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P60842

- IF4A1_HUMAN

UniProt

P60842 - IF4A1_HUMAN

Protein

Eukaryotic initiation factor 4A-I

Gene

EIF4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
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    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.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Enzyme regulationi

    Helicase activity and function in translation are inhibited by interaction with PDCD4.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi76 – 838ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. double-stranded RNA binding Source: MGI
    4. helicase activity Source: UniProtKB
    5. mRNA binding Source: UniProtKB
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. RNA cap binding Source: UniProtKB
    9. translation factor activity, nucleic acid binding Source: UniProtKB
    10. translation initiation factor activity Source: UniProtKB-KW

    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. organ regeneration Source: Ensembl
    8. RNA metabolic process Source: Reactome
    9. translation Source: Reactome
    10. translational initiation Source: Reactome
    11. viral process Source: UniProtKB-KW

    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-I (EC:3.6.4.13)
    Short name:
    eIF-4A-I
    Short name:
    eIF4A-I
    Alternative name(s):
    ATP-dependent RNA helicase eIF4A-1
    Gene namesi
    Name:EIF4A1
    Synonyms:DDX2A, EIF4A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3282. EIF4A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation initiation factor 4F complex Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27710.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 406405Eukaryotic initiation factor 4A-IPRO_0000054933Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei174 – 1741N6-acetyllysine1 Publication
    Modified residuei193 – 1931N6-acetyllysineBy similarity
    Modified residuei238 – 2381N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP60842.
    PaxDbiP60842.
    PRIDEiP60842.

    PTM databases

    PhosphoSiteiP60842.

    Expressioni

    Gene expression databases

    ArrayExpressiP60842.
    BgeeiP60842.
    CleanExiHS_EIF4A1.
    GenevestigatoriP60842.

    Organism-specific databases

    HPAiCAB011689.

    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/EIF4G3. Interacts with PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with PDCD4; this interferes with the interaction between EIF4A and EIF4G. Interacts with RBM4. Interacts with human cytomegalovirus/HHV-5 protein UL69.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4G1Q046377EBI-73449,EBI-73711
    EIF4G2P783443EBI-73449,EBI-296519
    EIF4HQ150562EBI-73449,EBI-748492

    Protein-protein interaction databases

    BioGridi108289. 75 interactions.
    DIPiDIP-29755N.
    IntActiP60842. 41 interactions.
    MINTiMINT-5001111.
    STRINGi9606.ENSP00000293831.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 253
    Helixi34 – 363
    Helixi41 – 5010
    Helixi57 – 6812
    Beta strandi72 – 754
    Helixi82 – 9312
    Beta strandi103 – 1064
    Helixi110 – 12415
    Turni125 – 1284
    Beta strandi131 – 1344
    Turni143 – 1453
    Beta strandi146 – 1494
    Beta strandi153 – 1575
    Helixi159 – 1679
    Beta strandi178 – 1836
    Helixi184 – 1896
    Turni190 – 1923
    Helixi193 – 20210
    Beta strandi208 – 2147
    Helixi218 – 22710
    Beta strandi232 – 2354
    Beta strandi241 – 2433
    Beta strandi246 – 2516
    Helixi256 – 26914
    Beta strandi273 – 2786
    Helixi282 – 2909
    Turni291 – 2966
    Beta strandi300 – 3023
    Helixi312 – 3165
    Helixi318 – 3203
    Beta strandi321 – 3233
    Beta strandi325 – 3284
    Helixi330 – 3334
    Helixi338 – 3403
    Beta strandi342 – 3487
    Helixi355 – 3606
    Turni364 – 3663
    Beta strandi370 – 3756
    Helixi378 – 39114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G9NX-ray2.25A/B20-238[»]
    2ZU6X-ray2.80A/C/D/F20-406[»]
    3EIQX-ray3.50A/D1-406[»]
    ProteinModelPortaliP60842.
    SMRiP60842. Positions 22-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60842.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 234172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini245 – 406162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 6029Q motifAdd
    BLAST
    Motifi182 – 1854DEAD box

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268797.
    HOVERGENiHBG107989.
    KOiK03257.
    OMAiWIADESG.
    PhylomeDBiP60842.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P60842-1) [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

    MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY    50
    GFEKPSAIQQ RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA 100
    TQALVLAPTR ELAQQIQKVV MALGDYMGAS CHACIGGTNV RAEVQKLQME 150
    APHIIVGTPG RVFDMLNRRY LSPKYIKMFV LDEADEMLSR GFKDQIYDIF 200
    QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE LTLEGIRQFY 250
    INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS 300
    AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP 350
    TNRENYIHRI GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL 400
    NVADLI 406
    Length:406
    Mass (Da):46,154
    Last modified:April 13, 2004 - v1
    Checksum:i6EF89939F3045420
    GO
    Isoform 2 (identifier: P60842-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         333-406: ARGIDVQQVS...EMPLNVADLI → GKLYPQNRSRWTVWP

    Note: No experimental confirmation available.

