Full text data of EIF4A2
EIF4A2
(DDX2B, EIF4F)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic initiation factor 4A-II; eIF-4A-II; eIF4A-II; 3.6.4.13 (ATP-dependent RNA helicase eIF4A-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic initiation factor 4A-II; eIF-4A-II; eIF4A-II; 3.6.4.13 (ATP-dependent RNA helicase eIF4A-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14240
ID IF4A2_HUMAN Reviewed; 407 AA.
AC Q14240; D3DNU9; Q53XJ6; Q96B90; Q96EA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Eukaryotic initiation factor 4A-II;
DE Short=eIF-4A-II;
DE Short=eIF4A-II;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-2;
GN Name=EIF4A2; Synonyms=DDX2B, EIF4F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=8521730;
RA Sudo K., Takahashi E., Nakamura Y.;
RT "Isolation and mapping of the human EIF4A2 gene homologous to the
RT murine protein synthesis initiation factor 4A-II gene Eif4a2.";
RL Cytogenet. Cell Genet. 71:385-388(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, Lymph, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH EIF4E.
RX PubMed=11408474; DOI=10.1074/jbc.C100284200;
RA Li W., Belsham G.J., Proud C.G.;
RT "Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually
RT interact in a 1:1 ratio in vivo.";
RL J. Biol. Chem. 276:29111-29115(2001).
RN [7]
RP POSSIBLE INTERACTION WITH NOM1.
RX PubMed=15715967; DOI=10.1016/j.gene.2004.12.027;
RA Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.;
RT "Identification of NOM1, a nucleolar, eIF4A binding protein encoded
RT within the chromosome 7q36 breakpoint region targeted in cases of
RT pediatric acute myeloid leukemia.";
RL Gene 347:137-145(2005).
RN [8]
RP INTERACTION WITH HHV-1 VHS.
RX PubMed=16014927; DOI=10.1128/JVI.79.15.9651-9664.2005;
RA Feng P., Everly D.N. Jr., Read G.S.;
RT "mRNA decay during herpes simplex virus (HSV) infections: protein-
RT protein interactions involving the HSV virion host shutoff protein and
RT translation factors eIF4H and eIF4A.";
RL J. Virol. 79:9651-9664(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L.,
RA Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W.,
RA Hammarstrom M., Moche M., Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-181.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the
CC eIF4F complex involved in cap recognition and is required for mRNA
CC binding to ribosome. In the current model of translation
CC initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR
CC of mRNAs which is necessary to allow efficient binding of the
CC small ribosomal subunit, and subsequent scanning for the initiator
CC codon.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
CC which varies with external and internal environmental conditions.
CC It is composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3 (By
CC similarity). Interacts with EIF4E. May interact with NOM1.
CC Interacts with HHV-1 Vhs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14240-2; Sequence=VSP_009629;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF4A2ID262.html";
CC -----------------------------------------------------------------------
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DR EMBL; D30655; BAA06336.1; -; mRNA.
DR EMBL; BT009860; AAP88862.1; -; mRNA.
DR EMBL; AC112907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78172.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78177.1; -; Genomic_DNA.
DR EMBL; BC012547; AAH12547.1; -; mRNA.
DR EMBL; BC013708; AAH13708.1; -; mRNA.
DR EMBL; BC015842; AAH15842.1; -; mRNA.
DR EMBL; BC048105; AAH48105.1; -; mRNA.
DR RefSeq; NP_001958.2; NM_001967.3.
DR RefSeq; XP_005247238.1; XM_005247181.1.
DR UniGene; Hs.518475; -.
DR UniGene; Hs.599481; -.
DR PDB; 3BOR; X-ray; 1.85 A; A=22-240.
DR PDBsum; 3BOR; -.
DR ProteinModelPortal; Q14240; -.
DR SMR; Q14240; 23-401.
DR IntAct; Q14240; 17.
DR MINT; MINT-202114; -.
DR STRING; 9606.ENSP00000326381; -.
DR PhosphoSite; Q14240; -.
DR DMDM; 45645183; -.
DR PaxDb; Q14240; -.
DR PRIDE; Q14240; -.
DR DNASU; 1974; -.
DR Ensembl; ENST00000323963; ENSP00000326381; ENSG00000156976.
DR Ensembl; ENST00000440191; ENSP00000398370; ENSG00000156976.
DR GeneID; 1974; -.
DR KEGG; hsa:1974; -.
DR UCSC; uc003fqs.3; human.
DR CTD; 1974; -.
DR GeneCards; GC03P186556; -.
DR H-InvDB; HIX0003899; -.
DR HGNC; HGNC:3284; EIF4A2.
DR HPA; CAB011690; -.
DR MIM; 601102; gene.
DR neXtProt; NX_Q14240; -.
DR PharmGKB; PA27712; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR InParanoid; Q14240; -.
DR KO; K03257; -.
DR OMA; NEITDNF; -.
DR PhylomeDB; Q14240; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF4A2; human.
DR EvolutionaryTrace; Q14240; -.
DR GeneWiki; EIF4A2; -.
DR GenomeRNAi; 1974; -.
DR NextBio; 7991; -.
DR PMAP-CutDB; Q14240; -.
DR PRO; PR:Q14240; -.
DR ArrayExpress; Q14240; -.
DR Bgee; Q14240; -.
DR CleanEx; HS_EIF4A2; -.
DR Genevestigator; Q14240; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Helicase; Host-virus interaction; Hydrolase; Initiation factor;
KW Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1 407 Eukaryotic initiation factor 4A-II.
FT /FTId=PRO_0000054938.
FT DOMAIN 64 235 Helicase ATP-binding.
FT DOMAIN 246 407 Helicase C-terminal.
FT NP_BIND 77 84 ATP (By similarity).
FT MOTIF 33 61 Q motif.
FT MOTIF 183 186 DEAD box.
FT VAR_SEQ 9 9 N -> NS (in isoform 2).
FT /FTId=VSP_009629.
FT VARIANT 93 93 Q -> H (in dbSNP:rs11538616).
FT /FTId=VAR_052158.
FT VARIANT 181 181 V -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035838.
FT CONFLICT 27 27 N -> S (in Ref. 5; AAH15842).
FT CONFLICT 212 213 LL -> FA (in Ref. 1; BAA06336).
FT HELIX 35 37
FT HELIX 42 51
FT HELIX 58 68
FT STRAND 73 75
FT HELIX 81 94
FT STRAND 104 107
FT HELIX 111 124
FT TURN 125 129
FT STRAND 132 135
FT STRAND 154 158
FT HELIX 160 168
FT STRAND 179 184
FT HELIX 185 190
FT HELIX 194 203
FT STRAND 209 213
FT HELIX 219 228
FT STRAND 233 235
SQ SEQUENCE 407 AA; 46402 MW; FAA7D3BA9D8C6DA0 CRC64;
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ
QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV
ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF
VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE
ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR
IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI
//
ID IF4A2_HUMAN Reviewed; 407 AA.
AC Q14240; D3DNU9; Q53XJ6; Q96B90; Q96EA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Eukaryotic initiation factor 4A-II;
DE Short=eIF-4A-II;
DE Short=eIF4A-II;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-2;
GN Name=EIF4A2; Synonyms=DDX2B, EIF4F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=8521730;
RA Sudo K., Takahashi E., Nakamura Y.;
RT "Isolation and mapping of the human EIF4A2 gene homologous to the
RT murine protein synthesis initiation factor 4A-II gene Eif4a2.";
RL Cytogenet. Cell Genet. 71:385-388(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, Lymph, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH EIF4E.
RX PubMed=11408474; DOI=10.1074/jbc.C100284200;
RA Li W., Belsham G.J., Proud C.G.;
RT "Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually
RT interact in a 1:1 ratio in vivo.";
RL J. Biol. Chem. 276:29111-29115(2001).
RN [7]
RP POSSIBLE INTERACTION WITH NOM1.
RX PubMed=15715967; DOI=10.1016/j.gene.2004.12.027;
RA Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.;
RT "Identification of NOM1, a nucleolar, eIF4A binding protein encoded
RT within the chromosome 7q36 breakpoint region targeted in cases of
RT pediatric acute myeloid leukemia.";
RL Gene 347:137-145(2005).
RN [8]
RP INTERACTION WITH HHV-1 VHS.
RX PubMed=16014927; DOI=10.1128/JVI.79.15.9651-9664.2005;
RA Feng P., Everly D.N. Jr., Read G.S.;
RT "mRNA decay during herpes simplex virus (HSV) infections: protein-
RT protein interactions involving the HSV virion host shutoff protein and
RT translation factors eIF4H and eIF4A.";
RL J. Virol. 79:9651-9664(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L.,
RA Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W.,
RA Hammarstrom M., Moche M., Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-181.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the
CC eIF4F complex involved in cap recognition and is required for mRNA
CC binding to ribosome. In the current model of translation
CC initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR
CC of mRNAs which is necessary to allow efficient binding of the
CC small ribosomal subunit, and subsequent scanning for the initiator
CC codon.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
CC which varies with external and internal environmental conditions.
CC It is composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3 (By
CC similarity). Interacts with EIF4E. May interact with NOM1.
CC Interacts with HHV-1 Vhs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14240-2; Sequence=VSP_009629;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF4A2ID262.html";
CC -----------------------------------------------------------------------
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DR EMBL; D30655; BAA06336.1; -; mRNA.
DR EMBL; BT009860; AAP88862.1; -; mRNA.
DR EMBL; AC112907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78172.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78177.1; -; Genomic_DNA.
DR EMBL; BC012547; AAH12547.1; -; mRNA.
DR EMBL; BC013708; AAH13708.1; -; mRNA.
DR EMBL; BC015842; AAH15842.1; -; mRNA.
DR EMBL; BC048105; AAH48105.1; -; mRNA.
DR RefSeq; NP_001958.2; NM_001967.3.
DR RefSeq; XP_005247238.1; XM_005247181.1.
DR UniGene; Hs.518475; -.
DR UniGene; Hs.599481; -.
DR PDB; 3BOR; X-ray; 1.85 A; A=22-240.
DR PDBsum; 3BOR; -.
DR ProteinModelPortal; Q14240; -.
DR SMR; Q14240; 23-401.
DR IntAct; Q14240; 17.
DR MINT; MINT-202114; -.
DR STRING; 9606.ENSP00000326381; -.
DR PhosphoSite; Q14240; -.
DR DMDM; 45645183; -.
DR PaxDb; Q14240; -.
DR PRIDE; Q14240; -.
DR DNASU; 1974; -.
DR Ensembl; ENST00000323963; ENSP00000326381; ENSG00000156976.
DR Ensembl; ENST00000440191; ENSP00000398370; ENSG00000156976.
DR GeneID; 1974; -.
DR KEGG; hsa:1974; -.
DR UCSC; uc003fqs.3; human.
DR CTD; 1974; -.
DR GeneCards; GC03P186556; -.
DR H-InvDB; HIX0003899; -.
DR HGNC; HGNC:3284; EIF4A2.
DR HPA; CAB011690; -.
DR MIM; 601102; gene.
DR neXtProt; NX_Q14240; -.
DR PharmGKB; PA27712; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR InParanoid; Q14240; -.
DR KO; K03257; -.
DR OMA; NEITDNF; -.
DR PhylomeDB; Q14240; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF4A2; human.
DR EvolutionaryTrace; Q14240; -.
DR GeneWiki; EIF4A2; -.
DR GenomeRNAi; 1974; -.
DR NextBio; 7991; -.
DR PMAP-CutDB; Q14240; -.
DR PRO; PR:Q14240; -.
DR ArrayExpress; Q14240; -.
DR Bgee; Q14240; -.
DR CleanEx; HS_EIF4A2; -.
DR Genevestigator; Q14240; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Helicase; Host-virus interaction; Hydrolase; Initiation factor;
KW Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1 407 Eukaryotic initiation factor 4A-II.
FT /FTId=PRO_0000054938.
FT DOMAIN 64 235 Helicase ATP-binding.
FT DOMAIN 246 407 Helicase C-terminal.
FT NP_BIND 77 84 ATP (By similarity).
FT MOTIF 33 61 Q motif.
FT MOTIF 183 186 DEAD box.
FT VAR_SEQ 9 9 N -> NS (in isoform 2).
FT /FTId=VSP_009629.
FT VARIANT 93 93 Q -> H (in dbSNP:rs11538616).
FT /FTId=VAR_052158.
FT VARIANT 181 181 V -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035838.
FT CONFLICT 27 27 N -> S (in Ref. 5; AAH15842).
FT CONFLICT 212 213 LL -> FA (in Ref. 1; BAA06336).
FT HELIX 35 37
FT HELIX 42 51
FT HELIX 58 68
FT STRAND 73 75
FT HELIX 81 94
FT STRAND 104 107
FT HELIX 111 124
FT TURN 125 129
FT STRAND 132 135
FT STRAND 154 158
FT HELIX 160 168
FT STRAND 179 184
FT HELIX 185 190
FT HELIX 194 203
FT STRAND 209 213
FT HELIX 219 228
FT STRAND 233 235
SQ SEQUENCE 407 AA; 46402 MW; FAA7D3BA9D8C6DA0 CRC64;
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ
QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV
ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF
VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE
ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR
IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI
//
MIM
601102
*RECORD*
*FIELD* NO
601102
*FIELD* TI
*601102 EUKARYOTIC TRANSLATION INITIATION FACTOR 4A, ISOFORM 2; EIF4A2
;;DDX2B
*FIELD* TX
read moreEukaryotic initiation factor 4A plays an important role in the binding
of mRNA to the 43S preinitiation complex when protein synthesis begins.
Two highly homologous forms of functional EIF4A genes, Eif4a1 (602641)
and Eif4a2, have been isolated in mice (Nielsen and Trachsel, 1988);
yeast cells also possess 2 EIF4A genes, TIF1 and TIF2 (601993). The
murine Eif4a and yeast TIF genes appear to belong to a DEAD-box gene
family, whose members exhibit extensive amino acid similarity and
contain the asp-glu-ala-asp (DEAD) sequence. DEAD-box genes have been
identified in species ranging from E-coli to humans. Their function
appears to be related to transcriptional/translational regulation.
CLONING
Sudo et al. (1995) isolated human cDNA highly homologous to murine
Eif4a2, which encodes one of the protein-synthesis initiation factors
involved in the binding of mRNA to the ribosome. The human homolog was
expressed in all normal tissues examined, but in variable amounts, being
highly expressed in skeletal muscle and ovary, and less abundantly in
liver, kidney, and pancreas.
GENE FUNCTION
Meijer et al. (2013) demonstrated that translational inhibition is the
primary event required for mRNA degradation. Translational inhibition
depends on miRNAs impairing the function of the eIF4F initiation
complex. Meijer et al. (2013) defined the RNA helicase eIF4A2 as the key
factor of eIF4F through which microRNAs function. They uncovered a
correlation between the presence of miRNA target sites in the 3-prime
untranslated region (UTR) of mRNAs and secondary structure in the
5-prime UTR, and showed that mRNAs with unstructured 5-prime UTRs are
refractory to miRNA repression. Meijer et al. (2013) concluded that
their data supported a linear model for miRNA-mediated gene regulation
in which translational repression via eIF4A2 is required first, followed
by mRNA destabilization.
MAPPING
Nielsen et al. (1993) mapped the mouse Eif4a2 gene to chromosome 16. By
fluorescence in situ hybridization, Sudo et al. (1995) mapped the EIF4A2
gene to 18p11.2. The International Radiation Hybrid Mapping Consortium
mapped the EIF4A2 gene to chromosome 3 (TMAP WI-30529) in a region of
conserved synteny with mouse chromosome 16.
*FIELD* RF
1. Meijer, H. A.; Kong, Y. W.; Lu, W. T.; Wilczynska, A.; Spriggs,
R. V.; Robinson, S. W.; Godfrey, J. D.; Willis, A. E.; Bushell, M.
: Translational repression and eIF4A2 activity are critical for microRNA-mediated
gene regulation. Science 340: 82-85, 2013.
2. Nielsen, P. J.; Rochelle, J. M.; Seldin, M. F.: The functional
genes for protein synthesis initiation factor 4AI and 4AII map to
mouse chromosomes 11 and 16. Mammalian Genome 4: 185-186, 1993.
3. Nielsen, P. J.; Trachsel, H.: The mouse protein synthesis initiation
factor 4A gene family includes two related functional genes which
are differentially expressed. EMBO J. 7: 2097-2105, 1988.
4. Sudo, K.; Takahashi, E.; Nakamura, Y.: Isolation and mapping of
the human EIF4A2 gene homologous to the murine protein synthesis initiation
factor 4A-II gene Eif4a2. Cytogenet. Cell Genet. 71: 385-388, 1995.
*FIELD* CN
Ada Hamosh - updated: 05/03/2013
Joanna S. Amberger - updated: 1/25/2002
*FIELD* CD
Victor A. McKusick: 3/4/1996
*FIELD* ED
alopez: 05/03/2013
joanna: 1/25/2002
carol: 6/22/1998
mark: 9/22/1997
mark: 3/4/1996
*RECORD*
*FIELD* NO
601102
*FIELD* TI
*601102 EUKARYOTIC TRANSLATION INITIATION FACTOR 4A, ISOFORM 2; EIF4A2
;;DDX2B
*FIELD* TX
read moreEukaryotic initiation factor 4A plays an important role in the binding
of mRNA to the 43S preinitiation complex when protein synthesis begins.
Two highly homologous forms of functional EIF4A genes, Eif4a1 (602641)
and Eif4a2, have been isolated in mice (Nielsen and Trachsel, 1988);
yeast cells also possess 2 EIF4A genes, TIF1 and TIF2 (601993). The
murine Eif4a and yeast TIF genes appear to belong to a DEAD-box gene
family, whose members exhibit extensive amino acid similarity and
contain the asp-glu-ala-asp (DEAD) sequence. DEAD-box genes have been
identified in species ranging from E-coli to humans. Their function
appears to be related to transcriptional/translational regulation.
CLONING
Sudo et al. (1995) isolated human cDNA highly homologous to murine
Eif4a2, which encodes one of the protein-synthesis initiation factors
involved in the binding of mRNA to the ribosome. The human homolog was
expressed in all normal tissues examined, but in variable amounts, being
highly expressed in skeletal muscle and ovary, and less abundantly in
liver, kidney, and pancreas.
GENE FUNCTION
Meijer et al. (2013) demonstrated that translational inhibition is the
primary event required for mRNA degradation. Translational inhibition
depends on miRNAs impairing the function of the eIF4F initiation
complex. Meijer et al. (2013) defined the RNA helicase eIF4A2 as the key
factor of eIF4F through which microRNAs function. They uncovered a
correlation between the presence of miRNA target sites in the 3-prime
untranslated region (UTR) of mRNAs and secondary structure in the
5-prime UTR, and showed that mRNAs with unstructured 5-prime UTRs are
refractory to miRNA repression. Meijer et al. (2013) concluded that
their data supported a linear model for miRNA-mediated gene regulation
in which translational repression via eIF4A2 is required first, followed
by mRNA destabilization.
MAPPING
Nielsen et al. (1993) mapped the mouse Eif4a2 gene to chromosome 16. By
fluorescence in situ hybridization, Sudo et al. (1995) mapped the EIF4A2
gene to 18p11.2. The International Radiation Hybrid Mapping Consortium
mapped the EIF4A2 gene to chromosome 3 (TMAP WI-30529) in a region of
conserved synteny with mouse chromosome 16.
*FIELD* RF
1. Meijer, H. A.; Kong, Y. W.; Lu, W. T.; Wilczynska, A.; Spriggs,
R. V.; Robinson, S. W.; Godfrey, J. D.; Willis, A. E.; Bushell, M.
: Translational repression and eIF4A2 activity are critical for microRNA-mediated
gene regulation. Science 340: 82-85, 2013.
2. Nielsen, P. J.; Rochelle, J. M.; Seldin, M. F.: The functional
genes for protein synthesis initiation factor 4AI and 4AII map to
mouse chromosomes 11 and 16. Mammalian Genome 4: 185-186, 1993.
3. Nielsen, P. J.; Trachsel, H.: The mouse protein synthesis initiation
factor 4A gene family includes two related functional genes which
are differentially expressed. EMBO J. 7: 2097-2105, 1988.
4. Sudo, K.; Takahashi, E.; Nakamura, Y.: Isolation and mapping of
the human EIF4A2 gene homologous to the murine protein synthesis initiation
factor 4A-II gene Eif4a2. Cytogenet. Cell Genet. 71: 385-388, 1995.
*FIELD* CN
Ada Hamosh - updated: 05/03/2013
Joanna S. Amberger - updated: 1/25/2002
*FIELD* CD
Victor A. McKusick: 3/4/1996
*FIELD* ED
alopez: 05/03/2013
joanna: 1/25/2002
carol: 6/22/1998
mark: 9/22/1997
mark: 3/4/1996