Reviewed, UniProtKB/Swiss-Prot P23588 (IF4B_HUMAN)

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 4B
      Short name=eIF-4B

Gene names

Name:

EIF4B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of translational initiation Ref.1 Traceable author statement. Source: ProtInc translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 4F complex Ref.1 Traceable author statement. Source: ProtInc
Molecular function	RNA binding Ref.1 Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro translation initiation factor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 611

611

Eukaryotic translation initiation factor 4B

PRO_0000081616

Regions

Domain

96 – 173

78

RRM

Compositional bias

164 – 331

168

Arg-rich

Compositional bias

169 – 325

157

Asp-rich

Amino acid modifications

Modified residue

93

1

Phosphoserine Ref.10 Ref.16

Modified residue

192

1

Phosphoserine Ref.13

Modified residue

219

1

Phosphoserine Ref.16

Modified residue

283

1

Phosphoserine Ref.16

Modified residue

406

1

Phosphoserine Ref.12 Ref.15

Modified residue

422

1

Phosphoserine Ref.11 Ref.14

Modified residue

425

1

Phosphoserine Ref.11

Modified residue

445

1

Phosphoserine Ref.12

Modified residue

459

1

Phosphoserine Ref.16 Ref.13 Ref.12

Modified residue

461

1

Phosphothreonine Ref.13

Modified residue

495

1

Phosphoserine Ref.16 Ref.13

Modified residue

497

1

Phosphoserine By similarity

Modified residue

498

1

Phosphoserine Ref.10 Ref.16

Modified residue

504

1

Phosphoserine Ref.10 Ref.16 Ref.12 Ref.11

Modified residue

586

1

N6-acetyllysine Ref.18

Modified residue

597

1

Phosphoserine Ref.16

Experimental info

Sequence conflict

164

1

R → K in BAD96248. Ref.4

Sequence conflict

246

1

R → C in AAH98437. Ref.6

Sequence conflict

343

1

K → E in CAA39265. Ref.1

Sequence conflict

391 – 392

2

LD → WN in CAA39265. Ref.1

Sequence conflict

471

1

L → Q in AAH73154. Ref.6

Sequence conflict

486

1

K → R in BAD96248. Ref.4

Sequence conflict

611

1

E → D in CAG33239. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

611

Helix Strand Turn

Details...

Beta strand

92 – 94

3

Beta strand

96 – 102

7

Helix

109 – 115

7

Turn

116 – 118

3

Beta strand

121 – 125

5

Beta strand

140 – 146

7

Helix

147 – 154

8

Helix

155 – 157

3

Beta strand

167 – 170

4

Sequences

	Sequence		Length	Mass (Da)
	P23588-1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 31CEFEA865FB10D2	FASTA	611	69,151
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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.

IPI

IPI00012079.

PIR

S12566.

RefSeq

NP_001408.2.

UniGene

Hs.648394
Hs.702041

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WI8	NMR	-	A	88-178	[»]
2J76	NMR	-	E	78-176	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P23588.

PTM databases

PhosphoSite

P23588.

Proteomic databases

PRIDE

P23588.

Genome annotation databases

Ensembl

ENST00000262056; 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]

GeneID

1975.

KEGG

hsa:1975.

UCSC

uc001sbh.2. human.

Organism-specific databases

CTD

1975.

GeneCards

GC12P051686.

H-InvDB

HIX0033725.

HGNC

HGNC:3285. EIF4B.

HPA

CAB019440.

MIM

603928. gene.

PharmGKB

PA27713.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P23588.

HOVERGEN

P23588.

OMA

GPRRDMD.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_498. Signaling by Insulin receptor.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P23588.

Bgee

P23588.

CleanEx

HS_EIF4B.

Genevestigator

P23588.

GermOnline

ENSG00000063046. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

PMAP-CutDB

P23588.

SOURCE

Search...

Entry information

Entry name

IF4B_HUMAN

Accession

Primary (citable) accession number: P23588
Secondary accession number(s): Q4G0E3 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.