AAA51467.1; -; Genomic_DNA.
EMBL; U00096; AAC74788.1; -; Genomic_DNA.
EMBL; AP009048; BAA15485.1; -; Genomic_DNA.
PIR; S13748; FIEC3.
RefSeq; NP_416233.1; NC_000913.3.
RefSeq; WP_001700733.1; NZ_STEB01000009.1.
PDB; 2IFE; NMR; -; A=81-180.
PDB; 5ME0; EM; 13.50 A; Z=38-180.
PDB; 5ME1; EM; 13.50 A; Z=37-180.
PDBsum; 2IFE; -.
PDBsum; 5ME0; -.
PDBsum; 5ME1; -.
SMR; P0A707; -.
BioGrid; 4262192; 98.
ComplexPortal; CPX-2244; Translation initiation factor complex.
DIP; DIP-36176N; -.
IntAct; P0A707; 50.
STRING; 511145.b1718; -.
ChEMBL; CHEMBL1075077; -.
iPTMnet; P0A707; -.
EPD; P0A707; -.
jPOST; P0A707; -.
PaxDb; P0A707; -.
PRIDE; P0A707; -.
EnsemblBacteria; AAC74788; AAC74788; b1718.
EnsemblBacteria; BAA15485; BAA15485; BAA15485.
GeneID; 946225; -.
KEGG; ecj:JW5829; -.
KEGG; eco:b1718; -.
PATRIC; fig|511145.12.peg.1788; -.
EchoBASE; EB0501; -.
EcoGene; EG10506; infC.
eggNOG; ENOG4108UUX; Bacteria.
eggNOG; COG0290; LUCA.
HOGENOM; HOG000035157; -.
InParanoid; P0A707; -.
KO; K02520; -.
PhylomeDB; P0A707; -.
BioCyc; EcoCyc:EG10506-MONOMER; -.
BioCyc; ECOL316407:JW5829-MONOMER; -.
EvolutionaryTrace; P0A707; -.
PRO; PR:P0A707; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
GO; GO:0003743; F:translation initiation factor activity; IDA:EcoCyc.
GO; GO:0009409; P:response to cold; IDA:EcoCyc.
GO; GO:0032790; P:ribosome disassembly; IMP:EcoCyc.
DisProt; DP00197; -.
Gene3D; 3.10.20.80; -; 1.
Gene3D; 3.30.110.10; -; 1.
HAMAP; MF_00080; IF_3; 1.
InterPro; IPR036788; T_IF-3_C_sf.
InterPro; IPR036787; T_IF-3_N_sf.
InterPro; IPR019813; Translation_initiation_fac3_CS.
InterPro; IPR001288; Translation_initiation_fac_3.
InterPro; IPR019815; Translation_initiation_fac_3_C.
InterPro; IPR019814; Translation_initiation_fac_3_N.
PANTHER; PTHR10938; PTHR10938; 1.
Pfam; PF00707; IF3_C; 1.
Pfam; PF05198; IF3_N; 1.
SUPFAM; SSF54364; SSF54364; 1.
SUPFAM; SSF55200; SSF55200; 1.
TIGRFAMs; TIGR00168; infC; 1.
PROSITE; PS00938; IF3; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Cytoplasm; Direct protein sequencing; Initiation factor; Methylation;
Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding.
CHAIN 1 180 Translation initiation factor IF-3.
{ECO:0000305|PubMed:330233}.
/FTId=PRO_0000367498.
INIT_MET 1 1 Removed; alternate.
{ECO:0000269|PubMed:330233}.
CHAIN 2 180 Translation initiation factor IF-3, N-
terminally processed.
{ECO:0000305|PubMed:330233}.
/FTId=PRO_0000014499.
CHAIN 7 180 Translation initiation factor IF-3S.
{ECO:0000305|PubMed:330233}.
/FTId=PRO_0000364089.
SITE 107 107 Important for 30S binding.
{ECO:0000305|PubMed:1457399}.
SITE 110 110 Important for 30S binding.
{ECO:0000305|PubMed:1457399}.
MOD_RES 1 1 N-methylmethionine; in Translation
initiation factor IF-3; alternate.
{ECO:0000269|PubMed:330233}.
MUTAGEN 107 107 Y->F,L: Reduced ribosome binding.
{ECO:0000269|PubMed:1457399}.
MUTAGEN 110 110 K->R,L: Reduced ribosome binding.
{ECO:0000269|PubMed:1457399}.
CONFLICT 22 22 Q -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 34 36 LGI -> IGMV (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 47 47 E -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 52 52 D -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 E -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 87 87 K -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 90 90 V -> K (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 103 103 D -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 G -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 161 161 F -> S (in Ref. 3; AAA51467).
{ECO:0000305}.
CONFLICT 178 178 K -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 180 180 Missing (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 92 98 {ECO:0000244|PDB:2IFE}.
HELIX 104 107 {ECO:0000244|PDB:2IFE}.
HELIX 109 119 {ECO:0000244|PDB:2IFE}.
STRAND 122 128 {ECO:0000244|PDB:2IFE}.
HELIX 140 152 {ECO:0000244|PDB:2IFE}.
TURN 153 155 {ECO:0000244|PDB:2IFE}.
STRAND 156 159 {ECO:0000244|PDB:2IFE}.
STRAND 171 176 {ECO:0000244|PDB:2IFE}.
SEQUENCE 180 AA; 20564 MW; 6120EB6AD42E9ABE CRC64;
MKGGKRVQTA RPNRINGEIR AQEVRLTGLE GEQLGIVSLR EALEKAEEAG VDLVEISPNA
EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP GTDEGDYQVK LRSLIRFLEE
GDKAKITLRF RGREMAHQQI GMEVLNRVKD DLQELAVVES FPTKIEGRQM IMVLAPKKKQ


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[EIF4A3 DDX48 KIAA0111] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic initiation factor 4A-like NUK-34) (Eukaryotic translation initiation factor 4A isoform 3) (Nuclear matrix protein 265) (NMP 265) (hNMP 265) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
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[Eif4a3 Ddx48] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[EIF4A3 DDX48] Eukaryotic initiation factor 4A-III (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[EIF4A3 DDX48] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[EIF4A3 DDX48 QtsA-15322] Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]
[EIF3L EIF3EIP EIF3S6IP HSPC021 HSPC025 MSTP005] Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein)
[EIF3E EIF3S6 INT6] Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (Viral integration site protein INT-6 homolog) (eIF-3 p48)
[Eif3l Eif3eip Eif3s6ip Paf67] Eukaryotic translation initiation factor 3 subunit L (eIF3l) (66 kDa tyrosine-rich heat shock protein) (67 kDa polymerase-associated factor) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) (HSP-66Y) (PAF67)
[EIF3F EIF3S5] Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47)
[Eif3b Eif3s9] Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (eIF3 p116)
[EIF3G EIF3S4] Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44)
[Eif3f Eif3s5] Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47)
[EIF3B EIF3S9] Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (Prt1 homolog) (hPrt1) (eIF-3-eta) (eIF3 p110) (eIF3 p116)
[EIF3I EIF3S2 TRIP1] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36)
[EIF3K EIF3S12 ARG134 HSPC029 MSTP001 PTD001] Eukaryotic translation initiation factor 3 subunit K (eIF3k) (Eukaryotic translation initiation factor 3 subunit 12) (Muscle-specific gene M9 protein) (PLAC-24) (eIF-3 p25) (eIF-3 p28)
[EIF3A EIF3S10 KIAA0139] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185)
[EIF3H EIF3S3] Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit)
[EIF3D EIF3S7] Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66)
[EIF3J EIF3S1 PRO0391] Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Eukaryotic translation initiation factor 3 subunit 1) (eIF-3-alpha) (eIF3 p35)
[EIF3C EIF3S8] Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110)
[Eif3e Eif3s6 Int6] Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (MMTV integration site 6) (Mammary tumor-associated protein INT-6) (Viral integration site protein INT-6) (eIF-3 p48)
[Eif3a Csma Eif3 Eif3s10] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Centrosomin) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185) (p162)
[Eif3a Eif3s10] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta)
[Eif3g Eif3p42 Eif3s4] Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44)
[EIF4E2 EIF4EL3] Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (Eukaryotic translation initiation factor 4E homologous protein) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) (mRNA cap-binding protein 4EHP) (h4EHP) (mRNA cap-binding protein type 3)
[sum1 eif3i tif34 SPAC4D7.05] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 39 kDa subunit homolog) (eIF-3 39 kDa subunit homolog) (eIF3 p39) (Suppressor of uncontrolled mitosis 1)
[SPAC25G10.08] Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 90 kDa subunit homolog) (eIF3 p90) (Translation initiation factor eIF3 p90 subunit homolog) (spPrt1)
[Eif3i Eif3s2 Trip1] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36)
[TIF1 TIF41A YKR059W; TIF2 TIF41B YJL138C J0660] ATP-dependent RNA helicase eIF4A (EC 3.6.4.13) (Eukaryotic initiation factor 4A) (eIF-4A) (Stimulator factor I 37 kDa component) (Translation initiation factor 1/2) (p37)

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