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Q14240 (IF4A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic initiation factor 4A-II

Short name=eIF-4A-II
Short name=eIF4A-II
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase eIF4A-2
Gene names
Name:EIF4A2
Synonyms:DDX2B, EIF4F
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3 By similarity. Interacts with EIF4E. May interact with NOM1. Interacts with HHV-1 Vhs. Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the DEAD box helicase family. eIF4A subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Initiation factor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

gene expression

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

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

helicase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

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

protein binding

Inferred from physical interaction PubMed 11922617. Source: IntAct

translation initiation factor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279583EBI-73473,EBI-6904388From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14240-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14240-2)

The sequence of this isoform differs from the canonical sequence as follows:
     9-9: N → NS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Eukaryotic initiation factor 4A-II
PRO_0000054938

Regions

Domain64 – 235172Helicase ATP-binding
Domain246 – 407162Helicase C-terminal
Nucleotide binding77 – 848ATP By similarity
Motif33 – 6129Q motif
Motif183 – 1864DEAD box

Natural variations

Alternative sequence91N → NS in isoform 2.
VSP_009629
Natural variant931Q → H.
Corresponds to variant rs11538616 [ dbSNP | Ensembl ].
VAR_052158
Natural variant1811V → L in a breast cancer sample; somatic mutation. Ref.11
VAR_035838

Experimental info

Sequence conflict271N → S in AAH15842. Ref.5
Sequence conflict212 – 2132LL → FA in BAA06336. Ref.1

Secondary structure

................................. 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: FAA7D3BA9D8C6DA0

FASTA40746,402
        10         20         30         40         50         60 
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ 

        70         80         90        100        110        120 
QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV 

       130        140        150        160        170        180 
ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF 

       190        200        210        220        230        240 
VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE 

       250        260        270        280        290        300 
ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV 

       310        320        330        340        350        360 
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR 

       370        380        390        400 
IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI 

« Hide

Isoform 2 [UniParc].

Checksum: 0F47C0C4EEF00DD3
Show »

FASTA40846,489

References

« Hide 'large scale' references
[1]"Isolation and mapping of the human EIF4A2 gene homologous to the murine protein synthesis initiation factor 4A-II gene Eif4a2."
Sudo K., Takahashi E., Nakamura Y.
Cytogenet. Cell Genet. 71:385-388(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Bone marrow, Brain, Lymph and Skeletal muscle.
[6]"Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo."
Li W., Belsham G.J., Proud C.G.
J. Biol. Chem. 276:29111-29115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E.
[7]"Identification of NOM1, a nucleolar, eIF4A binding protein encoded within the chromosome 7q36 breakpoint region targeted in cases of pediatric acute myeloid leukemia."
Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.
Gene 347:137-145(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH NOM1.
[8]"mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A."
Feng P., Everly D.N. Jr., Read G.S.
J. Virol. 79:9651-9664(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-1 VHS.
[9]"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].
[10]"Comparative structural analysis of human DEAD-box RNA helicases."
Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M., Thorsell A.G., Schuler H.
PLoS ONE 5:E12791-E12791(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-181.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30655 mRNA. Translation: BAA06336.1.
BT009860 mRNA. Translation: AAP88862.1.
AC112907 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78172.1.
CH471052 Genomic DNA. Translation: EAW78177.1.
BC012547 mRNA. Translation: AAH12547.1.
BC013708 mRNA. Translation: AAH13708.1.
BC015842 mRNA. Translation: AAH15842.1.
BC048105 mRNA. Translation: AAH48105.1.
CCDSCCDS3282.1. [Q14240-1]
RefSeqNP_001958.2. NM_001967.3. [Q14240-1]
UniGeneHs.518475.
Hs.599481.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BORX-ray1.85A22-240[»]
ProteinModelPortalQ14240.
SMRQ14240. Positions 23-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108290. 41 interactions.
IntActQ14240. 18 interactions.
MINTMINT-202114.
STRING9606.ENSP00000326381.

PTM databases

PhosphoSiteQ14240.

Polymorphism databases

DMDM45645183.

Proteomic databases

MaxQBQ14240.
PaxDbQ14240.
PRIDEQ14240.

Protocols and materials databases

DNASU1974.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323963; ENSP00000326381; ENSG00000156976. [Q14240-1]
ENST00000440191; ENSP00000398370; ENSG00000156976. [Q14240-2]
GeneID1974.
KEGGhsa:1974.
UCSCuc003fqs.3. human. [Q14240-1]
uc003fqu.3. human. [Q14240-2]

Organism-specific databases

CTD1974.
GeneCardsGC03P186556.
H-InvDBHIX0003899.
HGNCHGNC:3284. EIF4A2.
HPACAB011690.
MIM601102. gene.
neXtProtNX_Q14240.
PharmGKBPA27712.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG107989.
InParanoidQ14240.
KOK03257.
OMAMQLNFPH.
PhylomeDBQ14240.
TreeFamTF101524.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14240.
BgeeQ14240.
CleanExHS_EIF4A2.
GenevestigatorQ14240.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4A2. human.
EvolutionaryTraceQ14240.
GeneWikiEIF4A2.
GenomeRNAi1974.
NextBio7991.
PMAP-CutDBQ14240.
PROQ14240.
SOURCESearch...

Entry information

Entry nameIF4A2_HUMAN
AccessionPrimary (citable) accession number: Q14240
Secondary accession number(s): D3DNU9 expand/collapse secondary AC list , Q53XJ6, Q96B90, Q96EA8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 150 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 3

Human chromosome 3: entries, gene names and cross-references to MIM