Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13838 (DX39B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DDX39B
Synonyms:BAT1, UAP56
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.25 Ref.29 Ref.32 Ref.33 Ref.34

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 [Ref.32] reporting a stimulatory effect. Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.25 Ref.29 Ref.32 Ref.33 Ref.34

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.19

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.23 Ref.25 Ref.28 Ref.31 Ref.32 Ref.35

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. Ref.1 Ref.9 Ref.10 Ref.15 Ref.28

Domain

The helicase C-terminal domain mediates interaction with ALYREF/THOC4. Ref.14

Sequence similarities

Belongs to the DEAD box helicase family. DECD subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.3 µM for ATP Ref.18

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

Sequence caution

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

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.18PubMed 18593880. Source: GOC

RNA secondary structure unwinding

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

RNA splicing

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

mRNA export from nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred from genetic interaction PubMed 15047853. Source: UniProtKB

negative regulation of DNA damage checkpoint

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of DNA-templated transcription, elongation

Inferred from mutant phenotype Ref.29. Source: UniProtKB

spliceosomal complex assembly

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

viral mRNA export from host cell nucleus

Inferred from direct assay Ref.20. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.28. Source: UniProtKB

spliceosomal complex

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

transcription export complex

Inferred from direct assay Ref.13Ref.14. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Inferred from direct assay Ref.18. Source: UniProtKB

ATP-dependent protein binding

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

RNA-dependent ATPase activity

Inferred from direct assay Ref.18. Source: UniProtKB

U4 snRNA binding

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

U6 snRNA binding

Inferred from direct assay PubMed 18593880. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13838-1)

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.
Isoform 2 (identifier: Q13838-2)

The sequence of this isoform differs from the canonical sequence as follows:
     114-114: V → VYLGRVLGRGFWLGLV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 428427Spliceosome RNA helicase DDX39B
PRO_0000055071

Regions

Domain76 – 249174Helicase ATP-binding
Domain261 – 422162Helicase C-terminal
Nucleotide binding89 – 968ATP
Motif45 – 7329Q motif
Motif196 – 1994DECD box

Amino acid modifications

Modified residue21N-acetylalanine Ref.22 Ref.30
Modified residue361N6-acetyllysine Ref.24
Modified residue381Phosphoserine Ref.26
Modified residue1721Phosphothreonine Ref.26

Natural variations

Alternative sequence1141V → VYLGRVLGRGFWLGLV in isoform 2.
VSP_026347

Experimental info

Mutagenesis94 – 963GKT → AAA: Loss of ATPase and helicase activity. Ref.18
Mutagenesis951K → A: Loss of ATPase and helicase activity. Ref.18 Ref.19
Mutagenesis1971E → A: Loss of ATPase and helicase activity. Ref.18
Mutagenesis1981C → A: No effect on ATPase activity. Ref.34
Mutagenesis1991D → A: Increased ATPase activity and loss of helicase activity. Ref.18
Mutagenesis228 – 2303SAT → AAA: Decreased ATPase activity and loss of helicase activity. Ref.18
Sequence conflict2891Q → R in BAD96632. Ref.3

Secondary structure

......................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7A55167BF576FB6F

FASTA42848,991
        10         20         30         40         50         60 
MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI 

        70         80         90        100        110        120 
VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC 

       130        140        150        160        170        180 
HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA 

       190        200        210        220        230        240 
RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR 

       250        260        270        280        290        300 
KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC 

       310        320        330        340        350        360 
IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF 

       370        380        390        400        410        420 
NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI 


SSYIEQTR 

« Hide

Isoform 2 [UniParc].

Checksum: 5B25C9C18CA433A4
Show »

FASTA44350,679

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Chtop is a component of the dynamic TREX mRNA export complex."
Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B., Philipsen S., Wilson S.A.
EMBO J. 32:473-486(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI37201.
RefSeqNP_004631.1. NM_004640.6.
NP_542165.1. NM_080598.5.
UniGeneHs.254042.
Hs.730849.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5IX-ray1.90A259-428[»]
1T6NX-ray1.94A/B34-251[»]
1XTIX-ray1.95A44-428[»]
1XTJX-ray2.70A44-423[»]
1XTKX-ray2.40A45-428[»]
ProteinModelPortalQ13838.
SMRQ13838. Positions 46-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113649. 55 interactions.
IntActQ13838. 33 interactions.
MINTMINT-1032422.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ13838.

Polymorphism databases

DMDM2500529.

Proteomic databases

PaxDbQ13838.
PRIDEQ13838.

Protocols and materials databases

DNASU7919.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383508; 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]
GeneID7919.
KEGGhsa:7919.
UCSCuc003ntt.3. human. [Q13838-1]

Organism-specific databases

CTD7919.
GeneCardsGC06M031500.
GC06Mj31485.
GC06Mk31480.
GC06Ml31538.
GC06Mm31574.
GC06Mn31488.
GC06Mo31487.
HGNCHGNC:13917. DDX39B.
HPACAB034012.
MIM142560. gene.
neXtProtNX_Q13838.
PharmGKBPA25262.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOVERGENHBG107334.
InParanoidQ13838.
KOK12812.
PhylomeDBQ13838.
TreeFamTF300442.

Gene expression databases

ArrayExpressQ13838.
BgeeQ13838.
CleanExHS_BAT1.
GenevestigatorQ13838.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. 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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX39B. human.
EvolutionaryTraceQ13838.
GeneWikiBAT1.
GenomeRNAi7919.
NextBio30405.
PROQ13838.
SOURCESearch...

Entry information

Entry nameDX39B_HUMAN
AccessionPrimary (citable) accession number: Q13838
Secondary accession number(s): B0S8C0 expand/collapse secondary AC list , O43496, Q0EFA1, Q2L6F9, Q53GL9, Q5RJ64, Q5RJ66, Q5ST94, Q5STB4, Q5STB5, Q5STB7, Q5STB8, Q5STU4, Q5STU5, Q5STU6, Q5STU8, Q71V76
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM