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Protein

ATP-dependent RNA helicase DDX39A

Gene

Ddx39a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 958ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX39A (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 39
Gene namesi
Name:Ddx39a
Synonyms:Ddx39
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915528. Ddx39.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Can translocate to the cytoplasm in the presence of MX1.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 427426ATP-dependent RNA helicase DDX39APRO_0000055068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei171 – 1711PhosphothreonineBy similarity
Modified residuei426 – 4261PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VDW0.
MaxQBiQ8VDW0.
PaxDbiQ8VDW0.
PRIDEiQ8VDW0.
TopDownProteomicsiQ8VDW0-1. [Q8VDW0-1]

PTM databases

iPTMnetiQ8VDW0.
PhosphoSiteiQ8VDW0.
SwissPalmiQ8VDW0.

Expressioni

Gene expression databases

BgeeiQ8VDW0.
CleanExiMM_DDX39.
ExpressionAtlasiQ8VDW0. baseline and differential.
GenevisibleiQ8VDW0. MM.

Interactioni

Subunit structurei

Binds ALYREF/THOC4 and DDX39B/BAT1. Interacts with SARNP (By similarity). Interacts with MX1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212781. 1 interaction.
IntActiQ8VDW0. 1 interaction.
MINTiMINT-1868069.
STRINGi10090.ENSMUSP00000019576.

Structurei

3D structure databases

ProteinModelPortaliQ8VDW0.
SMRiQ8VDW0. Positions 45-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 248174Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini260 – 421162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi44 – 7229Q motifAdd
BLAST
Motifi195 – 1984DECD box

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0329. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00830000128348.
HOVERGENiHBG107334.
InParanoidiQ8VDW0.
KOiK13182.
OMAiRLIAPVH.
OrthoDBiEOG7W154N.
PhylomeDBiQ8VDW0.
TreeFamiTF300442.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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. AlignAdd to basket

Isoform 1 (identifier: Q8VDW0-1) [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

        10         20         30         40         50
MAEQDVENEL LDYDEDEEPQ APQESTPAPP KKDVKGSYVS IHSSGFRDFL
60 70 80 90 100
LKPELLRAIV DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL
110 120 130 140 150
ATLQQIEPVN GQVSVLVMCH TRELAFQISK EYERFSKYMP SVKVSVFFGG
160 170 180 190 200
LSIKKDEDVL KKNCPHVVVG TPGRILALVR SRSLNLRNVK HFVLDECDKM
210 220 230 240 250
LEQLDMRRDV QEIFRLTPHE KQCMMFSATL SKEIRPVCRK FMQDPMEVFV
260 270 280 290 300
DDETKLTLHG LQQYYVKLKD SEKNRKLFDL LDVLEFNQVV IFVKSVQRCM
310 320 330 340 350
ALAQLLVEQN FPAIAIHRGM AQEERLSRYQ QFKDFQRRIL VATNLFGRGM
360 370 380 390 400
DIERVNIVFN YDMPEDSDTY LHRVARAGRF GTKGLAVTFV SDENDAKILN
410 420
DVQDRFEVNV AELPEEIDIS TYIEQSR
Length:427
Mass (Da):49,067
Last modified:March 1, 2002 - v1
Checksum:i4A94699142FCABA8
GO
Isoform 2 (identifier: Q8VDW0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: Missing.

Note: No experimental confirmation available.
Show »
Length:182
Mass (Da):21,244
Checksum:i8720C875760F3E5F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 245245Missing in isoform 2. 1 PublicationVSP_013064Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088894 mRNA. Translation: BAC40637.1.
AK145927 mRNA. Translation: BAE26758.1.
AK146294 mRNA. Translation: BAE27051.1.
AK150997 mRNA. Translation: BAE30021.1.
AK162752 mRNA. Translation: BAE37049.1.
AK168079 mRNA. Translation: BAE40052.1.
BC020134 mRNA. Translation: AAH20134.1.
CCDSiCCDS22460.1. [Q8VDW0-1]
RefSeqiNP_932099.2. NM_197982.3. [Q8VDW0-1]
XP_006531395.1. XM_006531332.2. [Q8VDW0-1]
UniGeneiMm.28222.

Genome annotation databases

EnsembliENSMUST00000019576; ENSMUSP00000019576; ENSMUSG00000005481. [Q8VDW0-1]
ENSMUST00000109810; ENSMUSP00000105435; ENSMUSG00000005481. [Q8VDW0-1]
ENSMUST00000172396; ENSMUSP00000132222; ENSMUSG00000005481. [Q8VDW0-1]
GeneIDi68278.
KEGGimmu:68278.
UCSCiuc009mla.2. mouse. [Q8VDW0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088894 mRNA. Translation: BAC40637.1.
AK145927 mRNA. Translation: BAE26758.1.
AK146294 mRNA. Translation: BAE27051.1.
AK150997 mRNA. Translation: BAE30021.1.
AK162752 mRNA. Translation: BAE37049.1.
AK168079 mRNA. Translation: BAE40052.1.
BC020134 mRNA. Translation: AAH20134.1.
CCDSiCCDS22460.1. [Q8VDW0-1]
RefSeqiNP_932099.2. NM_197982.3. [Q8VDW0-1]
XP_006531395.1. XM_006531332.2. [Q8VDW0-1]
UniGeneiMm.28222.

3D structure databases

ProteinModelPortaliQ8VDW0.
SMRiQ8VDW0. Positions 45-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212781. 1 interaction.
IntActiQ8VDW0. 1 interaction.
MINTiMINT-1868069.
STRINGi10090.ENSMUSP00000019576.

PTM databases

iPTMnetiQ8VDW0.
PhosphoSiteiQ8VDW0.
SwissPalmiQ8VDW0.

Proteomic databases

EPDiQ8VDW0.
MaxQBiQ8VDW0.
PaxDbiQ8VDW0.
PRIDEiQ8VDW0.
TopDownProteomicsiQ8VDW0-1. [Q8VDW0-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019576; ENSMUSP00000019576; ENSMUSG00000005481. [Q8VDW0-1]
ENSMUST00000109810; ENSMUSP00000105435; ENSMUSG00000005481. [Q8VDW0-1]
ENSMUST00000172396; ENSMUSP00000132222; ENSMUSG00000005481. [Q8VDW0-1]
GeneIDi68278.
KEGGimmu:68278.
UCSCiuc009mla.2. mouse. [Q8VDW0-1]

Organism-specific databases

CTDi68278.
MGIiMGI:1915528. Ddx39.

Phylogenomic databases

eggNOGiKOG0329. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00830000128348.
HOVERGENiHBG107334.
InParanoidiQ8VDW0.
KOiK13182.
OMAiRLIAPVH.
OrthoDBiEOG7W154N.
PhylomeDBiQ8VDW0.
TreeFamiTF300442.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72187. mRNA 3'-end processing.

Miscellaneous databases

PROiQ8VDW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDW0.
CleanExiMM_DDX39.
ExpressionAtlasiQ8VDW0. baseline and differential.
GenevisibleiQ8VDW0. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: BALB/cJ, C57BL/6J and NOD.
    Tissue: Bone marrow, Liver and Thymus.
  2. "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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Spleen and Testis.

Entry informationi

Entry nameiDX39A_MOUSE
AccessioniPrimary (citable) accession number: Q8VDW0
Secondary accession number(s): Q3UJV4, Q8C2C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.