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Q8BGD9 (IF4B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Subunit structure

Self-associates and interacts with EIF3 p170 subunit By similarity.

Post-translational modification

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

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Eukaryotic translation initiation factor 4B
PRO_0000081617

Regions

Domain96 – 17378RRM
Compositional bias164 – 440277Arg-rich
Compositional bias169 – 325157Asp-rich

Amino acid modifications

Modified residue931Phosphoserine Ref.2
Modified residue1921Phosphoserine By similarity
Modified residue2191Phosphoserine By similarity
Modified residue2831Phosphoserine By similarity
Modified residue3651N6-acetyllysine Ref.7
Modified residue4061Phosphoserine Ref.6
Modified residue4121Phosphothreonine By similarity
Modified residue4181Phosphoserine By similarity
Modified residue4221Phosphoserine; by RPS6KA1 and RPS6KB1 By similarity
Modified residue4251Phosphoserine By similarity
Modified residue4451Phosphoserine By similarity
Modified residue4591Phosphoserine By similarity
Modified residue4981Phosphoserine Ref.3
Modified residue5041Phosphoserine By similarity
Modified residue5861N6-acetyllysine By similarity
Modified residue5971Phosphoserine Ref.2 Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8BGD9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A3254EBF55EDB6F2

FASTA61168,840
        10         20         30         40         50         60 
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVPKPVSW ADETDDLEGD VSTTWHSNDD 

        70         80         90        100        110        120 
DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTED SIKDFFRGLN 

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

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

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

       310        320        330        340        350        360 
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPRLNLKPRS APKEDDASAS TSQSSRAASI 

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

       430        440        450        460        470        480 
GSESSQTGAS ATSGRNTRRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK 

       490        500        510        520        530        540 
ENAWVKRSSN PPARSQSSDT EQPSPTSGGG KVAAVQPPEE GPSRKDGNKV DVVGATQGQA 

       550        560        570        580        590        600 
GSCSRGPGDG GSRDHWKDLD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG 

       610 
EDEDEGDDCT E 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
[2]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK045250 mRNA. Translation: BAC32280.1.
AK077423 mRNA. Translation: BAC36793.1.
AK170354 mRNA. Translation: BAE41740.1.
CCDSCCDS49737.1.
RefSeqNP_663600.2. NM_145625.3.
UniGeneMm.290022.
Mm.391795.

3D structure databases

ProteinModelPortalQ8BGD9.
SMRQ8BGD9. Positions 96-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid217684. 3 interactions.
IntActQ8BGD9. 2 interactions.
MINTMINT-1954873.

PTM databases

PhosphoSiteQ8BGD9.

Proteomic databases

MaxQBQ8BGD9.
PaxDbQ8BGD9.
PRIDEQ8BGD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169681; ENSMUSP00000127774; ENSMUSG00000058655.
GeneID75705.
KEGGmmu:75705.
UCSCuc007xuk.2. mouse.

Organism-specific databases

CTD1975.
MGIMGI:95304. Eif4b.

Phylogenomic databases

eggNOGNOG238591.
GeneTreeENSGT00530000063406.
HOGENOMHOG000006553.
HOVERGENHBG006129.
InParanoidQ8BGD9.
KOK03258.
OMASYRDGPR.
OrthoDBEOG7MKW86.
PhylomeDBQ8BGD9.
TreeFamTF101525.

Gene expression databases

ArrayExpressQ8BGD9.
BgeeQ8BGD9.
CleanExMM_EIF4B.
GenevestigatorQ8BGD9.

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

ChiTaRSEIF4B. mouse.
NextBio343748.
PROQ8BGD9.
SOURCESearch...

Entry information

Entry nameIF4B_MOUSE
AccessionPrimary (citable) accession number: Q8BGD9
Secondary accession number(s): Q3TD64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries