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P23588 (IF4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4B

Short name=eIF-4B
Gene names
Name:EIF4B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

Self-associates and interacts with EIF3 p170 subunit.

Post-translational modification

Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex. Ref.10 Ref.12

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityPolymorphism
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

regulation of translational initiation

Traceable author statement Ref.1. Source: ProtInc

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

translation initiation factor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PLK1P533503EBI-970310,EBI-476768

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Eukaryotic translation initiation factor 4B
PRO_0000081616

Regions

Domain96 – 17378RRM
Compositional bias164 – 331168Arg-rich
Compositional bias169 – 325157Asp-rich

Amino acid modifications

Modified residue931Phosphoserine Ref.15 Ref.19
Modified residue1921Phosphoserine Ref.19
Modified residue2191Phosphoserine Ref.15 Ref.19
Modified residue2831Phosphoserine Ref.15
Modified residue3651N6-acetyllysine By similarity
Modified residue4061Phosphoserine Ref.11 Ref.19 Ref.21
Modified residue4121Phosphothreonine Ref.21
Modified residue4181Phosphoserine Ref.21
Modified residue4221Phosphoserine; by RPS6KA1 and RPS6KB1 Ref.10 Ref.12 Ref.19
Modified residue4251Phosphoserine Ref.21
Modified residue4451Phosphoserine Ref.11 Ref.19 Ref.21
Modified residue4591Phosphoserine Ref.15
Modified residue4981Phosphoserine Ref.19 Ref.21
Modified residue5041Phosphoserine Ref.19 Ref.21
Modified residue5861N6-acetyllysine Ref.18
Modified residue5971Phosphoserine Ref.15 Ref.17 Ref.19 Ref.21

Natural variations

Natural variant2031P → R Found in a renal cell carcinoma case; somatic mutation. Ref.24
VAR_064710

Experimental info

Sequence conflict1641R → K in BAD96248. Ref.4
Sequence conflict2461R → C in AAH98437. Ref.6
Sequence conflict3431K → E in CAA39265. Ref.1
Sequence conflict391 – 3922LD → WN in CAA39265. Ref.1
Sequence conflict4711L → Q in AAH73154. Ref.6
Sequence conflict4861K → R in BAD96248. Ref.4
Sequence conflict6111E → D in CAG33239. Ref.3

Secondary structure

.................. 611
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23588 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 31CEFEA865FB10D2

FASTA61169,151
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif."
Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.
EMBO J. 9:2783-2790(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Human eukaryotic initiation factor 4B."
Yokoyama K.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adipose tissue.
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Testis and Uterus.
[7]Bienvenut W.V., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242; 340-372; 380-398; 473-486 AND 512-537, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence."
Methot N., Pause A., Hershey J.W., Sonenberg N.
Mol. Cell. Biol. 14:2307-2316(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3."
Methot N., Song M.S., Sonenberg N.
Mol. Cell. Biol. 16:5328-5334(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases."
Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D., Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.
EMBO J. 23:1761-1769(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-422.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity."
Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.
EMBO J. 25:2781-2791(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-422.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219; SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418; SER-425; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Solution structure of the RNA binding domain of eukaryotic initiation factor 4B."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 88-178.
[24]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-203.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55733 Genomic DNA. Translation: CAA39265.1.
AB076839 mRNA. Translation: BAB82380.1.
CR456958 mRNA. Translation: CAG33239.1.
AK222528 mRNA. Translation: BAD96248.1.
CH471054 Genomic DNA. Translation: EAW96657.1.
BC073139 mRNA. Translation: AAH73139.1.
BC073154 mRNA. Translation: AAH73154.1.
BC098437 mRNA. Translation: AAH98437.1.
PIRS12566.
RefSeqNP_001408.2. NM_001417.4.
UniGeneHs.648394.
Hs.702041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI8NMR-A88-178[»]
2J76NMR-E78-176[»]
ProteinModelPortalP23588.
SMRP23588. Positions 96-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108291. 55 interactions.
IntActP23588. 21 interactions.
MINTMINT-210187.
STRING9606.ENSP00000262056.

PTM databases

PhosphoSiteP23588.

Polymorphism databases

DMDM205371761.

Proteomic databases

PaxDbP23588.
PRIDEP23588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262056; ENSP00000262056; ENSG00000063046.
GeneID1975.
KEGGhsa:1975.
UCSCuc001sbh.4. human.

Organism-specific databases

CTD1975.
GeneCardsGC12P053400.
HGNCHGNC:3285. EIF4B.
HPACAB019440.
HPA046164.
MIM603928. gene.
neXtProtNX_P23588.
PharmGKBPA27713.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238591.
HOGENOMHOG000006553.
HOVERGENHBG006129.
InParanoidP23588.
KOK03258.
OrthoDBEOG7MKW86.
PhylomeDBP23588.
TreeFamTF101525.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP23588.
BgeeP23588.
CleanExHS_EIF4B.
GenevestigatorP23588.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23588.
GeneWikiEIF4B.
GenomeRNAi1975.
NextBio7995.
PMAP-CutDBP23588.
PROP23588.
SOURCESearch...

Entry information

Entry nameIF4B_HUMAN
AccessionPrimary (citable) accession number: P23588
Secondary accession number(s): Q4G0E3 expand/collapse secondary AC list , Q53HQ2, Q6GPH5, Q6IB46, Q8WYK5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM