Full text data of EIF4A1
EIF4A1
(DDX2A, EIF4A)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Eukaryotic initiation factor 4A-I; eIF-4A-I; eIF4A-I; 3.6.4.13 (ATP-dependent RNA helicase eIF4A-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic initiation factor 4A-I; eIF-4A-I; eIF4A-I; 3.6.4.13 (ATP-dependent RNA helicase eIF4A-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00025491
IPI00025491 Eukaryotic initiation factor 4A-I or Eukaryotic initiation factor 4A-II EIF4A is both a subunit of a high molecular weight protein complex involved in cap recognition and is required as a single polypeptide chain for mRNA binding to ribosome soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00025491 Eukaryotic initiation factor 4A-I or Eukaryotic initiation factor 4A-II EIF4A is both a subunit of a high molecular weight protein complex involved in cap recognition and is required as a single polypeptide chain for mRNA binding to ribosome soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P60842
ID IF4A1_HUMAN Reviewed; 406 AA.
AC P60842; B2R6L8; D3DTP9; J3QLC4; P04765; Q5U018; Q61516;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Eukaryotic initiation factor 4A-I;
DE Short=eIF-4A-I;
DE Short=eIF4A-I;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-1;
GN Name=EIF4A1; Synonyms=DDX2A, EIF4A;
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).
RX PubMed=8493113; DOI=10.1093/nar/21.8.2012;
RA Kim N.-S., Kato T., Abe N., Kato S.;
RT "Nucleotide sequence of human cDNA encoding eukaryotic initiation
RT factor 4AI.";
RL Nucleic Acids Res. 21:2012-2012(1993).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, and Lung;
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 [7]
RP INTERACTION WITH PAIP1.
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue
RT PAIP enhances translation.";
RL Nature 392:520-523(1998).
RN [8]
RP INTERACTION WITH UPF2.
RX PubMed=11073994; DOI=10.1128/MCB.20.23.8944-8957.2000;
RA Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
RT "Novel Upf2p orthologues suggest a functional link between translation
RT initiation and nonsense surveillance complexes.";
RL Mol. Cell. Biol. 20:8944-8957(2000).
RN [9]
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 [10]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; VPS26A; VPS29; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [11]
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 [12]
RP INTERACTION WITH RBM4.
RX PubMed=17284590; DOI=10.1073/pnas.0611015104;
RA Lin J.C., Hsu M., Tarn W.Y.;
RT "Cell stress modulates the function of splicing regulatory protein
RT RBM4 in translation control.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118 AND LYS-174, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP INTERACTION WITH HHV-5 PROTEIN UL69.
RX PubMed=20133758; DOI=10.1073/pnas.0914856107;
RA Aoyagi M., Gaspar M., Shenk T.E.;
RT "Human cytomegalovirus UL69 protein facilitates translation by
RT associating with the mRNA cap-binding complex and excluding 4EBP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH PDCD4, FUNCTION,
RP SUBUNIT, AND ENZYME REGULATION.
RX PubMed=19153607; DOI=10.1038/emboj.2008.278;
RA Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D.,
RA Song H.;
RT "Structural basis for translational inhibition by the tumour
RT suppressor Pdcd4.";
RL EMBO J. 28:274-285(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-406 IN COMPLEX WITH PDCD4,
RP FUNCTION, ENZYME REGULATION, AND SUBUNIT.
RX PubMed=19204291; DOI=10.1073/pnas.0808275106;
RA Chang J.H., Cho Y.H., Sohn S.Y., Choi J.M., Kim A., Kim Y.C.,
RA Jang S.K., Cho Y.;
RT "Crystal structure of the eIF4A-PDCD4 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3148-3153(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236.
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).
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 -!- ENZYME REGULATION: Helicase activity and function in translation
CC are inhibited by interaction with PDCD4.
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/EIF4G3.
CC Interacts with PAIP1, EIF4E and UPF2. Found in a complex with
CC XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact
CC with NOM1. Interacts with PDCD4; this interferes with the
CC interaction between EIF4A and EIF4G. Interacts with RBM4.
CC Interacts with human cytomegalovirus/HHV-5 protein UL69.
