Full text data of EIF4B
EIF4B
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Eukaryotic translation initiation factor 4B; eIF-4B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 4B; eIF-4B
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00012079
IPI00012079 Eukaryotic translation initiation factor 4B eukaryotic translation initiation factor 4F complex, RNA binding, translation initiation factor activity, regulation of translational initiation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00012079 Eukaryotic translation initiation factor 4B eukaryotic translation initiation factor 4F complex, RNA binding, translation initiation factor activity, regulation of translational initiation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P23588
ID IF4B_HUMAN Reviewed; 611 AA.
AC P23588; Q4G0E3; Q53HQ2; Q6GPH5; Q6IB46; Q8WYK5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Eukaryotic translation initiation factor 4B;
DE Short=eIF-4B;
GN Name=EIF4B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2390971;
RA Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.;
RT "Cloning and expression of eukaryotic initiation factor 4B cDNA:
RT sequence determination identifies a common RNA recognition motif.";
RL EMBO J. 9:2783-2790(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RA Yokoyama K.;
RT "Human eukaryotic initiation factor 4B.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242;
RP 340-372; 380-398; 473-486 AND 512-537, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP CHARACTERIZATION.
RX PubMed=8139536;
RA Methot N., Pause A., Hershey J.W., Sonenberg N.;
RT "The translation initiation factor eIF-4B contains an RNA-binding
RT region that is distinct and independent from its ribonucleoprotein
RT consensus sequence.";
RL Mol. Cell. Biol. 14:2307-2316(1994).
RN [9]
RP CHARACTERIZATION.
RX PubMed=8816444;
RA Methot N., Song M.S., Sonenberg N.;
RT "A region rich in aspartic acid, arginine, tyrosine, and glycine
RT (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-
RT association and interaction with eIF3.";
RL Mol. Cell. Biol. 16:5328-5334(1996).
RN [10]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=15071500; DOI=10.1038/sj.emboj.7600193;
RA Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D.,
RA Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.;
RT "Phosphorylation of eucaryotic translation initiation factor 4B Ser422
RT is modulated by S6 kinases.";
RL EMBO J. 23:1761-1769(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=16763566; DOI=10.1038/sj.emboj.7601166;
RA Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B.,
RA Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.;
RT "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its
RT phosphorylation and activity.";
RL EMBO J. 25:2781-2791(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283;
RP SER-459 AND SER-597, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219;
RP SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418;
RP SER-425; SER-445; SER-498; SER-504 AND SER-597, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP STRUCTURE BY NMR OF 88-178.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain of eukaryotic initiation
RT factor 4B.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [24]
RP VARIANT ARG-203.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Required for the binding of mRNA to ribosomes. Functions
CC in close association with EIF4-F and EIF4-A. Binds near the 5'-
CC terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the
CC ATPase activity and the ATP-dependent RNA unwinding activity of
CC both EIF4-A and EIF4-F.
CC -!- SUBUNIT: Self-associates and interacts with EIF3 p170 subunit.
CC -!- INTERACTION:
CC P53350:PLK1; NbExp=3; IntAct=EBI-970310, EBI-476768;
CC -!- PTM: Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1;
CC phosphorylation enhances the affinity of EIF4B for the EIF3
CC complex.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X55733; CAA39265.1; -; Genomic_DNA.
DR EMBL; AB076839; BAB82380.1; -; mRNA.
DR EMBL; CR456958; CAG33239.1; -; mRNA.
DR EMBL; AK222528; BAD96248.1; -; mRNA.
DR EMBL; CH471054; EAW96657.1; -; Genomic_DNA.
DR EMBL; BC073139; AAH73139.1; -; mRNA.
DR EMBL; BC073154; AAH73154.1; -; mRNA.
DR EMBL; BC098437; AAH98437.1; -; mRNA.
DR PIR; S12566; S12566.
DR RefSeq; NP_001408.2; NM_001417.4.
DR UniGene; Hs.648394; -.
DR UniGene; Hs.702041; -.
DR PDB; 1WI8; NMR; -; A=88-178.
DR PDB; 2J76; NMR; -; E=78-176.
DR PDBsum; 1WI8; -.
DR PDBsum; 2J76; -.
DR ProteinModelPortal; P23588; -.
DR SMR; P23588; 96-176.
DR IntAct; P23588; 21.
DR MINT; MINT-210187; -.
DR STRING; 9606.ENSP00000262056; -.
DR PhosphoSite; P23588; -.
DR DMDM; 205371761; -.
DR PaxDb; P23588; -.
DR PRIDE; P23588; -.
DR Ensembl; ENST00000262056; ENSP00000262056; ENSG00000063046.
DR GeneID; 1975; -.
DR KEGG; hsa:1975; -.
DR UCSC; uc001sbh.4; human.
DR CTD; 1975; -.
DR GeneCards; GC12P053400; -.
DR HGNC; HGNC:3285; EIF4B.
DR HPA; CAB019440; -.
DR MIM; 603928; gene.
DR neXtProt; NX_P23588; -.
DR PharmGKB; PA27713; -.
DR eggNOG; NOG238591; -.
DR HOGENOM; HOG000006553; -.
DR HOVERGEN; HBG006129; -.
DR InParanoid; P23588; -.
DR KO; K03258; -.
DR OrthoDB; EOG7MKW86; -.
DR PhylomeDB; P23588; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P23588; -.
DR GeneWiki; EIF4B; -.
DR GenomeRNAi; 1975; -.
DR NextBio; 7995; -.
DR PMAP-CutDB; P23588; -.
DR PRO; PR:P23588; -.
DR ArrayExpress; P23588; -.
DR Bgee; P23588; -.
DR CleanEx; HS_EIF4B; -.
DR Genevestigator; P23588; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Initiation factor; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1 611 Eukaryotic translation initiation factor
FT 4B.
FT /FTId=PRO_0000081616.
FT DOMAIN 96 173 RRM.
FT COMPBIAS 164 331 Arg-rich.
FT COMPBIAS 169 325 Asp-rich.
FT MOD_RES 93 93 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine.
FT MOD_RES 219 219 Phosphoserine.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 406 406 Phosphoserine.
FT MOD_RES 412 412 Phosphothreonine.
FT MOD_RES 418 418 Phosphoserine.
FT MOD_RES 422 422 Phosphoserine; by RPS6KA1 and RPS6KB1.
FT MOD_RES 425 425 Phosphoserine.
FT MOD_RES 445 445 Phosphoserine.
FT MOD_RES 459 459 Phosphoserine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 504 504 Phosphoserine.
FT MOD_RES 586 586 N6-acetyllysine.
FT MOD_RES 597 597 Phosphoserine.
FT VARIANT 203 203 P -> R (found in a renal cell carcinoma
FT case; somatic mutation).
FT /FTId=VAR_064710.
FT CONFLICT 164 164 R -> K (in Ref. 4; BAD96248).
FT CONFLICT 246 246 R -> C (in Ref. 6; AAH98437).
FT CONFLICT 343 343 K -> E (in Ref. 1; CAA39265).
FT CONFLICT 391 392 LD -> WN (in Ref. 1; CAA39265).
FT CONFLICT 471 471 L -> Q (in Ref. 6; AAH73154).
FT CONFLICT 486 486 K -> R (in Ref. 4; BAD96248).
FT CONFLICT 611 611 E -> D (in Ref. 3; CAG33239).
FT STRAND 92 94
FT STRAND 96 102
FT HELIX 109 115
FT TURN 116 118
FT STRAND 121 125
FT TURN 130 133
FT STRAND 140 146
FT HELIX 147 154
FT HELIX 155 157
FT STRAND 167 170
SQ SEQUENCE 611 AA; 69151 MW; 31CEFEA865FB10D2 CRC64;
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD VSTTWHSNDD
DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTEE SIKEFFRGLN
ISAVRLPREP SNPERLKGFG YAEFEDLDSL LSALSLNEES LGNRRIRVDV ADQAQDKDRD
DRSFGRDRNR DSDKTDTDWR ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG
YRDGPRRDMD RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS TSQSTRAASI
FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP RERHPSWRSE ETQERERSRT
GSESSQTGTS TTSSRNARRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK
ENAWVKRSSN PPARSQSSDT EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT
GNSSRGPGDG GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG
EDENEGEDYA E
//
ID IF4B_HUMAN Reviewed; 611 AA.
AC P23588; Q4G0E3; Q53HQ2; Q6GPH5; Q6IB46; Q8WYK5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Eukaryotic translation initiation factor 4B;
DE Short=eIF-4B;
GN Name=EIF4B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2390971;
RA Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.;
RT "Cloning and expression of eukaryotic initiation factor 4B cDNA:
RT sequence determination identifies a common RNA recognition motif.";
RL EMBO J. 9:2783-2790(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RA Yokoyama K.;
RT "Human eukaryotic initiation factor 4B.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242;
RP 340-372; 380-398; 473-486 AND 512-537, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP CHARACTERIZATION.
RX PubMed=8139536;
RA Methot N., Pause A., Hershey J.W., Sonenberg N.;
RT "The translation initiation factor eIF-4B contains an RNA-binding
RT region that is distinct and independent from its ribonucleoprotein
RT consensus sequence.";
RL Mol. Cell. Biol. 14:2307-2316(1994).
RN [9]
RP CHARACTERIZATION.
RX PubMed=8816444;
RA Methot N., Song M.S., Sonenberg N.;
RT "A region rich in aspartic acid, arginine, tyrosine, and glycine
RT (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-
RT association and interaction with eIF3.";
RL Mol. Cell. Biol. 16:5328-5334(1996).
RN [10]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=15071500; DOI=10.1038/sj.emboj.7600193;
RA Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D.,
RA Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.;
RT "Phosphorylation of eucaryotic translation initiation factor 4B Ser422
RT is modulated by S6 kinases.";
RL EMBO J. 23:1761-1769(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION AT SER-422.
RX PubMed=16763566; DOI=10.1038/sj.emboj.7601166;
RA Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B.,
RA Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.;
RT "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its
RT phosphorylation and activity.";
RL EMBO J. 25:2781-2791(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283;
RP SER-459 AND SER-597, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219;
RP SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418;
RP SER-425; SER-445; SER-498; SER-504 AND SER-597, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP STRUCTURE BY NMR OF 88-178.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain of eukaryotic initiation
RT factor 4B.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [24]
RP VARIANT ARG-203.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Required for the binding of mRNA to ribosomes. Functions
CC in close association with EIF4-F and EIF4-A. Binds near the 5'-
CC terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the
CC ATPase activity and the ATP-dependent RNA unwinding activity of
CC both EIF4-A and EIF4-F.
CC -!- SUBUNIT: Self-associates and interacts with EIF3 p170 subunit.
CC -!- INTERACTION:
CC P53350:PLK1; NbExp=3; IntAct=EBI-970310, EBI-476768;
CC -!- PTM: Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1;
CC phosphorylation enhances the affinity of EIF4B for the EIF3
CC complex.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X55733; CAA39265.1; -; Genomic_DNA.
DR EMBL; AB076839; BAB82380.1; -; mRNA.
DR EMBL; CR456958; CAG33239.1; -; mRNA.
DR EMBL; AK222528; BAD96248.1; -; mRNA.
DR EMBL; CH471054; EAW96657.1; -; Genomic_DNA.
DR EMBL; BC073139; AAH73139.1; -; mRNA.
DR EMBL; BC073154; AAH73154.1; -; mRNA.
DR EMBL; BC098437; AAH98437.1; -; mRNA.
DR PIR; S12566; S12566.
DR RefSeq; NP_001408.2; NM_001417.4.
DR UniGene; Hs.648394; -.
DR UniGene; Hs.702041; -.
DR PDB; 1WI8; NMR; -; A=88-178.
DR PDB; 2J76; NMR; -; E=78-176.
DR PDBsum; 1WI8; -.
DR PDBsum; 2J76; -.
DR ProteinModelPortal; P23588; -.
DR SMR; P23588; 96-176.
DR IntAct; P23588; 21.
DR MINT; MINT-210187; -.
DR STRING; 9606.ENSP00000262056; -.
DR PhosphoSite; P23588; -.
DR DMDM; 205371761; -.
DR PaxDb; P23588; -.
DR PRIDE; P23588; -.
DR Ensembl; ENST00000262056; ENSP00000262056; ENSG00000063046.
DR GeneID; 1975; -.
DR KEGG; hsa:1975; -.
DR UCSC; uc001sbh.4; human.
DR CTD; 1975; -.
DR GeneCards; GC12P053400; -.
DR HGNC; HGNC:3285; EIF4B.
DR HPA; CAB019440; -.
DR MIM; 603928; gene.
DR neXtProt; NX_P23588; -.
DR PharmGKB; PA27713; -.
DR eggNOG; NOG238591; -.
DR HOGENOM; HOG000006553; -.
DR HOVERGEN; HBG006129; -.
DR InParanoid; P23588; -.
DR KO; K03258; -.
DR OrthoDB; EOG7MKW86; -.
DR PhylomeDB; P23588; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P23588; -.
DR GeneWiki; EIF4B; -.
DR GenomeRNAi; 1975; -.
DR NextBio; 7995; -.
DR PMAP-CutDB; P23588; -.
DR PRO; PR:P23588; -.
DR ArrayExpress; P23588; -.
DR Bgee; P23588; -.
DR CleanEx; HS_EIF4B; -.
DR Genevestigator; P23588; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Initiation factor; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1 611 Eukaryotic translation initiation factor
FT 4B.
FT /FTId=PRO_0000081616.
FT DOMAIN 96 173 RRM.
FT COMPBIAS 164 331 Arg-rich.
FT COMPBIAS 169 325 Asp-rich.
FT MOD_RES 93 93 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine.
FT MOD_RES 219 219 Phosphoserine.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 406 406 Phosphoserine.
FT MOD_RES 412 412 Phosphothreonine.
FT MOD_RES 418 418 Phosphoserine.
FT MOD_RES 422 422 Phosphoserine; by RPS6KA1 and RPS6KB1.
FT MOD_RES 425 425 Phosphoserine.
FT MOD_RES 445 445 Phosphoserine.
FT MOD_RES 459 459 Phosphoserine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 504 504 Phosphoserine.
FT MOD_RES 586 586 N6-acetyllysine.
FT MOD_RES 597 597 Phosphoserine.
FT VARIANT 203 203 P -> R (found in a renal cell carcinoma
FT case; somatic mutation).
FT /FTId=VAR_064710.
FT CONFLICT 164 164 R -> K (in Ref. 4; BAD96248).
FT CONFLICT 246 246 R -> C (in Ref. 6; AAH98437).
FT CONFLICT 343 343 K -> E (in Ref. 1; CAA39265).
FT CONFLICT 391 392 LD -> WN (in Ref. 1; CAA39265).
FT CONFLICT 471 471 L -> Q (in Ref. 6; AAH73154).
FT CONFLICT 486 486 K -> R (in Ref. 4; BAD96248).
FT CONFLICT 611 611 E -> D (in Ref. 3; CAG33239).
FT STRAND 92 94
FT STRAND 96 102
FT HELIX 109 115
FT TURN 116 118
FT STRAND 121 125
FT TURN 130 133
FT STRAND 140 146
FT HELIX 147 154
FT HELIX 155 157
FT STRAND 167 170
SQ SEQUENCE 611 AA; 69151 MW; 31CEFEA865FB10D2 CRC64;
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD VSTTWHSNDD
DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTEE SIKEFFRGLN
ISAVRLPREP SNPERLKGFG YAEFEDLDSL LSALSLNEES LGNRRIRVDV ADQAQDKDRD
DRSFGRDRNR DSDKTDTDWR ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG
YRDGPRRDMD RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS TSQSTRAASI
FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP RERHPSWRSE ETQERERSRT
GSESSQTGTS TTSSRNARRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK
ENAWVKRSSN PPARSQSSDT EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT
GNSSRGPGDG GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG
EDENEGEDYA E
//
MIM
603928
*RECORD*
*FIELD* NO
603928
*FIELD* TI
*603928 EUKARYOTIC TRANSLATION INITIATION FACTOR 4B; EIF4B
*FIELD* TX
Eukaryotic translation initiation factor 4B (eIF4B) facilitates the
read morebinding of mRNA to the 43S preinitiation complex, which consists of the
40S ribosomal subunit bound to a ternary complex of eIF2, GTP, and
Met-tRNA stabilized by eIF3 (see p66; 603915). eIF4F, a heterotrimeric
protein, binds to the mRNA cap structure and, in combination with eIF4B,
is thought to unwind the secondary structure in the 5-prime untranslated
region of the mRNA to facilitate ribosome binding. Besides its
RNA-binding activity, eIF4B stimulates the ATPase and RNA helicase
activities of eIF4A (602641), one component of eIF4F (Methot et al.
(1996)).
By screening a fetal liver library with degenerate oligonucleotide
probes based on the partial protein sequence of HeLa cell eIF4B, Milburn
et al. (1990) isolated a partial cDNA encoding human eIF4B. They used
the partial cDNA to screen an osteosarcoma library and recovered
additional cDNAs corresponding to 2 distinct transcripts that had the
same coding region but 3-prime ends of different lengths. Northern blot
analysis revealed that eIF4B is expressed as 4.4- and 2.3-kb mRNAs in
human cell lines. Milburn et al. (1990) determined that the 2 mRNAs
differ by alternate utilization of polyadenylation signals. The
predicted 611-amino acid eIF4B protein contains a consensus RNA-binding
site (RNP-CS) near the N terminus, a central domain rich in aspartic
acid, arginine, tyrosine, and glycine (DRYG-rich), and a C-terminal
region with a large number of polar residues. The authors suggested that
the highly polar DRYG region may account for the aberrant migration of
eIF4B by SDS-PAGE: the factor has a predicted molecular weight of 70 kD,
but an apparent molecular weight of 80 kD. Overexpression of eIF4B in
mammalian cells inhibited translation. Southern blot analysis suggested
that there are multiple eIF4B genes or pseudogenes in the human genome.
Methot et al. (1994) determined that both the RNA recognition motif
(RRM)/RNP-CS and a C-terminal RNA-binding region are essential for eIF4B
function. Methot et al. (1996) demonstrated that the DRYG domain of
eIF4B mediates self-association and interaction with the p170 (602039)
subunit of eIF3. They proposed that eIF4B serves as a bridge between the
mRNA and the 40S ribosomal subunit, by binding both mRNA and 18S
ribosomal RNA. The direct interaction between eIF4B and eIF3, which is
present on the 43S preinitiation complex prior to mRNA binding, provides
an additional link between the mRNA and the ribosome.
*FIELD* RF
1. Methot, N.; Pause, A.; Hershey, J. W.; Sonenberg, N.: The translation
initiation factor eIF-4B contains an RNA-binding region that is distinct
and independent from its ribonucleoprotein consensus sequence. Molec.
Cell. Biol. 14: 2307-2316, 1994.
2. Methot, N.; Song, M. S.; Sonenberg, N.: A region rich in aspartic
acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation
factor 4B (eIF4B) self-association and interaction with eIF3. Molec.
Cell. Biol. 16: 5328-5334, 1996.
3. Milburn, S. C.; Hershey, J. W. B.; Davies, M. V.; Kelleher, K.;
Kaufman, R. J.: Cloning and expression of eukaryotic initiation factor
4B cDNA: sequence determination identifies a common RNA recognition
motif. EMBO J. 9: 2783-2790, 1990.
*FIELD* CD
Rebekah S. Rasooly: 6/21/1999
*FIELD* ED
alopez: 06/22/1999
alopez: 6/21/1999
*RECORD*
*FIELD* NO
603928
*FIELD* TI
*603928 EUKARYOTIC TRANSLATION INITIATION FACTOR 4B; EIF4B
*FIELD* TX
Eukaryotic translation initiation factor 4B (eIF4B) facilitates the
read morebinding of mRNA to the 43S preinitiation complex, which consists of the
40S ribosomal subunit bound to a ternary complex of eIF2, GTP, and
Met-tRNA stabilized by eIF3 (see p66; 603915). eIF4F, a heterotrimeric
protein, binds to the mRNA cap structure and, in combination with eIF4B,
is thought to unwind the secondary structure in the 5-prime untranslated
region of the mRNA to facilitate ribosome binding. Besides its
RNA-binding activity, eIF4B stimulates the ATPase and RNA helicase
activities of eIF4A (602641), one component of eIF4F (Methot et al.
(1996)).
By screening a fetal liver library with degenerate oligonucleotide
probes based on the partial protein sequence of HeLa cell eIF4B, Milburn
et al. (1990) isolated a partial cDNA encoding human eIF4B. They used
the partial cDNA to screen an osteosarcoma library and recovered
additional cDNAs corresponding to 2 distinct transcripts that had the
same coding region but 3-prime ends of different lengths. Northern blot
analysis revealed that eIF4B is expressed as 4.4- and 2.3-kb mRNAs in
human cell lines. Milburn et al. (1990) determined that the 2 mRNAs
differ by alternate utilization of polyadenylation signals. The
predicted 611-amino acid eIF4B protein contains a consensus RNA-binding
site (RNP-CS) near the N terminus, a central domain rich in aspartic
acid, arginine, tyrosine, and glycine (DRYG-rich), and a C-terminal
region with a large number of polar residues. The authors suggested that
the highly polar DRYG region may account for the aberrant migration of
eIF4B by SDS-PAGE: the factor has a predicted molecular weight of 70 kD,
but an apparent molecular weight of 80 kD. Overexpression of eIF4B in
mammalian cells inhibited translation. Southern blot analysis suggested
that there are multiple eIF4B genes or pseudogenes in the human genome.
Methot et al. (1994) determined that both the RNA recognition motif
(RRM)/RNP-CS and a C-terminal RNA-binding region are essential for eIF4B
function. Methot et al. (1996) demonstrated that the DRYG domain of
eIF4B mediates self-association and interaction with the p170 (602039)
subunit of eIF3. They proposed that eIF4B serves as a bridge between the
mRNA and the 40S ribosomal subunit, by binding both mRNA and 18S
ribosomal RNA. The direct interaction between eIF4B and eIF3, which is
present on the 43S preinitiation complex prior to mRNA binding, provides
an additional link between the mRNA and the ribosome.
*FIELD* RF
1. Methot, N.; Pause, A.; Hershey, J. W.; Sonenberg, N.: The translation
initiation factor eIF-4B contains an RNA-binding region that is distinct
and independent from its ribonucleoprotein consensus sequence. Molec.
Cell. Biol. 14: 2307-2316, 1994.
2. Methot, N.; Song, M. S.; Sonenberg, N.: A region rich in aspartic
acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation
factor 4B (eIF4B) self-association and interaction with eIF3. Molec.
Cell. Biol. 16: 5328-5334, 1996.
3. Milburn, S. C.; Hershey, J. W. B.; Davies, M. V.; Kelleher, K.;
Kaufman, R. J.: Cloning and expression of eukaryotic initiation factor
4B cDNA: sequence determination identifies a common RNA recognition
motif. EMBO J. 9: 2783-2790, 1990.
*FIELD* CD
Rebekah S. Rasooly: 6/21/1999
*FIELD* ED
alopez: 06/22/1999
alopez: 6/21/1999