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Q13838

- DX39B_HUMAN

UniProt

Q13838 - DX39B_HUMAN

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Protein
Spliceosome RNA helicase DDX39B
Gene
DDX39B, BAT1, UAP56
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.13 Publications
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 [1 Publication] reporting a stimulatory effect.13 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Kineticsi

  1. KM=3.3 µM for ATP1 Publication

Vmax=0.126 µM/min/mg enzyme with ATP as substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi89 – 968ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: UniProtKB
  3. ATP-dependent protein binding Source: BHF-UCL
  4. RNA-dependent ATPase activity Source: UniProtKB
  5. U4 snRNA binding Source: BHF-UCL
  6. U6 snRNA binding Source: BHF-UCL
  7. poly(A) RNA binding Source: UniProtKB
  8. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. RNA secondary structure unwinding Source: BHF-UCL
  3. RNA splicing Source: BHF-UCL
  4. mRNA export from nucleus Source: UniProtKB
  5. mRNA splicing, via spliceosome Source: UniProtKB
  6. negative regulation of DNA damage checkpoint Source: UniProtKB
  7. positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  8. spliceosomal complex assembly Source: BHF-UCL
  9. viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Spliceosome RNA helicase DDX39B (EC:3.6.4.13)
Alternative name(s):
56 kDa U2AF65-associated protein
ATP-dependent RNA helicase p47
DEAD box protein UAP56
HLA-B-associated transcript 1 protein
Gene namesi
Name:DDX39B
Synonyms:BAT1, UAP56
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:13917. DDX39B.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. spliceosomal complex Source: BHF-UCL
  5. transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 963GKT → AAA: Loss of ATPase and helicase activity. 1 Publication
Mutagenesisi95 – 951K → A: Loss of ATPase and helicase activity. 2 Publications
Mutagenesisi197 – 1971E → A: Loss of ATPase and helicase activity. 1 Publication
Mutagenesisi198 – 1981C → A: No effect on ATPase activity. 1 Publication
Mutagenesisi199 – 1991D → A: Increased ATPase activity and loss of helicase activity. 1 Publication
Mutagenesisi228 – 2303SAT → AAA: Decreased ATPase activity and loss of helicase activity. 1 Publication

Organism-specific databases

PharmGKBiPA25262.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 428427Spliceosome RNA helicase DDX39B
PRO_0000055071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei36 – 361N6-acetyllysine1 Publication
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei172 – 1721Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13838.
PaxDbiQ13838.
PRIDEiQ13838.

PTM databases

PhosphoSiteiQ13838.

Expressioni

Gene expression databases

ArrayExpressiQ13838.
BgeeiQ13838.
CleanExiHS_BAT1.
GenevestigatoriQ13838.

Organism-specific databases

HPAiCAB034012.

Interactioni

Subunit structurei

Homodimer, and heterodimer with DDX39A. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have dynamic structure involving ATP-dependent remodeling; in the complex bridges ALYREF/THOC4 and the THO complex, and, in a ATP-dependent manner, ALYREF/THOC4 and SARNP/CIP29. Component of the spliceosome. Interacts directly with U2AF2. Interacts with RBM8A, RNPS1 and SRRM1, FYTTD1/UIF, THOC1, MX1 and POLDIP3. Interacts with human cytomegalovirus/HHV-5 protein UL69.15 Publications

Protein-protein interaction databases

BioGridi113649. 61 interactions.
IntActiQ13838. 33 interactions.
MINTiMINT-1032422.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 504
Helixi54 – 629
Helixi70 – 8011
Beta strandi85 – 884
Helixi95 – 10612
Beta strandi116 – 1194
Helixi123 – 13614
Turni137 – 1393
Beta strandi145 – 1495
Helixi154 – 16310
Beta strandi167 – 1715
Helixi173 – 1819
Beta strandi183 – 1853
Beta strandi192 – 1976
Helixi198 – 2025
Helixi205 – 21612
Beta strandi220 – 22910
Turni233 – 2353
Helixi236 – 2405
Beta strandi247 – 2504
Beta strandi263 – 2686
Helixi271 – 2733
Helixi274 – 28411
Beta strandi288 – 2936
Helixi297 – 30913
Beta strandi314 – 3174
Beta strandi319 – 3213
Helixi323 – 33412
Beta strandi335 – 3373
Beta strandi339 – 3457
Helixi353 – 3553
Beta strandi357 – 3637
Helixi368 – 37811
Helixi380 – 3823
Beta strandi386 – 3916
Helixi394 – 40714
Beta strandi411 – 4133
Beta strandi417 – 4193
Helixi420 – 4223

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5IX-ray1.90A259-428[»]
1T6NX-ray1.94A/B34-251[»]
1XTIX-ray1.95A46-428[»]
1XTJX-ray2.70A44-423[»]
1XTKX-ray2.40A45-428[»]
ProteinModelPortaliQ13838.
SMRiQ13838. Positions 46-426.

Miscellaneous databases

EvolutionaryTraceiQ13838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 249174Helicase ATP-binding
Add
BLAST
Domaini261 – 422162Helicase C-terminal
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 7329Q motif
Add
BLAST
Motifi196 – 1994DECD box

Domaini

The helicase C-terminal domain mediates interaction with ALYREF/THOC4.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0513.
HOVERGENiHBG107334.
InParanoidiQ13838.
KOiK12812.
PhylomeDBiQ13838.
TreeFamiTF300442.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13838-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF    50
LLKPELLRAI VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV 100
LATLQQLEPV TGQVSVLVMC HTRELAFQIS KEYERFSKYM PNVKVAVFFG 150
GLSIKKDEEV LKKNCPHIVV GTPGRILALA RNKSLNLKHI KHFILDECDK 200
MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR KFMQDPMEIF 250
VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC 300
IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG 350
MDIERVNIAF NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL 400
NDVQDRFEVN ISELPDEIDI SSYIEQTR 428
Length:428
Mass (Da):48,991
Last modified:November 1, 1996 - v1
Checksum:i7A55167BF576FB6F
GO
Isoform 2 (identifier: Q13838-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-114: V → VYLGRVLGRGFWLGLV

Note: No experimental confirmation available.

Show »
Length:443
Mass (Da):50,679
Checksum:i5B25C9C18CA433A4
GO

Sequence cautioni

The sequence CAI17665.2 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 1141V → VYLGRVLGRGFWLGLV in isoform 2.
VSP_026347

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891Q → R in BAD96632. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z37166 mRNA. Translation: CAA85523.1.
BT009909 mRNA. Translation: AAP88911.1.
AK222912 mRNA. Translation: BAD96632.1.
AB088115 Genomic DNA. Translation: BAC54953.1.
AB103621 Genomic DNA. Translation: BAF31287.1.
AB202112 Genomic DNA. Translation: BAE78637.1.
BA000025 Genomic DNA. Translation: BAB63306.1.
AL662847 Genomic DNA. Translation: CAI17664.2.
AL662847 Genomic DNA. Translation: CAI17665.2. Sequence problems.
AL662801 Genomic DNA. Translation: CAI18279.2.
AL662801 Genomic DNA. Translation: CAI18280.1.
AL662801 Genomic DNA. Translation: CAI18281.2.
AL662801 Genomic DNA. Translation: CAI18282.2.
AL662801 Genomic DNA. Translation: CAI18283.2.
BX001040 Genomic DNA. Translation: CAI18634.1.
BX248516 Genomic DNA. Translation: CAI41922.1.
BX927320 Genomic DNA. Translation: CAQ09974.1.
CR753820 Genomic DNA. Translation: CAQ07176.1.
CR753864 Genomic DNA. Translation: CAQ10634.1.
CH471081 Genomic DNA. Translation: EAX03404.1.
BC000361 mRNA. Translation: AAH00361.1.
BC013006 mRNA. Translation: AAH13006.1.
AF029061 Genomic DNA. Translation: AAB94615.1.
AF029062 Genomic DNA. Translation: AAC63046.1.
CCDSiCCDS4697.1. [Q13838-1]
PIRiI37201.
RefSeqiNP_004631.1. NM_004640.6. [Q13838-1]
NP_542165.1. NM_080598.5. [Q13838-1]
UniGeneiHs.254042.
Hs.730849.