CC -!- INTERACTION:
CC Q04637:EIF4G1; NbExp=7; IntAct=EBI-73449, EBI-73711;
CC P78344:EIF4G2; NbExp=3; IntAct=EBI-73449, EBI-296519;
CC Q15056:EIF4H; NbExp=2; IntAct=EBI-73449, EBI-748492;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60842-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60842-2; Sequence=VSP_046032;
CC Note=No experimental confirmation available;
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.
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DR EMBL; D13748; BAA02897.1; -; mRNA.
DR EMBL; BT019880; AAV38683.1; -; mRNA.
DR EMBL; BT019881; AAV38684.1; -; mRNA.
DR EMBL; AK312630; BAG35515.1; -; mRNA.
DR EMBL; AC016876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90167.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90168.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90169.1; -; Genomic_DNA.
DR EMBL; BC006210; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC009585; AAH09585.1; -; mRNA.
DR EMBL; BC073752; AAH73752.1; -; mRNA.
DR PIR; S33681; S33681.
DR RefSeq; NP_001191439.1; NM_001204510.1.
DR RefSeq; NP_001407.1; NM_001416.3.
DR UniGene; Hs.129673; -.
DR PDB; 2G9N; X-ray; 2.25 A; A/B=20-236.
DR PDB; 2ZU6; X-ray; 2.80 A; A/C/D/F=20-406.
DR PDB; 3EIQ; X-ray; 3.50 A; A/D=1-406.
DR PDBsum; 2G9N; -.
DR PDBsum; 2ZU6; -.
DR PDBsum; 3EIQ; -.
DR ProteinModelPortal; P60842; -.
DR SMR; P60842; 22-400.
DR DIP; DIP-29755N; -.
DR IntAct; P60842; 40.
DR MINT; MINT-5001111; -.
DR STRING; 9606.ENSP00000293831; -.
DR ChEMBL; CHEMBL2052028; -.
DR PhosphoSite; P60842; -.
DR DMDM; 46397463; -.
DR PaxDb; P60842; -.
DR PRIDE; P60842; -.
DR DNASU; 1973; -.
DR Ensembl; ENST00000293831; ENSP00000293831; ENSG00000161960.
DR Ensembl; ENST00000577269; ENSP00000463486; ENSG00000161960.
DR GeneID; 1973; -.
DR KEGG; hsa:1973; -.
DR UCSC; uc002ghr.1; human.
DR CTD; 1973; -.
DR GeneCards; GC17P007476; -.
DR HGNC; HGNC:3282; EIF4A1.
DR HPA; CAB011689; -.
DR MIM; 602641; gene.
DR neXtProt; NX_P60842; -.
DR PharmGKB; PA27710; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR KO; K03257; -.
DR OMA; NACNHLA; -.
DR PhylomeDB; P60842; -.
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; EIF4A1; human.
DR EvolutionaryTrace; P60842; -.
DR GeneWiki; EIF4A1; -.
DR GenomeRNAi; 1973; -.
DR NextBio; 35536557; -.
DR PRO; PR:P60842; -.
DR ArrayExpress; P60842; -.
DR Bgee; P60842; -.
DR CleanEx; HS_EIF4A1; -.
DR Genevestigator; P60842; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0004386; F:helicase activity; TAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; TAS:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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:0006413; P:translational initiation; TAS:Reactome.
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; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Helicase; Host-virus interaction; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 Eukaryotic initiation factor 4A-I.
FT /FTId=PRO_0000054933.
FT DOMAIN 63 234 Helicase ATP-binding.
FT DOMAIN 245 406 Helicase C-terminal.
FT NP_BIND 76 83 ATP (By similarity).
FT MOTIF 32 60 Q motif.
FT MOTIF 182 185 DEAD box.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 118 118 N6-acetyllysine.
FT MOD_RES 174 174 N6-acetyllysine.
FT VAR_SEQ 333 406 ARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAI
FT NMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI -> GKLY
FT PQNRSRWTVWP (in isoform 2).
FT /FTId=VSP_046032.
FT STRAND 23 25
FT HELIX 34 36
FT HELIX 41 50
FT HELIX 57 68
FT STRAND 72 75
FT HELIX 82 93
FT STRAND 103 106
FT HELIX 110 124
FT TURN 125 128
FT STRAND 131 134
FT TURN 143 145
FT STRAND 146 149
FT STRAND 153 157
FT HELIX 159 167
FT STRAND 178 183
FT HELIX 184 189
FT TURN 190 192
FT HELIX 193 202
FT STRAND 208 214
FT HELIX 218 227
FT STRAND 232 235
FT STRAND 241 243
FT STRAND 246 251
FT HELIX 256 269
FT STRAND 273 278
FT HELIX 282 290
FT TURN 291 296
FT STRAND 300 302
FT HELIX 312 316
FT HELIX 318 320
FT STRAND 321 323
FT STRAND 325 328
FT HELIX 330 333
FT HELIX 338 340
FT STRAND 342 348
FT HELIX 355 360
FT TURN 364 366
FT STRAND 370 375
FT HELIX 378 391
SQ SEQUENCE 406 AA; 46154 MW; 6EF89939F3045420 CRC64;
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ
RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV
MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV
LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE
LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI
GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI
//
ID IF4A1_HUMAN Reviewed; 406 AA.
AC P60842; B2R6L8; D3DTP9; J3QLC4; P04765; Q5U018; Q61516;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Eukaryotic initiation factor 4A-I;
DE Short=eIF-4A-I;
DE Short=eIF4A-I;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-1;
GN Name=EIF4A1; Synonyms=DDX2A, EIF4A;
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).
RX PubMed=8493113; DOI=10.1093/nar/21.8.2012;
RA Kim N.-S., Kato T., Abe N., Kato S.;
RT "Nucleotide sequence of human cDNA encoding eukaryotic initiation
RT factor 4AI.";
RL Nucleic Acids Res. 21:2012-2012(1993).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, and Lung;
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 [7]
RP INTERACTION WITH PAIP1.
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue
RT PAIP enhances translation.";
RL Nature 392:520-523(1998).
RN [8]
RP INTERACTION WITH UPF2.
RX PubMed=11073994; DOI=10.1128/MCB.20.23.8944-8957.2000;
RA Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
RT "Novel Upf2p orthologues suggest a functional link between translation
RT initiation and nonsense surveillance complexes.";
RL Mol. Cell. Biol. 20:8944-8957(2000).
RN [9]
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 [10]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; VPS26A; VPS29; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [11]
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 [12]
RP INTERACTION WITH RBM4.
RX PubMed=17284590; DOI=10.1073/pnas.0611015104;
RA Lin J.C., Hsu M., Tarn W.Y.;
RT "Cell stress modulates the function of splicing regulatory protein
RT RBM4 in translation control.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118 AND LYS-174, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP INTERACTION WITH HHV-5 PROTEIN UL69.
RX PubMed=20133758; DOI=10.1073/pnas.0914856107;
RA Aoyagi M., Gaspar M., Shenk T.E.;
RT "Human cytomegalovirus UL69 protein facilitates translation by
RT associating with the mRNA cap-binding complex and excluding 4EBP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH PDCD4, FUNCTION,
RP SUBUNIT, AND ENZYME REGULATION.
RX PubMed=19153607; DOI=10.1038/emboj.2008.278;
RA Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D.,
RA Song H.;
RT "Structural basis for translational inhibition by the tumour
RT suppressor Pdcd4.";
RL EMBO J. 28:274-285(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-406 IN COMPLEX WITH PDCD4,
RP FUNCTION, ENZYME REGULATION, AND SUBUNIT.
RX PubMed=19204291; DOI=10.1073/pnas.0808275106;
RA Chang J.H., Cho Y.H., Sohn S.Y., Choi J.M., Kim A., Kim Y.C.,
RA Jang S.K., Cho Y.;
RT "Crystal structure of the eIF4A-PDCD4 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3148-3153(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236.
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).
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 -!- ENZYME REGULATION: Helicase activity and function in translation
CC are inhibited by interaction with PDCD4.
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/EIF4G3.
CC Interacts with PAIP1, EIF4E and UPF2. Found in a complex with
CC XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact
CC with NOM1. Interacts with PDCD4; this interferes with the
CC interaction between EIF4A and EIF4G. Interacts with RBM4.
CC Interacts with human cytomegalovirus/HHV-5 protein UL69.
CC -!- INTERACTION:
CC Q04637:EIF4G1; NbExp=7; IntAct=EBI-73449, EBI-73711;
CC P78344:EIF4G2; NbExp=3; IntAct=EBI-73449, EBI-296519;
CC Q15056:EIF4H; NbExp=2; IntAct=EBI-73449, EBI-748492;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60842-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60842-2; Sequence=VSP_046032;
CC Note=No experimental confirmation available;
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.
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DR EMBL; D13748; BAA02897.1; -; mRNA.
DR EMBL; BT019880; AAV38683.1; -; mRNA.
DR EMBL; BT019881; AAV38684.1; -; mRNA.
DR EMBL; AK312630; BAG35515.1; -; mRNA.
DR EMBL; AC016876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90167.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90168.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90169.1; -; Genomic_DNA.
DR EMBL; BC006210; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC009585; AAH09585.1; -; mRNA.
DR EMBL; BC073752; AAH73752.1; -; mRNA.
DR PIR; S33681; S33681.
DR RefSeq; NP_001191439.1; NM_001204510.1.
DR RefSeq; NP_001407.1; NM_001416.3.
DR UniGene; Hs.129673; -.
DR PDB; 2G9N; X-ray; 2.25 A; A/B=20-236.
DR PDB; 2ZU6; X-ray; 2.80 A; A/C/D/F=20-406.
DR PDB; 3EIQ; X-ray; 3.50 A; A/D=1-406.
DR PDBsum; 2G9N; -.
DR PDBsum; 2ZU6; -.
DR PDBsum; 3EIQ; -.
DR ProteinModelPortal; P60842; -.
DR SMR; P60842; 22-400.
DR DIP; DIP-29755N; -.
DR IntAct; P60842; 40.
DR MINT; MINT-5001111; -.
DR STRING; 9606.ENSP00000293831; -.
DR ChEMBL; CHEMBL2052028; -.
DR PhosphoSite; P60842; -.
DR DMDM; 46397463; -.
DR PaxDb; P60842; -.
DR PRIDE; P60842; -.
DR DNASU; 1973; -.
DR Ensembl; ENST00000293831; ENSP00000293831; ENSG00000161960.
DR Ensembl; ENST00000577269; ENSP00000463486; ENSG00000161960.
DR GeneID; 1973; -.
DR KEGG; hsa:1973; -.
DR UCSC; uc002ghr.1; human.
DR CTD; 1973; -.
DR GeneCards; GC17P007476; -.
DR HGNC; HGNC:3282; EIF4A1.
DR HPA; CAB011689; -.
DR MIM; 602641; gene.
DR neXtProt; NX_P60842; -.
DR PharmGKB; PA27710; -.
DR eggNOG; COG0513; -.
DR HOGENOM; HOG000268797; -.
DR HOVERGEN; HBG107989; -.
DR KO; K03257; -.
DR OMA; NACNHLA; -.
DR PhylomeDB; P60842; -.
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; EIF4A1; human.
DR EvolutionaryTrace; P60842; -.
DR GeneWiki; EIF4A1; -.
DR GenomeRNAi; 1973; -.
DR NextBio; 35536557; -.
DR PRO; PR:P60842; -.
DR ArrayExpress; P60842; -.
DR Bgee; P60842; -.
DR CleanEx; HS_EIF4A1; -.
DR Genevestigator; P60842; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0004386; F:helicase activity; TAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; TAS:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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:0006413; P:translational initiation; TAS:Reactome.
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; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Helicase; Host-virus interaction; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 Eukaryotic initiation factor 4A-I.
FT /FTId=PRO_0000054933.
FT DOMAIN 63 234 Helicase ATP-binding.
FT DOMAIN 245 406 Helicase C-terminal.
FT NP_BIND 76 83 ATP (By similarity).
FT MOTIF 32 60 Q motif.
FT MOTIF 182 185 DEAD box.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 118 118 N6-acetyllysine.
FT MOD_RES 174 174 N6-acetyllysine.
FT VAR_SEQ 333 406 ARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAI
FT NMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI -> GKLY
FT PQNRSRWTVWP (in isoform 2).
FT /FTId=VSP_046032.
FT STRAND 23 25
FT HELIX 34 36
FT HELIX 41 50
FT HELIX 57 68
FT STRAND 72 75
FT HELIX 82 93
FT STRAND 103 106
FT HELIX 110 124
FT TURN 125 128
FT STRAND 131 134
FT TURN 143 145
FT STRAND 146 149
FT STRAND 153 157
FT HELIX 159 167
FT STRAND 178 183
FT HELIX 184 189
FT TURN 190 192
FT HELIX 193 202
FT STRAND 208 214
FT HELIX 218 227
FT STRAND 232 235
FT STRAND 241 243
FT STRAND 246 251
FT HELIX 256 269
FT STRAND 273 278
FT HELIX 282 290
FT TURN 291 296
FT STRAND 300 302
FT HELIX 312 316
FT HELIX 318 320
FT STRAND 321 323
FT STRAND 325 328
FT HELIX 330 333
FT HELIX 338 340
FT STRAND 342 348
FT HELIX 355 360
FT TURN 364 366
FT STRAND 370 375
FT HELIX 378 391
SQ SEQUENCE 406 AA; 46154 MW; 6EF89939F3045420 CRC64;
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ
RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV
MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV
LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE
LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI
GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI
//
MIM
602641
*RECORD*
*FIELD* NO
602641
*FIELD* TI
*602641 EUKARYOTIC TRANSLATION INITIATION FACTOR 4A, ISOFORM 1; EIF4A1
;;DDX2A
*FIELD* TX
read more
CLONING
The eukaryotic initiation factor-4A family consists of 2 closely related
genes, EIF4A1 and EIF4A2 (601102). These factors are required for the
binding of mRNA to 40S ribosomal subunits. Nielsen et al. (1985) cloned
eif4a1 cDNAs from mouse liver. They identified 2 distinct cDNAs
differing in their untranslated regions. The sizes of these cDNAs
correspond to 2 discrete mRNA bands of 2.0 and 1.6 kb seen on Northern
blots of both mouse and human cells. Nielsen and Trachsel (1988) found
that eif4a1 was expressed at similar levels in all mouse tissues
examined, while eif4a2 had a much more varied pattern of expression.
Kim et al. (1993) cloned the human EIF4A1 cDNA. The EIF4A1 cDNA encodes
a predicted 406-amino acid polypeptide with 92.7% amino acid similarity
to the mouse protein. Kukimoto et al. (1997) characterized the promoter
region of human EIF4A1. The minimal promoter contains TATA and CAAT
motifs and consensus sequences for binding to SP1 and AP2.
MAPPING
By fluorescence in situ hybridization, Jones et al. (1998) mapped the
linked EIF4A1 and CD68 (153634) genes to 17p13. By interspecific
backcross analysis, they mapped the mouse Eif4a1 and Cd68 genes to
chromosome 11.
GENE FUNCTION
Cruz-Migoni et al. (2011) found that BPSL1549, a Burkholderia
pseudomallei toxin, promotes deamidation of glu339 of the translation
initiation factor Eif4a, abolishing its helicase activity and inhibiting
translation.
*FIELD* RF
1. Cruz-Migoni, A.; Hautbergue, G. M.; Artymiuk, P. J.; Baker, P.
J.; Bokori-Brown, M.; Chang, C.-T.; Dickman, M. J.; Essex-Lopresti,
A.; Harding, S. V.; Mahadi, N. M.; Marshall, L. E.; Mobbs, G. W.;
and 16 others: A Burkholderia pseudomallei toxin inhibits helicase
activity of translation factor elF4A. Science 334: 821-824, 2011.
2. Jones, E.; Quinn, C. M.; See, C. G.; Montgomery, D. S.; Ford, M.
J.; Kolble, K.; Gordon, S.; Greaves, D. R.: The linked human elongation
initiation factor 4A1 (EIF4A1) and CD68 genes map to chromosome 17p13. Genomics 53:
248-250, 1998.
3. Kim, N.-S.; Kato, T.; Abe, N.; Kato, S.: Nucleotide sequence of
human cDNA encoding eukaryotic initiation factor 4A1. Nucleic Acids
Res. 21: 2012 only, 1993.
4. Kukimoto, I.; Watanabe, S.; Taniguchi, K.; Ogata, T.; Yoshiike,
K.; Kanda, T.: Characterization of the cloned promoter of the human
initiation factor 4A1 gene. Biochem. Biophys. Res. Commun. 233:
844-847, 1997.
5. Nielsen, P. J.; McMaster, G. K.; Trachsel, H.: Cloning of eukaryotic
protein synthesis initiation factor genes: isolation and characterization
of cDNA clones encoding factor eIF-4A. Nucleic Acids Res. 13: 6867-6880,
1985.