    Show »
    Length:347
    Mass (Da):39,548
    Checksum:i4ACB22D62DCA8BD0
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei333 – 40674ARGID…VADLI → GKLYPQNRSRWTVWP in isoform 2. 1 PublicationVSP_046032Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13748 mRNA. Translation: BAA02897.1.
    BT019880 mRNA. Translation: AAV38683.1.
    BT019881 mRNA. Translation: AAV38684.1.
    AK312630 mRNA. Translation: BAG35515.1.
    AC016876 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90167.1.
    CH471108 Genomic DNA. Translation: EAW90168.1.
    CH471108 Genomic DNA. Translation: EAW90169.1.
    BC006210 mRNA. No translation available.
    BC009585 mRNA. Translation: AAH09585.1.
    BC073752 mRNA. Translation: AAH73752.1.
    CCDSiCCDS11113.1. [P60842-1]
    CCDS58511.1. [P60842-2]
    PIRiS33681.
    RefSeqiNP_001191439.1. NM_001204510.1. [P60842-2]
    NP_001407.1. NM_001416.3. [P60842-1]
    UniGeneiHs.129673.

    Genome annotation databases

    EnsembliENST00000293831; ENSP00000293831; ENSG00000161960. [P60842-1]
    ENST00000577269; ENSP00000463486; ENSG00000161960. [P60842-2]
    GeneIDi1973.
    KEGGihsa:1973.
    UCSCiuc002gho.2. human. [P60842-1]
    uc002ghr.1. human.

    Polymorphism databases

    DMDMi46397463.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13748 mRNA. Translation: BAA02897.1 .
    BT019880 mRNA. Translation: AAV38683.1 .
    BT019881 mRNA. Translation: AAV38684.1 .
    AK312630 mRNA. Translation: BAG35515.1 .
    AC016876 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90167.1 .
    CH471108 Genomic DNA. Translation: EAW90168.1 .
    CH471108 Genomic DNA. Translation: EAW90169.1 .
    BC006210 mRNA. No translation available.
    BC009585 mRNA. Translation: AAH09585.1 .
    BC073752 mRNA. Translation: AAH73752.1 .
    CCDSi CCDS11113.1. [P60842-1 ]
    CCDS58511.1. [P60842-2 ]
    PIRi S33681.
    RefSeqi NP_001191439.1. NM_001204510.1. [P60842-2 ]
    NP_001407.1. NM_001416.3. [P60842-1 ]
    UniGenei Hs.129673.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G9N X-ray 2.25 A/B 20-238 [» ]
    2ZU6 X-ray 2.80 A/C/D/F 20-406 [» ]
    3EIQ X-ray 3.50 A/D 1-406 [» ]
    ProteinModelPortali P60842.
    SMRi P60842. Positions 22-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108289. 75 interactions.
    DIPi DIP-29755N.
    IntActi P60842. 41 interactions.
    MINTi MINT-5001111.
    STRINGi 9606.ENSP00000293831.

    Chemistry

    ChEMBLi CHEMBL2052028.

    PTM databases

    PhosphoSitei P60842.

    Polymorphism databases

    DMDMi 46397463.

    Proteomic databases

    MaxQBi P60842.
    PaxDbi P60842.
    PRIDEi P60842.

    Protocols and materials databases

    DNASUi 1973.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293831 ; ENSP00000293831 ; ENSG00000161960 . [P60842-1 ]
    ENST00000577269 ; ENSP00000463486 ; ENSG00000161960 . [P60842-2 ]
    GeneIDi 1973.
    KEGGi hsa:1973.
    UCSCi uc002gho.2. human. [P60842-1 ]
    uc002ghr.1. human.

    Organism-specific databases

    CTDi 1973.
    GeneCardsi GC17P007476.
    HGNCi HGNC:3282. EIF4A1.
    HPAi CAB011689.
    MIMi 602641. gene.
    neXtProti NX_P60842.
    PharmGKBi PA27710.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268797.
    HOVERGENi HBG107989.
    KOi K03257.
    OMAi WIADESG.
    PhylomeDBi P60842.
    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 EIF4A1. human.
    EvolutionaryTracei P60842.
    GeneWikii EIF4A1.
    GenomeRNAii 1973.
    NextBioi 35536557.
    PROi P60842.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60842.
    Bgeei P60842.
    CleanExi HS_EIF4A1.
    Genevestigatori P60842.

    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

    1. "Nucleotide sequence of human cDNA encoding eukaryotic initiation factor 4AI."
      Kim N.-S., Kato T., Abe N., Kato S.
      Nucleic Acids Res. 21:2012-2012(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 and Lung.
    7. "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
      Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
      Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAIP1.
    8. "Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes."
      Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.
      Mol. Cell. Biol. 20:8944-8957(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UPF2.
    9. "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.
    10. "Exportin 7 defines a novel general nuclear export pathway."
      Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
      EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; VPS26A; VPS29; VPS35 AND SFN.
    11. "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.
    12. "Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
      Lin J.C., Hsu M., Tarn W.Y.
      Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM4.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118 AND LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1."
      Aoyagi M., Gaspar M., Shenk T.E.
      Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "Structural basis for translational inhibition by the tumour suppressor Pdcd4."
      Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D., Song H.
      EMBO J. 28:274-285(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH PDCD4, FUNCTION, SUBUNIT, ENZYME REGULATION.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-406 IN COMPLEX WITH PDCD4, FUNCTION, ENZYME REGULATION, SUBUNIT.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236.

    Entry informationi

    Entry nameiIF4A1_HUMAN
    AccessioniPrimary (citable) accession number: P60842
    Secondary accession number(s): B2R6L8
    , D3DTP9, J3QLC4, P04765, Q5U018, Q61516
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3