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P38919 (IF4A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic initiation factor 4A-III

Short name=eIF-4A-III
Short name=eIF4A-III
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase DDX48
ATP-dependent RNA helicase eIF4A-3
DEAD box protein 48
Eukaryotic initiation factor 4A-like NUK-34
Eukaryotic translation initiation factor 4A isoform 3
Nuclear matrix protein 265
Short name=NMP 265
Short name=hNMP 265
Gene names
Name:EIF4A3
Synonyms:DDX48, KIAA0111
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Ref.12 Ref.15 Ref.16 Ref.20 Ref.25 Ref.32

Catalytic activity

ATP + H2O = ADP + phosphate.

Enzyme regulation

The ATPase activity is increased some 4-fold in the presence of RNA. Ref.34

Subunit structure

Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. Identified in the spliceosome C complex. May interact with NOM1. Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-independent manner. Direct interaction with CWC22 is mediated by the helicase C-terminal domain. Full interaction with CWC22 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.31 Ref.34 Ref.36

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites By similarity. Ref.10 Ref.13 Ref.34

Tissue specificity

Ubiquitously expressed. Ref.10

Sequence similarities

Belongs to the DEAD box helicase family. eIF4A subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAA04879.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Nonsense-mediated mRNA decay
rRNA processing
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.11. Source: UniProtKB

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from direct assay PubMed 10523622. Source: HGNC

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype Ref.15. Source: UniProtKB

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

positive regulation of translation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.11Ref.34. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exon-exon junction complex

Inferred from direct assay PubMed 16601204. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay PubMed 10523622. Source: HGNC

ATP-dependent RNA helicase activity

Inferred from direct assay PubMed 10523622. Source: HGNC

poly(A) binding

Inferred from direct assay PubMed 10523622. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Eukaryotic initiation factor 4A-III
PRO_0000423267
Initiator methionine11Removed; alternate Ref.8
Chain2 – 411410Eukaryotic initiation factor 4A-III, N-terminally processed
PRO_0000054942

Regions

Domain69 – 239171Helicase ATP-binding
Domain250 – 411162Helicase C-terminal
Nucleotide binding85 – 906ATP
Nucleotide binding367 – 3715ATP
Motif38 – 6629Q motif
Motif187 – 1904DEAD box

Sites

Binding site601ATP; via carbonyl oxygen
Binding site651ATP
Binding site3421ATP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.28 Ref.30
Modified residue21N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processed Ref.8 Ref.24 Ref.26 Ref.28 Ref.30 Ref.35
Modified residue121Phosphoserine Ref.28 Ref.30
Modified residue1631Phosphothreonine Ref.23 Ref.28
Modified residue2961N6-acetyllysine Ref.27
Modified residue3211N6-acetyllysine Ref.27

Experimental info

Mutagenesis881K → A: ATPase activity is not induced in presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly. Ref.16
Mutagenesis2701D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273. Ref.31
Mutagenesis2731D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270. Ref.31
Mutagenesis276 – 2772TI → GD: Loss of CWC22-binding and loss of incorporation into EJCs.
Mutagenesis301 – 3033NFT → LAG: Loss of CWC22-binding and loss of incorporation into EJCs. Ref.31
Mutagenesis3341T → V: Reduced incorporation into EJCs. Ref.36
Mutagenesis4011D → K: Loss of incorporation into EJCs; when associated with R-402. Ref.34
Mutagenesis4021E → R: Loss of incorporation into EJCs; when associated with K-401. Ref.34
Sequence conflict2101P → S in CAA56074. Ref.1
Sequence conflict3701R → Q in CAA56074. Ref.1

Secondary structure

................................................................................... 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38919 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3A21888CA96CA5EA

FASTA41146,871
        10         20         30         40         50         60 
MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK 

        70         80         90        100        110        120 
PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPTRELAV 

       130        140        150        160        170        180 
QIQKGLLALG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA 

       190        200        210        220        230        240 
IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL 

       250        260        270        280        290        300 
VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA 

       310        320        330        340        350        360 
NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL 

