Q13838 (DX39B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DDX39B
Synonyms:	BAT1, UAP56

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It 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. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and ALYREF/THOC4. Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.26 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 and ALYREF/THOC4. Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.26
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Homodimer, and heterodimer with DDX39A. Component of the THO complex, which is composed of THOC1, THOC2, THOC5, THOC6 and THOC7. Together with THOC3, ALYREF/THOC4 and DDX39B, THO forms the transcription/export (TREX) complex. Component of the spliceosome. Interacts directly with U2AF2. Interacts directly with ALYREF/THOC4 and is necessARy for ALYREF/THOC4 recruitment to spliced mRNA. Interacts with RBM8A, RNPS1 and SRRM1. Interacts with FYTTD1/UIF and THOC1. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with MX1. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.21 Ref.25 Ref.27
Subcellular location	Nucleus. Nucleus speckle. Cytoplasm. Note: Can translocate to the cytoplasm in the presence of MX1. Ref.1 Ref.9 Ref.10 Ref.15 Ref.25
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 process	Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA secondary structure unwinding Inferred from direct assay PubMed 18593880. Source: BHF-UCL intronless viral mRNA export from host nucleus Inferred from direct assay Ref.19. Source: UniProtKB spliceosomal complex assembly Inferred from direct assay PubMed 18593880. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from direct assay PubMed 18593880. Source: BHF-UCL transcription export complex Inferred from direct assay Ref.13Ref.14. Source: UniProtKB
Molecular_function	ATP 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 U4 snRNA binding Inferred from direct assay PubMed 18593880. Source: BHF-UCL U6 snRNA binding Inferred from direct assay PubMed 18593880. Source: BHF-UCL
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

Spliceosome RNA helicase DDX39B

PRO_0000055071

Regions

Domain

76 – 249

174

Helicase ATP-binding

Domain

261 – 422

162

Helicase C-terminal

Nucleotide binding

89 – 96

8

ATP

Motif

45 – 73

29

Q motif

Motif

196 – 199

4

DECD box

Amino acid modifications

Modified residue

36

1

N6-acetyllysine Ref.22

Modified residue

38

1

Phosphoserine Ref.23

Modified residue

172

1

Phosphothreonine Ref.23

Natural variations

Alternative sequence

114

1

V → VYLGRVLGRGFWLGLV in isoform 2.

VSP_026347

Experimental info

Mutagenesis

94 – 96

3

GKT → AAA: Loss of ATPase and helicase activity. Ref.18

Mutagenesis

95

1

K → A: Loss of ATPase and helicase activity. Ref.18

Mutagenesis

197

1

E → A: Loss of ATPase and helicase activity. Ref.18

Mutagenesis

198

1

C → A: No effect on ATPase activity. Ref.26

Mutagenesis

199

1

D → A: Increased ATPase activity and loss of helicase activity. Ref.18

Mutagenesis

228 – 230

3

SAT → AAA: Decreased ATPase activity and loss of helicase activity. Ref.18

Sequence conflict

289

1

Q → R in BAD96632. Ref.3

Secondary structure

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428

Helix Strand Turn

Details...

Helix

47 – 50

4

Helix

54 – 62

9

Helix

70 – 80

11

Beta strand

85 – 88

4

Helix

95 – 106

12

Beta strand

116 – 119

4

Helix

123 – 136

14

Turn

137 – 139

3

Beta strand

145 – 149

5

Helix

154 – 163

10

Beta strand

167 – 171

5

Helix

173 – 181

9

Beta strand

183 – 185

3

Beta strand

192 – 197

6

Helix

198 – 202

5

Helix

205 – 216

12

Beta strand

220 – 229

10

Turn

233 – 235

3

Helix

236 – 240

5

Beta strand

247 – 250

4

Beta strand

263 – 268

6

Helix

271 – 273

3

Helix

274 – 284

11

Beta strand

288 – 293

6

Helix

297 – 309

13

Beta strand

314 – 317

4

Beta strand

319 – 321

3

Helix

323 – 334

12

Beta strand

335 – 337

3

Beta strand

339 – 345

7

Helix

353 – 355

3

Beta strand

357 – 363

7

Helix

368 – 378

11

Helix

380 – 382

3

Beta strand

386 – 391

6

Helix

394 – 407

14

Beta strand

411 – 413

3

Beta strand

417 – 419

3

Helix

420 – 422

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7A55167BF576FB6F	FASTA	428	48,991
	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
	Isoform 2 [UniParc]. Checksum: 5B25C9C18CA433A4	FASTA	443	50,679
	10 20 30 40 50 60 MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI 70 80 90 100 110 120 VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVYLGRVL 130 140 150 160 170 180 GRGFWLGLVS VLVMCHTREL AFQISKEYER FSKYMPNVKV AVFFGGLSIK KDEEVLKKNC 190 200 210 220 230 240 PHIVVGTPGR ILALARNKSL NLKHIKHFIL DECDKMLEQL DMRRDVQEIF RMTPHEKQVM 250 260 270 280 290 300 MFSATLSKEI RPVCRKFMQD PMEIFVDDET KLTLHGLQQY YVKLKDNEKN RKLFDLLDVL 310 320 330 340 350 360 EFNQVVIFVK SVQRCIALAQ LLVEQNFPAI AIHRGMPQEE RLSRYQQFKD FQRRILVATN 370 380 390 400 410 420 LFGRGMDIER VNIAFNYDMP EDSDTYLHRV ARAGRFGTKG LAITFVSDEN DAKILNDVQD 430 440 RFEVNISELP DEIDISSYIE QTR

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, 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, 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]	"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.
[20]	"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.
[21]	"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.
[22]	"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, MASS SPECTROMETRY.
[23]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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].
[25]	"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.
[26]	"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.
[27]	"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.

IPI

IPI00641829.
IPI00848161.

PIR

I37201.

RefSeq

NP_004631.1. NM_004640.6.
NP_542165.1. NM_080598.5.

UniGene

Hs.254042.
Hs.730849.

3D structure databases

PDBe
RCSB PDB
PDBj

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	44-428	[»]
1XTJ	X-ray	2.70	A	44-423	[»]
1XTK	X-ray	2.40	A	45-428	[»]

ProteinModelPortal

Q13838.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13838. 26 interactions.

MINT

MINT-1032422.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q13838.

Polymorphism databases

DMDM

2500529.

Proteomic databases

PaxDb

Q13838.

PRIDE

Q13838.

Protocols and materials databases

DNASU

7919.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000383508; ENSP00000373000; ENSG00000215425.
ENST00000396172; ENSP00000379475; ENSG00000198563.
ENST00000400295; ENSP00000383151; ENSG00000215425.
ENST00000400296; ENSP00000383152; ENSG00000215425.
ENST00000412106; ENSP00000393712; ENSG00000225073.
ENST00000412330; ENSP00000398775; ENSG00000225859.
ENST00000413678; ENSP00000391463; ENSG00000229496.
ENST00000414440; ENSP00000411853; ENSG00000229496.
ENST00000415689; ENSP00000390999; ENSG00000225073.
ENST00000416863; ENSP00000407419; ENSG00000229496.
ENST00000430784; ENSP00000399030; ENSG00000235439.
ENST00000431360; ENSP00000404695; ENSG00000235439.
ENST00000441425; ENSP00000388880; ENSG00000230624.
ENST00000445218; ENSP00000411136; ENSG00000225859.
ENST00000448296; ENSP00000405560; ENSG00000225859.
ENST00000453138; ENSP00000387994; ENSG00000230624.
ENST00000456476; ENSP00000400326; ENSG00000225073.
ENST00000456666; ENSP00000394160; ENSG00000230624.
ENST00000458640; ENSP00000416269; ENSG00000198563.

GeneID

7919.

KEGG

hsa:7919.

UCSC

uc003ntt.3. human.

Organism-specific databases

CTD

7919.

GeneCards

GC06M031500.

HGNC

HGNC:13917. DDX39B.

HPA

CAB034012.

MIM

142560. gene.

neXtProt

NX_Q13838.

PharmGKB

PA25262.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOVERGEN

HBG107334.

InParanoid

Q13838.

KO

K12812.

OrthoDB

EOG4XSKPX.

PhylomeDB

Q13838.

Gene expression databases

ArrayExpress

Q13838.

Bgee

Q13838.

CleanEx

HS_BAT1.

Genevestigator

Q13838.

GermOnline

ENSG00000198563. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDX39B. human.

EvolutionaryTrace

Q13838.

GenomeRNAi

7919.

NextBio

30405.

SOURCE

Search...

Entry information

Entry name

DX39B_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.