6. 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.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Carol A. Bocchini - updated: 12/4/1998
*FIELD* CD
Jennifer P. Macke: 5/20/1998
*FIELD* ED
alopez: 12/02/2011
alopez: 12/2/2011
terry: 11/29/2011
terry: 12/4/1998
dkim: 12/3/1998
terry: 8/19/1998
carol: 6/22/1998
dholmes: 6/16/1998
*RECORD*
*FIELD* NO
602641
*FIELD* TI
*602641 EUKARYOTIC TRANSLATION INITIATION FACTOR 4A, ISOFORM 1; EIF4A1
;;DDX2A
*FIELD* TX
read more
CLONING
The eukaryotic initiation factor-4A family consists of 2 closely related
genes, EIF4A1 and EIF4A2 (601102). These factors are required for the
binding of mRNA to 40S ribosomal subunits. Nielsen et al. (1985) cloned
eif4a1 cDNAs from mouse liver. They identified 2 distinct cDNAs
differing in their untranslated regions. The sizes of these cDNAs
correspond to 2 discrete mRNA bands of 2.0 and 1.6 kb seen on Northern
blots of both mouse and human cells. Nielsen and Trachsel (1988) found
that eif4a1 was expressed at similar levels in all mouse tissues
examined, while eif4a2 had a much more varied pattern of expression.
Kim et al. (1993) cloned the human EIF4A1 cDNA. The EIF4A1 cDNA encodes
a predicted 406-amino acid polypeptide with 92.7% amino acid similarity
to the mouse protein. Kukimoto et al. (1997) characterized the promoter
region of human EIF4A1. The minimal promoter contains TATA and CAAT
motifs and consensus sequences for binding to SP1 and AP2.
MAPPING
By fluorescence in situ hybridization, Jones et al. (1998) mapped the
linked EIF4A1 and CD68 (153634) genes to 17p13. By interspecific
backcross analysis, they mapped the mouse Eif4a1 and Cd68 genes to
chromosome 11.
GENE FUNCTION
Cruz-Migoni et al. (2011) found that BPSL1549, a Burkholderia
pseudomallei toxin, promotes deamidation of glu339 of the translation
initiation factor Eif4a, abolishing its helicase activity and inhibiting
translation.
*FIELD* RF
1. Cruz-Migoni, A.; Hautbergue, G. M.; Artymiuk, P. J.; Baker, P.
J.; Bokori-Brown, M.; Chang, C.-T.; Dickman, M. J.; Essex-Lopresti,
A.; Harding, S. V.; Mahadi, N. M.; Marshall, L. E.; Mobbs, G. W.;
and 16 others: A Burkholderia pseudomallei toxin inhibits helicase
activity of translation factor elF4A. Science 334: 821-824, 2011.
2. Jones, E.; Quinn, C. M.; See, C. G.; Montgomery, D. S.; Ford, M.
J.; Kolble, K.; Gordon, S.; Greaves, D. R.: The linked human elongation
initiation factor 4A1 (EIF4A1) and CD68 genes map to chromosome 17p13. Genomics 53:
248-250, 1998.
3. Kim, N.-S.; Kato, T.; Abe, N.; Kato, S.: Nucleotide sequence of
human cDNA encoding eukaryotic initiation factor 4A1. Nucleic Acids
Res. 21: 2012 only, 1993.
4. Kukimoto, I.; Watanabe, S.; Taniguchi, K.; Ogata, T.; Yoshiike,
K.; Kanda, T.: Characterization of the cloned promoter of the human
initiation factor 4A1 gene. Biochem. Biophys. Res. Commun. 233:
844-847, 1997.
5. Nielsen, P. J.; McMaster, G. K.; Trachsel, H.: Cloning of eukaryotic
protein synthesis initiation factor genes: isolation and characterization
of cDNA clones encoding factor eIF-4A. Nucleic Acids Res. 13: 6867-6880,
1985.
6. 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.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Carol A. Bocchini - updated: 12/4/1998
*FIELD* CD
Jennifer P. Macke: 5/20/1998
*FIELD* ED
alopez: 12/02/2011
alopez: 12/2/2011
terry: 11/29/2011
terry: 12/4/1998
dkim: 12/3/1998
terry: 8/19/1998
carol: 6/22/1998
dholmes: 6/16/1998