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Q9UMR2 (DD19B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
ATP-dependent RNA helicase DDX19B

EC=3.6.4.13
Alternative name(s):
DEAD box RNA helicase DEAD5
DEAD box protein 19B
Gene names
Name:DDX19B
Synonyms:DBP5, DDX19, TDBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with NUP214 or RNA in a mutually exclusive manner.

Subcellular location

Cytoplasm. Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Nuclear pore complex cytoplasmic fibrils.

Domain

The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis. Ref.10

Sequence similarities

Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UMR2-1)

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: Q9UMR2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-130: Missing.
Isoform 3 (identifier: Q9UMR2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-109: Missing.
Isoform 4 (identifier: Q9UMR2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-19: ATDSWALAVDEQEAAAES → MAGAAGRVQDRALRRFPITLPVGD
     100-130: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 479478ATP-dependent RNA helicase DDX19B
PRO_0000055022

Regions

Domain125 – 295171Helicase ATP-binding
Domain306 – 474169Helicase C-terminal
Nucleotide binding138 – 1458ATP
Region2 – 300299N-terminal lobe
Region55 – 6814N-terminal helix
Region301 – 479179C-terminal lobe
Motif92 – 12029Q motif
Motif242 – 2454DEAD box

Sites

Binding site1191ATP
Binding site4291ATP
Binding site4321ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.9

Natural variations

Alternative sequence2 – 109108Missing in isoform 3.
VSP_041347
Alternative sequence2 – 1918ATDSW…AAAES → MAGAAGRVQDRALRRFPITL PVGD in isoform 4.
VSP_044727
Alternative sequence100 – 13031Missing in isoform 2 and isoform 4.
VSP_015239
Natural variant1491V → L.
Corresponds to variant rs34607244 [ dbSNP | Ensembl ].
VAR_052160

Experimental info

Mutagenesis2231D → R: Impairs interaction with NUP214 and RNA. Ref.11
Mutagenesis2431E → Q: Loss of activity. Ref.1
Mutagenesis2581I → A: Impairs interaction with NUP214. Ref.11
Mutagenesis2591R → D: Impairs interaction with NUP214. Ref.11
Mutagenesis2621R → A: Impairs interaction with NUP214. Ref.11
Sequence conflict1281A → V in CAG33496. Ref.4
Sequence conflict2011N → Y in BAG63488. Ref.5
Sequence conflict3311I → T in CAG33496. Ref.4
Sequence conflict3671M → V in CAG38540. Ref.4

Secondary structure

............................................................................ 479
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 8F6F93B12B7E9871

FASTA47953,927
        10         20         30         40         50         60 
MATDSWALAV DEQEAAAESL SNLHLKEEKI KPDTNGAVVK TNANAEKTDE EEKEDRAAQS 

        70         80         90        100        110        120 
LLNKLIRSNL VDNTNQVEVL QRDPNSPLYS VKSFEELRLK PQLLQGVYAM GFNRPSKIQE 

       130        140        150        160        170        180 
NALPLMLAEP PQNLIAQSQS GTGKTAAFVL AMLSQVEPAN KYPQCLCLSP TYELALQTGK 

       190        200        210        220        230        240 
VIEQMGKFYP ELKLAYAVRG NKLERGQKIS EQIVIGTPGT VLDWCSKLKF IDPKKIKVFV 

       250        260        270        280        290        300 
LDEADVMIAT QGHQDQSIRI QRMLPRNCQM LLFSATFEDS VWKFAQKVVP DPNVIKLKRE 

       310        320        330        340        350        360 
EETLDTIKQY YVLCSSRDEK FQALCNLYGA ITIAQAMIFC HTRKTASWLA AELSKEGHQV 

       370        380        390        400        410        420 
ALLSGEMMVE QRAAVIERFR EGKEKVLVTT NVCARGIDVE QVSVVINFDL PVDKDGNPDN 

       430        440        450        460        470 
ETYLHRIGRT GRFGKRGLAV NMVDSKHSMN ILNRIQEHFN KKIERLDTDD LDEIEKIAN 

« Hide

Isoform 2 [UniParc].

Checksum: 178321CBF4CA276A
Show »

FASTA44850,490
Isoform 3 [UniParc].

Checksum: 0BA1AD0FFF915AED
Show »

FASTA37141,911
Isoform 4 [UniParc].

