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Q14240

- IF4A2_HUMAN

UniProt

Q14240 - IF4A2_HUMAN

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Protein

Eukaryotic initiation factor 4A-II

Gene
EIF4A2, DDX2B, EIF4F
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 848ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. helicase activity Source: ProtInc
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. translation initiation factor activity Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  6. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  7. regulation of translational initiation Source: ProtInc
  8. RNA metabolic process Source: Reactome
  9. translation Source: Reactome
  10. translational initiation Source: Reactome
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic initiation factor 4A-II (EC:3.6.4.13)
Short name:
eIF-4A-II
Short name:
eIF4A-II
Alternative name(s):
ATP-dependent RNA helicase eIF4A-2
Gene namesi
Name:EIF4A2
Synonyms:DDX2B, EIF4F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3284. EIF4A2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Eukaryotic initiation factor 4A-IIPRO_0000054938Add
BLAST

Proteomic databases

MaxQBiQ14240.
PaxDbiQ14240.
PRIDEiQ14240.

PTM databases

PhosphoSiteiQ14240.

Miscellaneous databases

PMAP-CutDBQ14240.

Expressioni

Gene expression databases

ArrayExpressiQ14240.
BgeeiQ14240.
CleanExiHS_EIF4A2.
GenevestigatoriQ14240.

Organism-specific databases

HPAiCAB011690.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279584EBI-73473,EBI-6904388From a different organism.

Protein-protein interaction databases

BioGridi108290. 41 interactions.
IntActiQ14240. 18 interactions.
MINTiMINT-202114.
STRINGi9606.ENSP00000326381.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 373
Helixi42 – 5110
Helixi58 – 6811
Beta strandi73 – 753
Helixi81 – 9414
Beta strandi104 – 1074
Helixi111 – 12414
Turni125 – 1295
Beta strandi132 – 1354
Beta strandi154 – 1585
Helixi160 – 1689
Beta strandi179 – 1846
Helixi185 – 1906
Helixi194 – 20310
Beta strandi209 – 2135
Helixi219 – 22810
Beta strandi233 – 2353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BORX-ray1.85A22-240[»]
ProteinModelPortaliQ14240.
SMRiQ14240. Positions 23-401.

Miscellaneous databases

EvolutionaryTraceiQ14240.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 235172Helicase ATP-bindingAdd
BLAST
Domaini246 – 407162Helicase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi33 – 6129Q motifAdd
BLAST
Motifi183 – 1864DEAD box

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0513.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiQ14240.
KOiK03257.
OMAiMQLNFPH.
PhylomeDBiQ14240.
TreeFamiTF101524.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. 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]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14240-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA    50
YGFEKPSAIQ QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK 100
ETQALVLAPT RELAQQIQKV ILALGDYMGA TCHACIGGTN VRNEMQKLQA 150
EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF VLDEADEMLS RGFKDQIYEI 200
FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE ELTLEGIKQF 250
YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV 300
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL 350
PTNRENYIHR IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP 400
MNVADLI 407
Length:407
Mass (Da):46,402
Last modified:March 15, 2004 - v2
Checksum:iFAA7D3BA9D8C6DA0
GO
Isoform 2 (identifier: Q14240-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:408
Mass (Da):46,489
Checksum:i0F47C0C4EEF00DD3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931Q → H.
Corresponds to variant rs11538616 [ dbSNP | Ensembl ].
VAR_052158
Natural varianti181 – 1811V → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035838

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 91N → NS in isoform 2. VSP_009629

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271N → S in AAH15842. 1 Publication
Sequence conflicti212 – 2132LL → FA in BAA06336. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3282.1. [Q14240-1]
RefSeqiNP_001958.2. NM_001967.3. [Q14240-1]
UniGeneiHs.518475.
Hs.599481.

Genome annotation databases

EnsembliENST00000323963; ENSP00000326381; ENSG00000156976. [Q14240-1]
ENST00000440191; ENSP00000398370; ENSG00000156976. [Q14240-2]
GeneIDi1974.
KEGGihsa:1974.
UCSCiuc003fqs.3. human. [Q14240-1]
uc003fqu.3. human. [Q14240-2]

Polymorphism databases

DMDMi45645183.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3282.1. [Q14240-1 ]
RefSeqi NP_001958.2. NM_001967.3. [Q14240-1 ]
UniGenei Hs.518475.
Hs.599481.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BOR X-ray 1.85 A 22-240 [» ]
ProteinModelPortali Q14240.
SMRi Q14240. Positions 23-401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108290. 41 interactions.
IntActi Q14240. 18 interactions.
MINTi MINT-202114.
STRINGi 9606.ENSP00000326381.

PTM databases

PhosphoSitei Q14240.

Polymorphism databases

DMDMi 45645183.

Proteomic databases

MaxQBi Q14240.
PaxDbi Q14240.
PRIDEi Q14240.

Protocols and materials databases

DNASUi 1974.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323963 ; ENSP00000326381 ; ENSG00000156976 . [Q14240-1 ]
ENST00000440191 ; ENSP00000398370 ; ENSG00000156976 . [Q14240-2 ]
GeneIDi 1974.
KEGGi hsa:1974.
UCSCi uc003fqs.3. human. [Q14240-1 ]
uc003fqu.3. human. [Q14240-2 ]

Organism-specific databases

CTDi 1974.
GeneCardsi GC03P186556.
H-InvDB HIX0003899.
HGNCi HGNC:3284. EIF4A2.
HPAi CAB011690.
MIMi 601102. gene.
neXtProti NX_Q14240.
PharmGKBi PA27712.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
HOGENOMi HOG000268797.
HOVERGENi HBG107989.
InParanoidi Q14240.
KOi K03257.
OMAi MQLNFPH.
PhylomeDBi Q14240.
TreeFami TF101524.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF4A2. human.
EvolutionaryTracei Q14240.
GeneWikii EIF4A2.
GenomeRNAii 1974.
NextBioi 7991.
PMAP-CutDB Q14240.
PROi Q14240.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14240.
Bgeei Q14240.
CleanExi HS_EIF4A2.
Genevestigatori Q14240.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. 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 ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-181.

Entry informationi

Entry nameiIF4A2_HUMAN
AccessioniPrimary (citable) accession number: Q14240
Secondary accession number(s): D3DNU9
, Q53XJ6, Q96B90, Q96EA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 15, 2004
Last modified: September 3, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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