BAT1 Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability. Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect. Belongs to the DEAD box helicase family. DECD subfamily. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.13; Helicase; RNA splicing; RNA-binding; Spliceosome
Chromosomal Location of Human Ortholog: 6p21.33
Cellular Component:  nuclear matrix; nuclear speck; nucleoplasm; nucleus; spliceosomal complex; transcription export complex
Molecular Function:  ATP binding; ATP-dependent protein binding; ATP-dependent RNA helicase activity; ATPase activity; identical protein binding; protein binding; protein-containing complex binding; RNA-dependent ATPase activity; U4 snRNA binding; U6 snRNA binding
Biological Process:  liver development; mRNA 3'-end processing; mRNA export from nucleus; mRNA splicing, via spliceosome; negative regulation of DNA damage checkpoint; positive regulation of cell growth involved in cardiac muscle cell development; positive regulation of DNA biosynthetic process; positive regulation of DNA-templated transcription, elongation; positive regulation of translation; positive regulation of vascular smooth muscle cell proliferation; RNA export from nucleus; RNA secondary structure unwinding; RNA splicing; spliceosomal complex assembly; viral mRNA export from host cell nucleus
Reference #:  Q13838 (UniProtKB)
Alt. Names/Synonyms: 56 kDa U2AF65-associated protein; ATP-dependent RNA helicase p47; BAT1; D6S81E; DDX39B; DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B; DEAD box protein UAP56; DEAD-box helicase 39B; DEAD-box protein UAP56; DExD-box helicase 39B; DX39B; HLA-B associated transcript 1; HLA-B-associated transcript 1 protein; nuclear RNA helicase (DEAD family); Spliceosome RNA helicase BAT1; Spliceosome RNA helicase DDX39B; UAP56
Gene Symbols: DDX39B
Molecular weight: 48,991 Da
Basal Isoelectric point: 5.44  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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BAT1

Protein Structure Not Found.


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