Checksum: A1A34DAB7C730309
Show »

FASTA45451,194

References

« Hide 'large scale' references
[1]"Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p."
Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.
EMBO J. 18:4332-4347(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, MUTAGENESIS OF GLU-243.
[2]"Identification and characterization of a gene coding a novel isoform of DEAD-box protein."
Yin L., Li J., Zhu H., Lin M., Cheng L., Wang Y., Zhou Z., Sha J.
Reprod. Fertil. Dev. 14:185-189(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Testis.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
Tissue: Mammary gland, Stomach and Testis.
[6]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORMS 1 AND 3).
Tissue: Ovary and Skin.
[9]"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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"The DEXD/H-box RNA helicase DDX19 is regulated by an alpha-helical switch."
Collins R., Karlberg T., Lehtio L., Schutz P., van den Berg S., Dahlgren L.G., Hammarstrom M., Weigelt J., Schuler H.
J. Biol. Chem. 284:10296-10300(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-475 ALONE AND IN COMPLEX WITH RNA, REGULATION BY N-TERMINAL HELIX DOMAIN.
[11]"The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner."
von Moeller H., Basquin C., Conti E.
Nat. Struct. Mol. Biol. 16:247-254(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-479 IN COMPLEX WITH NUP214 AND ATP ANALOG, ATP-BINDING SITES, MUTAGENESIS OF ASP-223; ILE-258; ARG-259 AND ARG-262.
[12]"Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19."
Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G., Hoelz A.
Proc. Natl. Acad. Sci. U.S.A. 106:3089-3094(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-300 IN COMPLEX WITH NUP214 AND ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ237946 mRNA. Translation: CAB52189.1.
AF353720 mRNA. Translation: AAK40102.1.
AL136639 mRNA. Translation: CAB66574.1.
CR457215 mRNA. Translation: CAG33496.1.
CR533509 mRNA. Translation: CAG38540.1.
AK027378 mRNA. Translation: BAG51311.1.
AK301938 mRNA. Translation: BAG63358.1.
AK302107 mRNA. Translation: BAG63488.1.
AK316346 mRNA. Translation: BAH14717.1.
AC012184 Genomic DNA. No translation available.
CH471241 Genomic DNA. Translation: EAW51827.1.
CH471241 Genomic DNA. Translation: EAW51831.1.
CH471241 Genomic DNA. Translation: EAW51832.1.
CH471241 Genomic DNA. Translation: EAW51834.1.
BC003626 mRNA. Translation: AAH03626.1.
BC010008 mRNA. Translation: AAH10008.1.
RefSeqNP_001014449.1. NM_001014449.2.
NP_001014451.1. NM_001014451.2.
NP_001244101.1. NM_001257172.1.
NP_001244102.1. NM_001257173.1.
NP_001244103.1. NM_001257174.1.
NP_009173.1. NM_007242.5.
UniGeneHs.221761.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EWSX-ray2.70A/B54-475[»]
3FHCX-ray2.80B68-302[»]
3FHTX-ray2.20A/B68-479[»]
3FMOX-ray2.51B1-300[»]
3FMPX-ray3.19B/D1-479[»]
3G0HX-ray2.70A54-475[»]
ProteinModelPortalQ9UMR2.
SMRQ9UMR2. Positions 60-467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116426. 14 interactions.
DIPDIP-48486N.
IntActQ9UMR2. 13 interactions.
MINTMINT-4831823.
STRING9606.ENSP00000288071.

PTM databases

PhosphoSiteQ9UMR2.

Polymorphism databases

DMDM10719979.

Proteomic databases

PaxDbQ9UMR2.
PRIDEQ9UMR2.

Protocols and materials databases

DNASU11269.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288071; ENSP00000288071; ENSG00000157349. [Q9UMR2-1]
ENST00000355992; ENSP00000348271; ENSG00000157349. [Q9UMR2-2]
ENST00000393657; ENSP00000377267; ENSG00000157349. [Q9UMR2-3]
ENST00000451014; ENSP00000392639; ENSG00000157349. [Q9UMR2-4]
ENST00000563392; ENSP00000456574; ENSG00000157349. [Q9UMR2-3]
ENST00000568625; ENSP00000456757; ENSG00000157349. [Q9UMR2-3]
GeneID11269.
KEGGhsa:11269.
UCSCuc002eyo.4. human. [Q9UMR2-1]
uc002eyp.4. human. [Q9UMR2-2]

Organism-specific databases

CTD11269.
GeneCardsGC16P070328.
HGNCHGNC:2742. DDX19B.
HPACAB037229.
CAB037284.
HPA046380.
MIM605812. gene.
neXtProtNX_Q9UMR2.
PharmGKBPA27208.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG107989.
InParanoidQ9UMR2.
PhylomeDBQ9UMR2.
TreeFamTF314957.

Gene expression databases

ArrayExpressQ9UMR2.
BgeeQ9UMR2.
CleanExHS_DDX19B.
GenevestigatorQ9UMR2.

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

ChiTaRSDDX19B. human.
EvolutionaryTraceQ9UMR2.
GeneWikiDDX19B.
GenomeRNAi11269.
NextBio42879.
PROQ9UMR2.
SOURCESearch...

Entry information

Entry nameDD19B_HUMAN
AccessionPrimary (citable) accession number: Q9UMR2
Secondary accession number(s): B3KNE9 expand/collapse secondary AC list , B4DXS6, E7EMK4, Q6FIB7, Q6IAE0, Q96KE7, Q9H0U0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 133 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM