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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:Q13838
Protein Name:Spliceosome RNA helicase BAT1 aka DEAD box protein UAP56
Length:428
Molecular Weight:48991.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate mRNA

Cross database links:

Genevestigator: Q13838
RefSeq: NP_004631.1    NP_542165.1   
Entrez Gene ID: 7919   
Pfam: PF00270    PF00271   
OMIM: 142560  gene
KEGG: hsa:7919   

Gene Ontology

GO:0016607 C:nuclear speck
GO:0005681 C:spliceosomal complex
GO:0000346 C:transcription export complex
GO:0005524 F:ATP binding
GO:0043008 F:ATP-dependent protein binding
GO:0004004 F:ATP-dependent RNA helicase activity
GO:0042802 F:identical protein binding
GO:0030621 F:U4 snRNA binding
GO:0017070 F:U6 snRNA binding
GO:0046784 P:intronless viral mRNA export from host nucleus
GO:0010501 P:RNA secondary structure unwinding
GO:0000245 P:spliceosome assembly

References (20)

[1] “The BAT1 gene in the MHC encodes an evolutionarily conserved putative nuclear RNA helicase of the DEAD family.”  Peelman L.et.al.   7601445
[2] “Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity.”  Shiina T.et.al.   16702430
[3] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[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] “U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction.”  Fleckner J.et.al.   9242493
[6] “Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly.”  Luo M.-J.et.al.   11675789
[7] “An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.”  McCracken S.et.al.   12944400
[8] “Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.”  Lehner B.et.al.   14667819
[9] “Linking transcriptional elongation and messenger RNA export to metastatic breast cancers.”  Guo S.et.al.   15833825
[10] “Recruitment of the human TREX complex to mRNA during splicing.”  Masuda S.et.al.   15998806
[11] “Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors.”  Li Y.et.al.   15870275
[12] “Human mRNA export machinery recruited to the 5' end of mRNA.”  Cheng H.et.al.   17190602
[13] “Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factor.”  Shen J.et.al.   17562711
[14] “Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication.”  Boyne J.R.et.al.   18974867
[15] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[16] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[17] “UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA.”  Hautbergue G.M.et.al.   19836239
[18] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[19] “Crystal structure of the human ATP-dependent splicing and export factor UAP56.”  Shi H.et.al.   15585580
[20] “Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export.”  Zhao R.et.al.   15296731
Structure:
1T5I   1T6N   1XTI   1XTJ   1XTK     

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)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI 
61:	VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC 
121:	HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA 
181:	RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR 
241:	KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC 
301:	IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF 
361:	NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI 
421:	SSYIEQTR