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3.A.18.1.1
The nuclear mRNA Export Complex (mRNA-E also called TREX) (including the exon junction complex) [TAP+p15 interact as a complex with the nuclear pore to facilitate mRNA transport to the cytoplasm] (Nojimma et al. 2007; Cheng et al., 2006)

Accession Number:P38919
Protein Name:Eukaryotic initiation factor 4A-III aka Eif4A3
Length:411
Molecular Weight:46871.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate mRNA

Cross database links:

Genevestigator: P38919
eggNOG: prNOG15154
HEGENOM: HBG737336
RefSeq: NP_055555.1   
Entrez Gene ID: 9775   
Pfam: PF00270    PF00271   
OMIM: 608546  gene
KEGG: hsa:9775   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0016607 C:nuclear speck
GO:0005681 C:spliceosomal complex
GO:0005524 F:ATP binding
GO:0004004 F:ATP-dependent RNA helicase activity
GO:0008143 F:poly(A) RNA binding
GO:0005515 F:protein binding
GO:0006397 P:mRNA processing
GO:0051028 P:mRNA transport
GO:0017148 P:negative regulation of translation
GO:0000184 P:nuclear-transcribed mRNA catabolic process,...
GO:0008380 P:RNA splicing
GO:0006364 P:rRNA processing

References (26)

[1] “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.et.al.   7788527
[2] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[3] “DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.”  Zody M.C.et.al.   16625196
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “A human common nuclear matrix protein homologous to eukaryotic translation initiation factor 4A.”  Holzmann K.et.al.   10623621
[6] “Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.”  Jurica M.S.et.al.   11991638
[7] “eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay.”  Shibuya T.et.al.   15034551
[8] “eIF4A3 is a novel component of the exon junction complex.”  Chan C.C.et.al.   14730019
[9] “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.et.al.   15715967
[10] “Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements.”  Gehring N.H.et.al.   16209946
[11] “The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity.”  Ballut L.et.al.   16170325
[12] “Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core.”  Tange T.O.et.al.   16314458
[13] “Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay.”  Shibuya T.et.al.   16495234
[14] “MLN51 stimulates the RNA-helicase activity of eIF4AIII.”  Noble C.G.et.al.   17375189
[15] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[16] “SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs.”  Ma X.M.et.al.   18423201
[17] “Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.”  Cantin G.T.et.al.   18220336
[18] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[19] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[20] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[21] “Exon junction complex enhances translation of spliced mRNAs at multiple steps.”  Lee H.C.et.al.   19409878
[22] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[23] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[24] “The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA.”  Bono F.et.al.   16923391
[25] “Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.”  Andersen C.B.et.al.   16931718
[26] “Mechanism of ATP turnover inhibition in the EJC.”  Nielsen K.H.et.al.   19033377
Structure:
2HXY   2HYI   2J0Q   2J0S   2J0U   3EX7   2XB2   4C9B     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
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FASTA formatted sequence
1:	MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK 
61:	PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPTRELAV 
121:	QIQKGLLALG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA 
181:	IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL 
241:	VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA 
301:	NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL 
361:	YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I