Reviewed, UniProtKB/Swiss-Prot Q14240 (IF4A2_HUMAN)

Names and origin

Protein names

Recommended name:
    Eukaryotic initiation factor 4A-II
      Short name=eIF-4A-II
      Short name=eIF4A-II
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent RNA helicase eIF4A-2

Gene names

Name:	EIF4A2
Synonyms:	DDX2B, EIF4F

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
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 process	Host-virus interaction Protein biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Initiation factor
Technical term	3D-structure
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translational initiation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 4F complex Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Inferred from physical interaction. Source: IntAct translation initiation factor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4G1	Q04637	2	EBI-73473,EBI-73711

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 407

407

Eukaryotic initiation factor 4A-II

PRO_0000054938

Regions

Domain

64 – 235

172

Helicase ATP-binding

Domain

246 – 407

162

Helicase C-terminal

Nucleotide binding

77 – 84

8

ATP By similarity

Motif

33 – 61

29

Q motif

Motif

183 – 186

4

DEAD box

Natural variations

Alternative sequence

9

1

N → NS in isoform 2.

VSP_009629

Natural variant

181

1

V → L in a breast cancer sample; somatic mutation.

VAR_035838

Experimental info

Sequence conflict

27

1

N → S in AAH15842. Ref.2

Sequence conflict

212 – 213

2

LL → FA in BAA06336. Ref.1

Secondary structure

1

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407

Helix Strand Turn

Details...

Helix

35 – 37

3

Helix

42 – 51

10

Helix

58 – 68

11

Beta strand

73 – 75

3

Helix

81 – 94

14

Beta strand

104 – 107

4

Helix

111 – 124

14

Turn

125 – 129

5

Beta strand

132 – 135

4

Beta strand

154 – 158

5

Helix

160 – 168

9

Beta strand

179 – 184

6

Helix

185 – 190

6

Helix

194 – 203

10

Beta strand

209 – 213

5

Helix

219 – 228

10

Beta strand

233 – 235

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: FAA7D3BA9D8C6DA0	FASTA	407	46,402
	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
	Isoform 2 [UniParc]. Checksum: 0F47C0C4EEF00DD3		408	46,489
	10 20 30 40 50 60 MSGGSADYNS REHGGPEGMD PDGVIESNWN EIVDNFDDMN LKESLLRGIY AYGFEKPSAI 70 80 90 100 110 120 QQRAIIPCIK GYDVIAQAQS GTGKTATFAI SILQQLEIEF KETQALVLAP TRELAQQIQK 130 140 150 160 170 180 VILALGDYMG ATCHACIGGT NVRNEMQKLQ AEAPHIVVGT PGRVFDMLNR RYLSPKWIKM 190 200 210 220 230 240 FVLDEADEML SRGFKDQIYE IFQKLNTSIQ VVLLSATMPT DVLEVTKKFM RDPIRILVKK 250 260 270 280 290 300 EELTLEGIKQ FYINVEREEW KLDTLCDLYE TLTITQAVIF LNTRRKVDWL TEKMHARDFT 310 320 330 340 350 360 VSALHGDMDQ KERDVIMREF RSGSSRVLIT TDLLARGIDV QQVSLVINYD LPTNRENYIH 370 380 390 400 RIGRGGRFGR KGVAINFVTE EDKRILRDIE TFYNTTVEEM PMNVADLI

References

	« Hide 'large scale' referencesShow '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: 8521730] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lung.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Bone marrow, Brain, Lymph and Skeletal muscle.
[3]	"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: 11408474] [Abstract] Cited for: INTERACTION WITH EIF4E.
[4]	"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: 15715967] [Abstract] Cited for: POSSIBLE INTERACTION WITH NOM1.
[5]	"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: 16014927] [Abstract] Cited for: INTERACTION WITH HHV-1 VHS.
[6]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-181.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

D30655 mRNA. Translation: BAA06336.1.
BC012547 mRNA. Translation: AAH12547.1.
BC013708 mRNA. Translation: AAH13708.1.
BC015842 mRNA. Translation: AAH15842.1.
BC048105 mRNA. Translation: AAH48105.1.

RefSeq

NP_001958.2.

UniGene

Hs.599481
Hs.700566

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BOR	X-ray	1.85	A	22-240	[»]

SMR

Q14240. Positions 30-407.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14240.

PTM databases

PhosphoSite

Q14240.

Genome annotation databases

Ensembl

ENSG00000156976. Homo sapiens. [Contig view]

GeneID

1974.

KEGG

hsa:1974.

Organism-specific databases

H-InvDB

HIX0003899.
HIX0003933.

HGNC

HGNC:3284. EIF4A2.

HPA

CAB011690.

MIM

601102. gene.

PharmGKB

PA27712.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q14240.

HOVERGEN

Q14240.

Enzyme and pathway databases

Reactome

REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

CleanEx

HS_EIF4A2.

GermOnline

ENSG00000156976. Homo sapiens.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

LinkHub

Q14240.

NextBio

7991.

SOURCE

Search...

Entry information

Entry name

IF4A2_HUMAN

Accession

Primary (citable) accession number: Q14240
Secondary accession number(s): Q96B90, Q96EA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 15, 2004
Last modified:	November 25, 2008
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)