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UniProtKB/Swiss-Prot entry P23588


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IF4B_HUMAN
Primary accession number P23588
Secondary accession numbers Q4G0E3 Q53HQ2 Q6GPH5 Q6IB46 Q8WYK5
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on September 2, 2008 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 90)
Name and origin of the protein
Protein name Eukaryotic translation initiation factor 4B
Synonym eIF-4B
Gene name
Name: EIF4B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2390971 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix carcinoma;
Yokoyama K.;
"Human eukaryotic initiation factor 4B.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Testis, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242; 340-372; 380-398; 473-486 AND 512-537, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Calvo F., Kolch W.;
Submitted (MAR-2008) to UniProtKB.
[8]
CHARACTERIZATION.
PubMed=8139536 [NCBI, ExPASy, EBI, Israel, Japan]
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.";
Mol. Cell. Biol. 14:2307-2316(1994).
[9]
CHARACTERIZATION.
PubMed=8816444 [NCBI, ExPASy, EBI, Israel, Japan]
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.";
Mol. Cell. Biol. 16:5328-5334(1996).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-498 AND SER-504, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-425 AND SER-504, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-445; SER-459 AND SER-504, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-459; THR-461 AND SER-495, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459; SER-495; SER-498; SER-504 AND SER-597, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[18]
STRUCTURE BY NMR OF 88-178.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RNA binding domain of eukaryotic initiation factor 4B.";
Submitted (NOV-2004) to the PDB data bank.
Comments
  • FUNCTION: Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
  • SUBUNIT: Self-associates and interacts with EIF3 p170 subunit.
  • SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X55733; CAA39265.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB076839; BAB82380.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456958; CAG33239.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222528; BAD96248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471054; EAW96657.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073139; AAH73139.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073154; AAH73154.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC098437; AAH98437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00012079; -.
PIR S12566; S12566.
RefSeq NP_001408.2; -.
UniGene Hs.648394
3D structure databases
PDB
1WI8; NMR; -; A=88-178.[ExPASy / RCSB / EBI]
2J76; NMR; -; E=78-176.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WI8; -.
2J76; -.
ModBase P23588.
PTM databases
PhosphoSite P23588; -.
Enzyme and pathway databases
Reactome REACT_1762; 3' -UTR-mediated translational regulation.
REACT_498; Signaling by Insulin receptor.
REACT_71; Gene Expression.
Organism-specific databases
GeneCards GC12P051686; -.
H-InvDB HIX0033725; -.
HGNC HGNC:3285; EIF4B.
GenAtlas EIF4B.
HPA CAB019440; -.
MIM 603928; gene. [NCBI / EBI]
PharmGKB PA27713; -.
Gene expression databases
ArrayExpress P23588; -.
Bgee P23588; -.
CleanEx HS_EIF4B; -.
GermOnline ENSG00000063046; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0016281; Cellular component: eukaryotic translation initiation factor 4F complex (traceable author statement from ProtInc).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0003743; Molecular function: translation initiation factor activity (traceable author statement from ProtInc).
GO:0006446; Biological process: regulation of translational initiation (traceable author statement from ProtInc).
GO:0006412; Biological process: translation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
Pfam PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 1.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P23588; -.
Genome annotation databases
Ensembl ENSG00000063046; Homo sapiens. [Contig view]
GeneID 1975; -.
KEGG hsa:1975; -.
Phylogenomic databases
HOGENOM P23588; -.
HOVERGEN P23588; -.
OMA P23588; GPRRDMD.
Other
PMAP-CutDB P23588; -.
SOURCE EIF4B; Homo sapiens.
ProtoNet P23588.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Initiation factor; Phosphoprotein; Protein biosynthesis; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   611  611     Eukaryotic translation initiation factor 4B. PRO_0000081616
DOMAIN   96   173  78     RRM. 
COMPBIAS   164   331  168     Arg-rich. 
COMPBIAS   169   325  157     Asp-rich. 
MOD_RES   93    93        Phosphoserine. 
MOD_RES   192   192        Phosphoserine. 
MOD_RES   219   219        Phosphoserine. 
MOD_RES   283   283        Phosphoserine. 
MOD_RES   406   406        Phosphoserine. 
MOD_RES   422   422        Phosphoserine. 
MOD_RES   425   425        Phosphoserine. 
MOD_RES   445   445        Phosphoserine. 
MOD_RES   459   459        Phosphoserine. 
MOD_RES   461   461        Phosphothreonine. 
MOD_RES   495   495        Phosphoserine. 
MOD_RES   497   497        Phosphoserine (By similarity). 
MOD_RES   498   498        Phosphoserine. 
MOD_RES   504   504        Phosphoserine. 
MOD_RES   597   597        Phosphoserine. 
CONFLICT   164   164        R -> K (in Ref. 4; BAD96248). 
CONFLICT   246   246        R -> C (in Ref. 6; AAH98437). 
CONFLICT   343   343        K -> E (in Ref. 1; CAA39265). 
CONFLICT   391   392        LD -> WN (in Ref. 1; CAA39265). 
CONFLICT   471   471        L -> Q (in Ref. 6; AAH73154). 
CONFLICT   486   486        K -> R (in Ref. 4; BAD96248). 
CONFLICT   611   611        E -> D (in Ref. 3; CAG33239). 
STRAND   92    94  3      
STRAND   96   102  7      
HELIX   109   115  7      
TURN   116   118  3      
STRAND   121   125  5      
STRAND   140   146  7      
HELIX   147   154  8      
HELIX   155   157  3      
STRAND   167   170  4      
Sequence information
Length: 611 AA [This is the length of the unprocessed precursor] Molecular weight: 69151 Da [This is the MW of the unprocessed precursor] CRC64: 31CEFEA865FB10D2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD VSTTWHSNDD 

        70         80         90        100        110        120 
DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTEE SIKEFFRGLN 

       130        140        150        160        170        180 
ISAVRLPREP SNPERLKGFG YAEFEDLDSL LSALSLNEES LGNRRIRVDV ADQAQDKDRD 

       190        200        210        220        230        240 
DRSFGRDRNR DSDKTDTDWR ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG 

       250        260        270        280        290        300 
YRDGPRRDMD RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED 

       310        320        330        340        350        360 
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS TSQSTRAASI 

       370        380        390        400        410        420 
FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP RERHPSWRSE ETQERERSRT 

       430        440        450        460        470        480 
GSESSQTGTS TTSSRNARRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK 

       490        500        510        520        530        540 
ENAWVKRSSN PPARSQSSDT EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT 

       550        560        570        580        590        600 
GNSSRGPGDG GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG 

       610 
EDENEGEDYA E 

P23588 in FASTA format

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