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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:Q9UBU9
Protein Name:Nuclear RNA export factor 1 aka TAP aka NXF1 aka REF
Length:619
Molecular Weight:70182.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Nucleus1
Substrate mRNA

Cross database links:

Genevestigator: Q9UBU9
HEGENOM: HBG714807
RefSeq: NP_006353.2   
Entrez Gene ID: 10482   
Pfam: PF00560    PF02136    PF03943   
OMIM: 602647  gene

Gene Ontology

GO:0005737 C:cytoplasm
GO:0016607 C:nuclear speck
GO:0000166 F:nucleotide binding
GO:0005515 F:protein binding
GO:0044419 P:interspecies interaction between organisms

References (24)

[1] “TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus.”  Braun I.C.et.al.   10202158
[2] “The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences.”  Kang Y.et.al.   10323864
[3] “Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs.”  Bear J.et.al.   10454577
[4] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[5] “Human chromosome 11 DNA sequence and analysis including novel gene identification.”  Taylor T.D.et.al.   16554811
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation.”  Yoon D.-W.et.al.   9175835
[8] “TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus.”  Grueter P.et.al.   9660949
[9] “The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human.”  Katahira J.et.al.   10228171
[10] “Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export.”  Braun I.C.et.al.   11259411
[11] “The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.”  Bachi A.et.al.   10668806
[12] “Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins.”  Suyama M.et.al.   11256625
[13] “Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex.”  Kataoka N.et.al.   11707413
[14] “Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.”  Kim V.N.et.al.   11546873
[15] “Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.”  Lykke-Andersen J.et.al.   11546874
[16] “eIF4A3 is a novel component of the exon junction complex.”  Chan C.C.et.al.   14730019
[17] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[18] “UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA.”  Hautbergue G.M.et.al.   19836239
[19] “Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA.”  Katahira J.et.al.   19165146
[20] “Assembly and mobility of exon-exon junction complexes in living cells.”  Schmidt U.et.al.   19324961
[21] “The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain.”  Liker E.et.al.   11060011
[22] “Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.”  Fribourg S.et.al.   11583626
[23] “Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution.”  Grant R.P.et.al.   12581645
[24] “Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.”  Grant R.P.et.al.   11875519
Structure:
1FO1   1FT8   1GO5   1JKG   1JN5   1KOH   1KOO   1OAI   2Z5K   2Z5M   [...more]

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:	MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA 
61:	MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF 
121:	KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL 
181:	DRENRRISII INSSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA 
241:	QNIDVVLNRR SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG 
301:	NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR LDGHELPPPI 
361:	AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS GDRQGLLDAY HDGACCSLSI 
421:	PFIPQNPARS SLAEYFKDSR NVKKLKDPTL RFRLLKHTRL NVVAFLNELP KTQHDVNSFV 
481:	VDISAQTSTL LCFSVNGVFK EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS 
541:	SEEIQRAFAM PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA 
601:	QAFTHLKAKG EIPEVAFMK