Genome annotation databases

EnsembliENST00000383508; ENSP00000373000; ENSG00000215425. [Q13838-1]
ENST00000396172; ENSP00000379475; ENSG00000198563. [Q13838-1]
ENST00000400295; ENSP00000383151; ENSG00000215425. [Q13838-1]
ENST00000400296; ENSP00000383152; ENSG00000215425. [Q13838-1]
ENST00000412106; ENSP00000393712; ENSG00000225073. [Q13838-1]
ENST00000412330; ENSP00000398775; ENSG00000225859. [Q13838-1]
ENST00000413678; ENSP00000391463; ENSG00000229496. [Q13838-1]
ENST00000414440; ENSP00000411853; ENSG00000229496. [Q13838-1]
ENST00000415689; ENSP00000390999; ENSG00000225073. [Q13838-1]
ENST00000416863; ENSP00000407419; ENSG00000229496. [Q13838-1]
ENST00000430784; ENSP00000399030; ENSG00000235439. [Q13838-1]
ENST00000431360; ENSP00000404695; ENSG00000235439. [Q13838-1]
ENST00000441425; ENSP00000388880; ENSG00000230624. [Q13838-1]
ENST00000445218; ENSP00000411136; ENSG00000225859. [Q13838-1]
ENST00000448296; ENSP00000405560; ENSG00000225859. [Q13838-1]
ENST00000453138; ENSP00000387994; ENSG00000230624. [Q13838-1]
ENST00000456476; ENSP00000400326; ENSG00000225073. [Q13838-1]
ENST00000456666; ENSP00000394160; ENSG00000230624. [Q13838-1]
ENST00000458640; ENSP00000416269; ENSG00000198563. [Q13838-1]
GeneIDi7919.
KEGGihsa:7919.
UCSCiuc003ntt.3. human. [Q13838-1]

Polymorphism databases

DMDMi2500529.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z37166 mRNA. Translation: CAA85523.1 .
BT009909 mRNA. Translation: AAP88911.1 .
AK222912 mRNA. Translation: BAD96632.1 .
AB088115 Genomic DNA. Translation: BAC54953.1 .
AB103621 Genomic DNA. Translation: BAF31287.1 .
AB202112 Genomic DNA. Translation: BAE78637.1 .
BA000025 Genomic DNA. Translation: BAB63306.1 .
AL662847 Genomic DNA. Translation: CAI17664.2 .
AL662847 Genomic DNA. Translation: CAI17665.2 . Sequence problems.
AL662801 Genomic DNA. Translation: CAI18279.2 .
AL662801 Genomic DNA. Translation: CAI18280.1 .
AL662801 Genomic DNA. Translation: CAI18281.2 .
AL662801 Genomic DNA. Translation: CAI18282.2 .
AL662801 Genomic DNA. Translation: CAI18283.2 .
BX001040 Genomic DNA. Translation: CAI18634.1 .
BX248516 Genomic DNA. Translation: CAI41922.1 .
BX927320 Genomic DNA. Translation: CAQ09974.1 .
CR753820 Genomic DNA. Translation: CAQ07176.1 .
CR753864 Genomic DNA. Translation: CAQ10634.1 .
CH471081 Genomic DNA. Translation: EAX03404.1 .
BC000361 mRNA. Translation: AAH00361.1 .
BC013006 mRNA. Translation: AAH13006.1 .
AF029061 Genomic DNA. Translation: AAB94615.1 .
AF029062 Genomic DNA. Translation: AAC63046.1 .
CCDSi CCDS4697.1. [Q13838-1 ]
PIRi I37201.
RefSeqi NP_004631.1. NM_004640.6. [Q13838-1 ]
NP_542165.1. NM_080598.5. [Q13838-1 ]
UniGenei Hs.254042.
Hs.730849.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T5I X-ray 1.90 A 259-428 [» ]
1T6N X-ray 1.94 A/B 34-251 [» ]
1XTI X-ray 1.95 A 46-428 [» ]
1XTJ X-ray 2.70 A 44-423 [» ]
1XTK X-ray 2.40 A 45-428 [» ]
ProteinModelPortali Q13838.
SMRi Q13838. Positions 46-426.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113649. 61 interactions.
IntActi Q13838. 33 interactions.
MINTi MINT-1032422.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei Q13838.

Polymorphism databases

DMDMi 2500529.

Proteomic databases

MaxQBi Q13838.
PaxDbi Q13838.
PRIDEi Q13838.

Protocols and materials databases

DNASUi 7919.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000383508 ; ENSP00000373000 ; ENSG00000215425 . [Q13838-1 ]
ENST00000396172 ; ENSP00000379475 ; ENSG00000198563 . [Q13838-1 ]
ENST00000400295 ; ENSP00000383151 ; ENSG00000215425 . [Q13838-1 ]
ENST00000400296 ; ENSP00000383152 ; ENSG00000215425 . [Q13838-1 ]
ENST00000412106 ; ENSP00000393712 ; ENSG00000225073 . [Q13838-1 ]
ENST00000412330 ; ENSP00000398775 ; ENSG00000225859 . [Q13838-1 ]
ENST00000413678 ; ENSP00000391463 ; ENSG00000229496 . [Q13838-1 ]
ENST00000414440 ; ENSP00000411853 ; ENSG00000229496 . [Q13838-1 ]
ENST00000415689 ; ENSP00000390999 ; ENSG00000225073 . [Q13838-1 ]
ENST00000416863 ; ENSP00000407419 ; ENSG00000229496 . [Q13838-1 ]
ENST00000430784 ; ENSP00000399030 ; ENSG00000235439 . [Q13838-1 ]
ENST00000431360 ; ENSP00000404695 ; ENSG00000235439 . [Q13838-1 ]
ENST00000441425 ; ENSP00000388880 ; ENSG00000230624 . [Q13838-1 ]
ENST00000445218 ; ENSP00000411136 ; ENSG00000225859 . [Q13838-1 ]
ENST00000448296 ; ENSP00000405560 ; ENSG00000225859 . [Q13838-1 ]
ENST00000453138 ; ENSP00000387994 ; ENSG00000230624 . [Q13838-1 ]
ENST00000456476 ; ENSP00000400326 ; ENSG00000225073 . [Q13838-1 ]
ENST00000456666 ; ENSP00000394160 ; ENSG00000230624 . [Q13838-1 ]
ENST00000458640 ; ENSP00000416269 ; ENSG00000198563 . [Q13838-1 ]
GeneIDi 7919.
KEGGi hsa:7919.
UCSCi uc003ntt.3. human. [Q13838-1 ]

Organism-specific databases

CTDi 7919.
GeneCardsi GC06M031500.
GC06Mj31485.
GC06Mk31480.
GC06Ml31538.
GC06Mm31574.
GC06Mn31488.
GC06Mo31487.
HGNCi HGNC:13917. DDX39B.
HPAi CAB034012.
MIMi 142560. gene.
neXtProti NX_Q13838.
PharmGKBi PA25262.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
HOVERGENi HBG107334.
InParanoidi Q13838.
KOi K12812.
PhylomeDBi Q13838.
TreeFami TF300442.

Miscellaneous databases

ChiTaRSi DDX39B. human.
EvolutionaryTracei Q13838.
GeneWikii BAT1.
GenomeRNAii 7919.
NextBioi 30405.
PROi Q13838.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13838.
Bgeei Q13838.
CleanExi HS_BAT1.
Genevestigatori Q13838.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The BAT1 gene in the MHC encodes an evolutionarily conserved putative nuclear RNA helicase of the DEAD family."
    Peelman L., Chardon P., Nunes M., Renard C., Geffrotin C., Vaiman M., van Zeveren A., Coppieters W., van de Weghe A., Bouquet Y., Choy W., Strominger J., Spies T.
    Genomics 26:210-218(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney epithelium.
  4. "Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
    Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.
    , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
    Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  8. "Homo sapiens BAT1 (BAT1) gene, partial cds; and PERB18 pseudogene, complete sequence."
    Allcock R.J.N., Price P., Gaudieri S., Leelayuwat C., Witt C.S., Dawkins R.L.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-428.
  9. "U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction."
    Fleckner J., Zhang M., Valcarcel J., Green M.R.
    Genes Dev. 11:1864-1872(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH U2AF2 AND THE SPLICEOSOME, SUBCELLULAR LOCATION.
  10. "Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly."
    Luo M.-J., Zhou Z., Magni K., Christoforides C., Rappsilber J., Mann M., Reed R.
    Nature 413:644-647(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALYREF/THOC4 AND THE SPLICEOSOME, SUBCELLULAR LOCATION.
  11. "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
    McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
    J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM8A; RNPS1; SRRM1 AND ALYREF/THOC4.
  12. "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., Semple J.I., Brown S.E., Counsell D., Campbell R.D., Sanderson C.M.
    Genomics 83:153-167(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH ALYREF/THOC4 AND DDX39A.
  13. "Linking transcriptional elongation and messenger RNA export to metastatic breast cancers."
    Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.
    Cancer Res. 65:3011-3016(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Recruitment of the human TREX complex to mRNA during splicing."
    Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.
    Genes Dev. 19:1512-1517(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ALYREF/THOC4, DOMAIN.
  15. "Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors."
    Li Y., Wang X., Zhang X., Goodrich D.W.
    Mol. Cell. Biol. 25:4023-4033(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THOC1, SUBCELLULAR LOCATION.
  16. "Human mRNA export machinery recruited to the 5' end of mRNA."
    Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
    Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE TREX COMPLEX.
  17. "The UL69 transactivator protein of human cytomegalovirus interacts with DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation of unspliced RNA."
    Lischka P., Toth Z., Thomas M., Mueller R., Stamminger T.
    Mol. Cell. Biol. 26:1631-1643(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
  18. "Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factor."
    Shen J., Zhang L., Zhao R.
    J. Biol. Chem. 282:22544-22550(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 94-GLY--THR-96; LYS-95; GLU-197; ASP-199 AND 228-SER--THR-230.
  19. "ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56."
    Taniguchi I., Ohno M.
    Mol. Cell. Biol. 28:601-608(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALYREF, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-95.
  20. "Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
    Boyne J.R., Colgan K.J., Whitehouse A.
    PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE TREX COMPLEX.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  23. "UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA."
    Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., Jones R., Ponting C.P., Dickman M.J., Wilson S.A.
    Curr. Biol. 19:1918-1924(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYTTD1.
  24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex."
    Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.
    Genes Dev. 24:2043-2053(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALYREF AND SARNP.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Interferon-induced antiviral protein MxA interacts with the cellular RNA helicases UAP56 and URH49."
    Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.
    J. Biol. Chem. 286:34743-34751(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MX1.
  29. "Genome instability and transcription elongation impairment in human cells depleted of THO/TREX."
    Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R., Aguilera A.
    PLoS Genet. 7:E1002386-E1002386(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export."
    Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.
    PLoS ONE 7:E43804-E43804(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLDIP3.
  32. Cited for: FUNCTION, INTERACTION WITH CHTOP.
  33. "Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA."
    Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.
    Nucleic Acids Res. 41:1294-1306(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  34. "Crystal structure of the human ATP-dependent splicing and export factor UAP56."
    Shi H., Cordin O., Minder C.M., Linder P., Xu R.-M.
    Proc. Natl. Acad. Sci. U.S.A. 101:17628-17633(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 44-428 IN COMPLEX WITH ADP, FUNCTION, MUTAGENESIS OF CYS-198.
  35. "Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export."
    Zhao R., Shen J., Green M.R., MacMorris M., Blumenthal T.
    Structure 12:1373-1381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-428, DIMERIZATION.

Entry informationi

Entry nameiDX39B_HUMAN
AccessioniPrimary (citable) accession number: Q13838
Secondary accession number(s): B0S8C0
, O43496, Q0EFA1, Q2L6F9, Q53GL9, Q5RJ64, Q5RJ66, Q5ST94, Q5STB4, Q5STB5, Q5STB7, Q5STB8, Q5STU4, Q5STU5, Q5STU6, Q5STU8, Q71V76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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