       370        380        390        400        410 
YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a putative human translation initiation factor with similarity to initiation factor 4AII."
Leffers H., Wiemann S., Ansorge W.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
[2]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[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. expand/collapse author list , 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].
Tissue: Heart.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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. expand/collapse author list , 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].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Lymph, Placenta and Skin.
[8]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: T-cell.
[9]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 340-358, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"A human common nuclear matrix protein homologous to eukaryotic translation initiation factor 4A."
Holzmann K., Gerner C., Poeltl A., Schaefer R., Obrist P., Ensinger C., Grimm R., Sauermann G.
Biochem. Biophys. Res. Commun. 267:339-344(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Leukocyte.
[11]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]"eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay."
Shibuya T., Tange T.O., Sonenberg N., Moore M.J.
Nat. Struct. Mol. Biol. 11:346-351(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA SPLICING AND NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH MAGOH AND RBM8A, RNA-BINDING.
[13]"eIF4A3 is a novel component of the exon junction complex."
Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE EXON JUNCTION COMPLEX, INTERACTION WITH NXF1 AND ALYREF/THOC4, RNA-BINDING, SUBCELLULAR LOCATION.
[14]"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.
[15]"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH CASC3, MUTAGENESIS OF LYS-88, RNA-BINDING.
[17]"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, MASS SPECTROMETRY.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay."
Shibuya T., Tange T.O., Stroupe M.E., Moore M.J.
RNA 12:360-374(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASC3 AND MAGOH, MUTAGENESIS.
[20]"MLN51 stimulates the RNA-helicase activity of eIF4AIII."
Noble C.G., Song H.
PLoS ONE 2:E303-E303(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ATPASE AND RNA-HELICASE ACTIVITY.
[21]"SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs."
Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.
Cell 133:303-313(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLDIP3.
[22]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Exon junction complex enhances translation of spliced mRNAs at multiple steps."
Lee H.C., Choe J., Chi S.G., Kim Y.K.
Biochem. Biophys. Res. Commun. 384:334-340(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA TRANSLATION.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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-296 AND LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND THR-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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 MET-1 AND ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"CWC22 connects pre-mRNA splicing and exon junction complex assembly."
Steckelberg A.L., Boehm V., Gromadzka A.M., Gehring N.H.
Cell Rep. 2:454-461(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CWC22, MUTAGENESIS OF ASP-270; ASP-273; 276-THR-ILE-277 AND 301-ASN--THR-303.
[32]"Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly."
Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C., Blanchette M., Le Hir H.
Nat. Struct. Mol. Biol. 19:983-990(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH CASC3; CWC22; MAGOH; PRPF19 AND RBM8A, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-401 AND GLU-402.
[35]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay."
Alexandrov A., Colognori D., Shu M.D., Steitz J.A.
Proc. Natl. Acad. Sci. U.S.A. 109:21313-21318(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CWC22, MUTAGENESIS OF THR-334.
[37]"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
Bono F., Ebert J., Lorentzen E., Conti E.
Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-411 IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; AMP-PNP AND POLY URACIL.
[38]"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; ADP-NP AND POLY URACIL.
[39]"Mechanism of ATP turnover inhibition in the EJC."
Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R.
RNA 15:67-75(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; TRANSITION STATE ANALOG ADP-ALF3 AND POLY URACIL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79538 mRNA. Translation: CAA56074.1.
D21853 mRNA. Translation: BAA04879.2. Different initiation.
AK290608 mRNA. Translation: BAF83297.1.
CR456750 mRNA. Translation: CAG33031.1.
AC087741 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89584.1.
BC003662 mRNA. Translation: AAH03662.1.
BC004386 mRNA. Translation: AAH04386.1.
BC011151 mRNA. Translation: AAH11151.1.
PIRS45142.
RefSeqNP_055555.1. NM_014740.3.
UniGeneHs.389649.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HXYX-ray3.30A/B/C/D23-410[»]
2HYIX-ray2.30C/I1-411[»]
2J0QX-ray3.20A/B2-411[»]
2J0SX-ray2.21A2-411[»]
2J0UX-ray3.00A/B38-411[»]
2XB2X-ray3.40A/X1-411[»]
3EX7X-ray2.30C/H1-411[»]
4C9BX-ray2.00A1-411[»]
ProteinModelPortalP38919.
SMRP38919. Positions 21-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115119. 222 interactions.
DIPDIP-33218N.
IntActP38919. 134 interactions.
MINTMINT-1460615.
STRING9606.ENSP00000269349.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteP38919.

Polymorphism databases

DMDM20532400.

2D gel databases

REPRODUCTION-2DPAGEIPI00009328.

Proteomic databases

PaxDbP38919.
PeptideAtlasP38919.
PRIDEP38919.

Protocols and materials databases

DNASU9775.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269349; ENSP00000269349; ENSG00000141543.
GeneID9775.
KEGGhsa:9775.
UCSCuc002jxs.3. human.

Organism-specific databases

CTD9775.
GeneCardsGC17M078109.
HGNCHGNC:18683. EIF4A3.
HPAHPA021878.
MIM608546. gene.
neXtProtNX_P38919.
PharmGKBPA162384945.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG107989.
InParanoidP38919.
KOK13025.
OMATQIQKVI.
PhylomeDBP38919.
TreeFamTF300466.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP38919.
BgeeP38919.
CleanExHS_EIF4A3.
GenevestigatorP38919.

Family and domain databases

InterProIPR011545. 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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4A3. human.
EvolutionaryTraceP38919.
GeneWikiEIF4A3.
GenomeRNAi9775.
NextBio36802.
PROP38919.
SOURCESearch...

Entry information

Entry nameIF4A3_HUMAN
AccessionPrimary (citable) accession number: P38919
Secondary accession number(s): Q15033, Q6IBQ2, Q96A18
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM