DDX39B
entrez
7919
canonical
uniprot
Q13838
canonical
ensembl
ENSG00000198563
resolver
ensembl
ENSG00000215425
resolver
ensembl
ENSG00000225073
resolver
ensembl
ENSG00000225859
resolver
ensembl
ENSG00000229496
resolver
ensembl
ENSG00000230624
resolver
ensembl
ENSG00000235439
resolver
ensp
ENSP00000379475
resolver
ensp
ENSP00000416269
resolver
genesymbol
DDX39B
resolver
genesymbol_syn
BAT1
resolver
genesymbol_syn
UAP56
resolver
hgnc
HGNC:13917
resolver
uniprot
B0S8C0
resolver
uniprot
O43496
resolver
uniprot
Q0EFA1
resolver
uniprot
Q2L6F9
resolver
uniprot
Q53GL9
resolver
uniprot
Q5RJ64
resolver
uniprot
Q5RJ66
resolver
uniprot
Q5ST94
resolver
uniprot
Q5STB4
resolver
uniprot
Q5STB5
resolver
uniprot
Q5STB7
resolver
uniprot
Q5STB8
resolver
uniprot
Q5STU4
resolver
uniprot
Q5STU5
resolver
uniprot
Q5STU6
resolver
uniprot
Q5STU8
resolver
uniprot
Q71V76
resolver
uniprot_entry
DX39B_HUMAN
resolver
uniprot_sec
B0S8C0
resolver
uniprot_sec
O43496
resolver
uniprot_sec
Q0EFA1
resolver
uniprot_sec
Q2L6F9
resolver
uniprot_sec
Q53GL9
resolver
uniprot_sec
Q5RJ64
resolver
uniprot_sec
Q5RJ66
resolver
uniprot_sec
Q5ST94
resolver
uniprot_sec
Q5STB4
resolver
uniprot_sec
Q5STB5
resolver
uniprot_sec
Q5STB7
resolver
uniprot_sec
Q5STB8
resolver
uniprot_sec
Q5STU4
resolver
uniprot_sec
Q5STU5
resolver
uniprot_sec
Q5STU6
resolver
uniprot_sec
Q5STU8
resolver
uniprot_sec
Q71V76
resolver
amino_acid_sequence
MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Involved in nuclear export of spliced and unspliced mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). 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 (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex 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/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). The THOC1-THOC2-THOC3 core complex alone is sufficient to promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). Associates with SARNP/CIP29, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC4 and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4. 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. {ECO:0000269|PubMed:11675789, ECO:0000269|PubMed:15585580, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17562711, ECO:0000269|PubMed:17984224, ECO:0000269|PubMed:20844015, ECO:0000269|PubMed:22144908, ECO:0000269|PubMed:23222130, ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:33191911, ECO:0000269|PubMed:37578863, ECO:0000269|PubMed:9242493}.; FUNCTION: 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. {ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:9242493}.; FUNCTION: (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}.
uniprot
proteins
mass_dalton
48991
uniprot
proteins
mutagenesis
MUTAGEN 94..96; /note="GKT->AAA: Loss of ATPase and helicase activity."; /evidence="ECO:0000269|PubMed:17562711"; MUTAGEN 95; /note="K->A: Loss of ATPase and helicase activity."; /evidence="ECO:0000269|PubMed:17562711, ECO:0000269|PubMed:17984224"; MUTAGEN 197; /note="E->A: Loss of ATPase and helicase activity."; /evidence="ECO:0000269|PubMed:17562711"; MUTAGEN 198; /note="C->A: No effect on ATPase activity."; /evidence="ECO:0000269|PubMed:15585580"; MUTAGEN 199; /note="D->A: Increased ATPase activity and loss of helicase activity."; /evidence="ECO:0000269|PubMed:17562711"; MUTAGEN 228..230; /note="SAT->AAA: Decreased ATPase activity and loss of helicase activity."; /evidence="ECO:0000269|PubMed:17562711"; MUTAGEN 283; /note="D->R: Abolishes interaction with SARNP; when associated with 2-A--T-258 del."; /evidence="ECO:0000269|PubMed:37578863
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DECD subfamily
uniprot
proteins
pubmed
11675789
uniprot
proteins
pubmed
12944400
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14667819
uniprot
proteins
pubmed
15296731
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15585580
uniprot
proteins
pubmed
15833825
uniprot
proteins
pubmed
15870275
uniprot
proteins
pubmed
15998806
uniprot
proteins
pubmed
16478985
uniprot
proteins
pubmed
16702430
uniprot
proteins
pubmed
17190602
uniprot
proteins
pubmed
17562711
uniprot
proteins
pubmed
17984224
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18974867
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19836239
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20844015
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21859714
uniprot
proteins
pubmed
22144908
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22928037
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23222130
uniprot
proteins
pubmed
23299939
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25662211
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
33191911
uniprot
proteins
pubmed
37020021
uniprot
proteins
pubmed
37578863
uniprot
proteins
pubmed
7601445
uniprot
proteins
pubmed
9242493
uniprot
proteins
sequence_length
428
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Can translocate to the cytoplasm in the presence of MX1. TREX complex assembly seems to occur in regions surrounding nuclear speckles known as perispeckles.
uniprot
proteins