GenomeNet

Database: UniProt
Entry: Q8VDW0
LinkDB: Q8VDW0
Original site: Q8VDW0 
ID   DX39A_MOUSE             Reviewed;         427 AA.
AC   Q8VDW0; Q3UJV4; Q8C2C2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-OCT-2019, entry version 146.
DE   RecName: Full=ATP-dependent RNA helicase DDX39A;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 39;
GN   Name=Ddx39a; Synonyms=Ddx39;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in pre-mRNA splicing. Required for the export
CC       of mRNA out of the nucleus (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Binds ALYREF/THOC4 and DDX39B/BAT1 (By similarity).
CC       Interacts with SARNP (By similarity). Interacts with MX1 (By
CC       similarity). Interacts with MCM3AP (By similarity).
CC       {ECO:0000250|UniProtKB:O00148}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Can translocate to the cytoplasm in the
CC       presence of MX1. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VDW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDW0-2; Sequence=VSP_013064;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily. {ECO:0000305}.
DR   EMBL; AK088894; BAC40637.1; -; mRNA.
DR   EMBL; AK145927; BAE26758.1; -; mRNA.
DR   EMBL; AK146294; BAE27051.1; -; mRNA.
DR   EMBL; AK150997; BAE30021.1; -; mRNA.
DR   EMBL; AK162752; BAE37049.1; -; mRNA.
DR   EMBL; AK168079; BAE40052.1; -; mRNA.
DR   EMBL; BC020134; AAH20134.1; -; mRNA.
DR   CCDS; CCDS22460.1; -. [Q8VDW0-1]
DR   RefSeq; NP_932099.2; NM_197982.3. [Q8VDW0-1]
DR   RefSeq; XP_006531395.1; XM_006531332.3.
DR   SMR; Q8VDW0; -.
DR   BioGrid; 212781; 4.
DR   IntAct; Q8VDW0; 1.
DR   MINT; Q8VDW0; -.
DR   STRING; 10090.ENSMUSP00000019576; -.
DR   iPTMnet; Q8VDW0; -.
DR   PhosphoSitePlus; Q8VDW0; -.
DR   SwissPalm; Q8VDW0; -.
DR   EPD; Q8VDW0; -.
DR   jPOST; Q8VDW0; -.
DR   PaxDb; Q8VDW0; -.
DR   PeptideAtlas; Q8VDW0; -.
DR   PRIDE; Q8VDW0; -.
DR   TopDownProteomics; Q8VDW0-1; -. [Q8VDW0-1]
DR   Ensembl; ENSMUST00000019576; ENSMUSP00000019576; ENSMUSG00000005481. [Q8VDW0-1]
DR   Ensembl; ENSMUST00000109810; ENSMUSP00000105435; ENSMUSG00000005481. [Q8VDW0-1]
DR   Ensembl; ENSMUST00000172396; ENSMUSP00000132222; ENSMUSG00000005481. [Q8VDW0-1]
DR   Ensembl; ENSMUST00000212949; ENSMUSP00000148329; ENSMUSG00000005481. [Q8VDW0-1]
DR   GeneID; 68278; -.
DR   KEGG; mmu:68278; -.
DR   UCSC; uc009mla.2; mouse. [Q8VDW0-1]
DR   CTD; 68278; -.
DR   MGI; MGI:1915528; Ddx39.
DR   eggNOG; KOG0329; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000154912; -.
DR   InParanoid; Q8VDW0; -.
DR   KO; K13182; -.
DR   OMA; CGYQKMT; -.
DR   OrthoDB; 779000at2759; -.
DR   PhylomeDB; Q8VDW0; -.
DR   TreeFam; TF300442; -.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR   ChiTaRS; Ddx39; mouse.
DR   PRO; PR:Q8VDW0; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000005481; Expressed in 280 organ(s), highest expression level in metanephric renal vesicle.
DR   ExpressionAtlas; Q8VDW0; baseline and differential.
DR   Genevisible; Q8VDW0; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000346; C:transcription export complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW   Cytoplasm; Helicase; Hydrolase; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O00148}.
FT   CHAIN         2    427       ATP-dependent RNA helicase DDX39A.
FT                                /FTId=PRO_0000055068.
FT   DOMAIN       75    248       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      260    421       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      88     95       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        44     72       Q motif.
FT   MOTIF       195    198       DECD box.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   MOD_RES      35     35       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   MOD_RES      37     37       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   MOD_RES     171    171       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   MOD_RES     426    426       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK     31     31       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK     35     35       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK    154    154       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK    162    162       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK    240    240       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   CROSSLNK    255    255       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O00148}.
FT   VAR_SEQ       1    245       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_013064.
SQ   SEQUENCE   427 AA;  49067 MW;  4A94699142FCABA8 CRC64;
     MAEQDVENEL LDYDEDEEPQ APQESTPAPP KKDVKGSYVS IHSSGFRDFL LKPELLRAIV
     DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL ATLQQIEPVN GQVSVLVMCH
     TRELAFQISK EYERFSKYMP SVKVSVFFGG LSIKKDEDVL KKNCPHVVVG TPGRILALVR
     SRSLNLRNVK HFVLDECDKM LEQLDMRRDV QEIFRLTPHE KQCMMFSATL SKEIRPVCRK
     FMQDPMEVFV DDETKLTLHG LQQYYVKLKD SEKNRKLFDL LDVLEFNQVV IFVKSVQRCM
     ALAQLLVEQN FPAIAIHRGM AQEERLSRYQ QFKDFQRRIL VATNLFGRGM DIERVNIVFN
     YDMPEDSDTY LHRVARAGRF GTKGLAVTFV SDENDAKILN DVQDRFEVNV AELPEEIDIS
     TYIEQSR
//
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