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Q13838

- DX39B_HUMAN

UniProt

Q13838 - DX39B_HUMAN

Protein

Spliceosome RNA helicase DDX39B

Gene

DDX39B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.
    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.

    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 substrate1 Publication

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    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.

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 963GKT → AAA: Loss of ATPase and helicase activity.
    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.

    Organism-specific databases

    PharmGKBiPA25262.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 428427Spliceosome RNA helicase DDX39BPRO_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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALYREFQ86V814EBI-348622,EBI-347640
    CHTOPQ9Y3Y26EBI-348622,EBI-347794

    Protein-protein interaction databases

    BioGridi113649. 62 interactions.
    IntActiQ13838. 33 interactions.
    MINTiMINT-1032422.

    Structurei

    Secondary structure

    1
    428
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13838.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 249174Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 422162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

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

    Domaini

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

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    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.

    Experimental Info

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei114 – 1141V → VYLGRVLGRGFWLGLV in isoform 2. CuratedVSP_026347

    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113649. 62 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

    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: October 1, 2014
    This is version 151 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