Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P23588 (IF4B_HUMAN)

Last modified November 3, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Eukaryotic translation initiation factor 4B
      Short name=eIF-4B
Gene names
Name: EIF4B
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

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.10 Ref.16
Modified residue1921Phosphoserine Ref.13
Modified residue2191Phosphoserine Ref.16
Modified residue2831Phosphoserine Ref.16
Modified residue4061Phosphoserine Ref.12 Ref.15
Modified residue4221Phosphoserine Ref.11 Ref.14
Modified residue4251Phosphoserine Ref.11
Modified residue4451Phosphoserine Ref.12
Modified residue4591Phosphoserine Ref.16 Ref.13 Ref.12
Modified residue4611Phosphothreonine Ref.13
Modified residue4951Phosphoserine Ref.16 Ref.13
Modified residue4971Phosphoserine By similarity
Modified residue4981Phosphoserine Ref.10 Ref.16
Modified residue5041Phosphoserine Ref.10 Ref.16 Ref.12 Ref.11
Modified residue5861N6-acetyllysine Ref.18
Modified residue5971Phosphoserine Ref.16

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
P23588-1 [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: 2390971] [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: 15489334] [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, 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: 8139536] [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: 8816444] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-498 AND SER-504, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-425 AND SER-504, MASS SPECTROMETRY.
[12]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-445; SER-459 AND SER-504, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-459; THR-461 AND SER-495, MASS SPECTROMETRY.
[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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, MASS SPECTROMETRY.
[16]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459; SER-495; SER-498; SER-504 AND SER-597, MASS SPECTROMETRY.
[17]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, MASS SPECTROMETRY.
[19]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00012079.
PIRS12566.
RefSeqNP_001408.2.
UniGeneHs.648394
Hs.702041

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WI8NMR-A88-178[»]
2J76NMR-E78-176[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP23588.

PTM databases

PhosphoSiteP23588.

Proteomic databases

PRIDEP23588.

Genome annotation databases

EnsemblENST00000262056; ENSP00000262056; ENSG00000063046; Homo sapiens. [Genome view]
ENST00000416762; ENSP00000412530; ENSG00000063046; Homo sapiens. [Genome view]
ENST00000420463; ENSP00000388806; ENSG00000063046; Homo sapiens. [Genome view]
ENST00000430205; ENSP00000414531; ENSG00000063046; Homo sapiens. [Genome view]
ENST00000438209; ENSP00000396578; ENSG00000063046; Homo sapiens. [Genome view]
GeneID1975.
KEGGhsa:1975.
UCSCuc001sbh.2. human.

Organism-specific databases

CTD1975.
GeneCardsGC12P051686.
H-InvDBHIX0033725.
HGNCHGNC:3285. EIF4B.
HPACAB019440.
MIM603928. gene.
PharmGKBPA27713.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP23588.
HOVERGENP23588.
OMAGPRRDMD.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_498. Signaling by Insulin receptor.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP23588.
BgeeP23588.
CleanExHS_EIF4B.
GenevestigatorP23588.
GermOnlineENSG00000063046. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

PMAP-CutDBP23588.
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: November 3, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

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

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents