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Protein

Eukaryotic translation initiation factor 4B

Gene

Eif4b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_283781. S6K1 signalling.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_298277. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_298772. Deadenylation of mRNA.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4B
Short name:
eIF-4B
Gene namesi
Name:Eif4b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:95304. Eif4b.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 611611Eukaryotic translation initiation factor 4BPRO_0000081617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931Phosphoserine1 Publication
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei365 – 3651N6-acetyllysine1 Publication
Modified residuei406 – 4061Phosphoserine1 Publication
Modified residuei412 – 4121PhosphothreonineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei422 – 4221Phosphoserine; by RPS6KA1 and RPS6KB1By similarity
Modified residuei425 – 4251PhosphoserineBy similarity
Modified residuei445 – 4451PhosphoserineBy similarity
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei498 – 4981Phosphoserine1 Publication
Modified residuei504 – 5041PhosphoserineBy similarity
Modified residuei586 – 5861N6-acetyllysineBy similarity
Modified residuei597 – 5971Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BGD9.
PaxDbiQ8BGD9.
PRIDEiQ8BGD9.

PTM databases

PhosphoSiteiQ8BGD9.

Expressioni

Gene expression databases

BgeeiQ8BGD9.
CleanExiMM_EIF4B.
ExpressionAtlasiQ8BGD9. baseline and differential.
GenevisibleiQ8BGD9. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi217684. 3 interactions.
IntActiQ8BGD9. 2 interactions.
MINTiMINT-1954873.
STRINGi10090.ENSMUSP00000127774.

Structurei

3D structure databases

ProteinModelPortaliQ8BGD9.
SMRiQ8BGD9. Positions 96-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 17378RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi164 – 440277Arg-richAdd
BLAST
Compositional biasi169 – 325157Asp-richAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG238591.
GeneTreeiENSGT00530000063406.
HOGENOMiHOG000006553.
HOVERGENiHBG006129.
InParanoidiQ8BGD9.
KOiK03258.
OMAiWRSKMRP.
OrthoDBiEOG7MKW86.
PhylomeDBiQ8BGD9.
TreeFamiTF101525.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVPKPVSW ADETDDLEGD
60 70 80 90 100
VSTTWHSNDD DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL
110 120 130 140 150
GNLPYDVTED SIKDFFRGLN ISAVRLPREP SNPDRLKGFG YAEFEDLDSL
160 170 180 190 200
LSALSLNEES LGNRRIRVDV ADQAQDKDRD DRSFGRDRNR DSDKTDTDWR
210 220 230 240 250
ARPTTDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG YRDGPRRDMD
260 270 280 290 300
RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED
310 320 330 340 350
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPRLNLKPRS APKEDDASAS
360 370 380 390 400
TSQSSRAASI FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLDRRP
410 420 430 440 450
RERHPSWRSE ETQERERSRT GSESSQTGAS ATSGRNTRRR ESEKSLENET
460 470 480 490 500
LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK ENAWVKRSSN PPARSQSSDT
510 520 530 540 550
EQPSPTSGGG KVAAVQPPEE GPSRKDGNKV DVVGATQGQA GSCSRGPGDG
560 570 580 590 600
GSRDHWKDLD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG
610
EDEDEGDDCT E
Length:611
Mass (Da):68,840
Last modified:March 1, 2003 - v1
Checksum:iA3254EBF55EDB6F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045250 mRNA. Translation: BAC32280.1.
AK077423 mRNA. Translation: BAC36793.1.
AK170354 mRNA. Translation: BAE41740.1.
CCDSiCCDS49737.1.
RefSeqiNP_663600.2. NM_145625.3.
UniGeneiMm.290022.
Mm.391795.

Genome annotation databases

EnsembliENSMUST00000169681; ENSMUSP00000127774; ENSMUSG00000058655.
GeneIDi75705.
KEGGimmu:75705.
UCSCiuc007xuk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045250 mRNA. Translation: BAC32280.1.
AK077423 mRNA. Translation: BAC36793.1.
AK170354 mRNA. Translation: BAE41740.1.
CCDSiCCDS49737.1.
RefSeqiNP_663600.2. NM_145625.3.
UniGeneiMm.290022.
Mm.391795.

3D structure databases

ProteinModelPortaliQ8BGD9.
SMRiQ8BGD9. Positions 96-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217684. 3 interactions.
IntActiQ8BGD9. 2 interactions.
MINTiMINT-1954873.
STRINGi10090.ENSMUSP00000127774.

PTM databases

PhosphoSiteiQ8BGD9.

Proteomic databases

MaxQBiQ8BGD9.
PaxDbiQ8BGD9.
PRIDEiQ8BGD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000169681; ENSMUSP00000127774; ENSMUSG00000058655.
GeneIDi75705.
KEGGimmu:75705.
UCSCiuc007xuk.2. mouse.

Organism-specific databases

CTDi1975.
MGIiMGI:95304. Eif4b.

Phylogenomic databases

eggNOGiNOG238591.
GeneTreeiENSGT00530000063406.
HOGENOMiHOG000006553.
HOVERGENiHBG006129.
InParanoidiQ8BGD9.
KOiK03258.
OMAiWRSKMRP.
OrthoDBiEOG7MKW86.
PhylomeDBiQ8BGD9.
TreeFamiTF101525.

Enzyme and pathway databases

ReactomeiREACT_283781. S6K1 signalling.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_298277. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_298772. Deadenylation of mRNA.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiEif4b. mouse.
NextBioi343748.
PROiQ8BGD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGD9.
CleanExiMM_EIF4B.
ExpressionAtlasiQ8BGD9. baseline and differential.
GenevisibleiQ8BGD9. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  3. 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.

Entry informationi

Entry nameiIF4B_MOUSE
AccessioniPrimary (citable) accession number: Q8BGD9
Secondary accession number(s): Q3TD64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.