DX39A_HUMAN
ID DX39A_HUMAN Reviewed; 427 AA.
AC O00148; B1Q2N1; Q8N5M0; Q9BVP6; Q9H5W0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=ATP-dependent RNA helicase DDX39A;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 39;
DE AltName: Full=Nuclear RNA helicase URH49;
GN Name=DDX39A; Synonyms=DDX39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Jelinek W.R.;
RT "Human nuclear RNA helicase.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, RNA-BINDING, AND
RP ALTERNATIVE SPLICING.
RX PubMed=17548965; DOI=10.4161/cbt.6.6.4192;
RA Sugiura T., Nagano Y., Noguchi Y.;
RT "DDX39, upregulated in lung squamous cell cancer, displays RNA helicase
RT activities and promotes cancer cell growth.";
RL Cancer Biol. Ther. 6:957-964(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH DDX39B.
RX PubMed=14667819; DOI=10.1016/s0888-7543(03)00235-0;
RA Lehner B., Semple J.I., Brown S.E., Counsell D., Campbell R.D.,
RA Sanderson C.M.;
RT "Analysis of a high-throughput yeast two-hybrid system and its use to
RT predict the function of intracellular proteins encoded within the human MHC
RT class III region.";
RL Genomics 83:153-167(2004).
RN [8]
RP FUNCTION, INTERACTION WITH ALYREF/THOC4, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15047853; DOI=10.1093/nar/gkh347;
RA Pryor A., Tung L., Yang Z., Kapadia F., Chang T.-H., Johnson L.F.;
RT "Growth-regulated expression and G0-specific turnover of the mRNA that
RT encodes URH49, a mammalian DExH/D box protein that is highly related to the
RT mRNA export protein UAP56.";
RL Nucleic Acids Res. 32:1857-1865(2004).
RN [9]
RP INTERACTION WITH HHV-5 PROTEIN UL69.
RX PubMed=16478985; DOI=10.1128/mcb.26.5.1631-1643.2006;
RA Lischka P., Toth Z., Thomas M., Mueller R., Stamminger T.;
RT "The UL69 transactivator protein of human cytomegalovirus interacts with
RT DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation of
RT unspliced RNA.";
RL Mol. Cell. Biol. 26:1631-1643(2006).
RN [10]
RP INTERACTION WITH SARNP.
RX PubMed=17196963; DOI=10.1016/j.yexcr.2006.11.014;
RA Sugiura T., Sakurai K., Nagano Y.;
RT "Intracellular characterization of DDX39, a novel growth-associated RNA
RT helicase.";
RL Exp. Cell Res. 313:782-790(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-171 AND SER-426, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MX1.
RX PubMed=21859714; DOI=10.1074/jbc.m111.251843;
RA Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.;
RT "Interferon-induced antiviral protein MxA interacts with the cellular RNA
RT helicases UAP56 and URH49.";
RL J. Biol. Chem. 286:34743-34751(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND THR-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP INTERACTION WITH MCM3AP.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-35; LYS-154; LYS-162;
RP LYS-240 AND LYS-255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: [Isoform 1]: Involved in pre-mRNA splicing. Required for the
CC export of mRNA out of the nucleus. {ECO:0000269|PubMed:15047853,
CC ECO:0000269|PubMed:17548965}.
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. Interacts with SARNP.
CC Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with
CC MX1. Interacts with MCM3AP isoform GANP (PubMed:23652018).
CC {ECO:0000269|PubMed:14667819, ECO:0000269|PubMed:15047853,
CC ECO:0000269|PubMed:16478985, ECO:0000269|PubMed:17196963,
CC ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:23652018}.
CC -!- INTERACTION:
CC O00148; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-348253, EBI-11984237;
CC O00148; O00148: DDX39A; NbExp=4; IntAct=EBI-348253, EBI-348253;
CC O00148; Q13838: DDX39B; NbExp=4; IntAct=EBI-348253, EBI-348622;
CC O00148; P04792: HSPB1; NbExp=3; IntAct=EBI-348253, EBI-352682;
CC O00148; P42858: HTT; NbExp=3; IntAct=EBI-348253, EBI-466029;
CC O00148; P78317: RNF4; NbExp=3; IntAct=EBI-348253, EBI-2340927;
CC O00148; P82979: SARNP; NbExp=4; IntAct=EBI-348253, EBI-347495;
CC O00148; P21673: SAT1; NbExp=3; IntAct=EBI-348253, EBI-711613;
CC O00148; P54274: TERF1; NbExp=2; IntAct=EBI-348253, EBI-710997;
CC O00148; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-348253, EBI-10180829;
CC O00148; O76024: WFS1; NbExp=3; IntAct=EBI-348253, EBI-720609;
CC O00148; H0YHG0; NbExp=3; IntAct=EBI-348253, EBI-6190012;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21859714}. Cytoplasm
CC {ECO:0000269|PubMed:21859714}. Note=Can translocate to the cytoplasm in
CC the presence of MX1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=L;
CC IsoId=O00148-1; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=O00148-2; Sequence=VSP_046559, VSP_046560;
CC Name=3; Synonyms=SS;
CC IsoId=O00148-3; Sequence=VSP_057426, VSP_057427;
CC -!- TISSUE SPECIFICITY: Detected in testis, and at lower levels in brain,
CC kidney, lung, thymus, spleen and salivary gland.
CC {ECO:0000269|PubMed:15047853}.
CC -!- INDUCTION: Up-regulated in proliferating cells. Present at low levels
CC in quiescent cells. {ECO:0000269|PubMed:15047853}.
CC -!- MISCELLANEOUS: [Isoform 2]: Probably devoid of RNA helicase activity.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Probably devoid of RNA helicase activity.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15509.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U90426; AAB50231.1; -; mRNA.
DR EMBL; AB254849; BAG16272.1; -; mRNA.
DR EMBL; AK026614; BAB15509.1; ALT_INIT; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84417.1; -; Genomic_DNA.
DR EMBL; BC001009; AAH01009.1; -; mRNA.
DR EMBL; BC032128; AAH32128.1; -; mRNA.
DR CCDS; CCDS12308.1; -. [O00148-1]
DR RefSeq; NP_005795.2; NM_005804.3. [O00148-1]
DR RefSeq; XP_011525922.1; XM_011527620.1. [O00148-1]
DR AlphaFoldDB; O00148; -.
DR SMR; O00148; -.
DR BioGRID; 115507; 1066.
DR CORUM; O00148; -.
DR IntAct; O00148; 80.
DR MINT; O00148; -.
DR STRING; 9606.ENSP00000242776; -.
DR BindingDB; O00148; -.
DR ChEMBL; CHEMBL4105795; -.
DR GlyGen; O00148; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00148; -.
DR PhosphoSitePlus; O00148; -.
DR SwissPalm; O00148; -.
DR BioMuta; DDX39A; -.
DR EPD; O00148; -.
DR jPOST; O00148; -.
DR MassIVE; O00148; -.
DR MaxQB; O00148; -.
DR PaxDb; O00148; -.
DR PeptideAtlas; O00148; -.
DR PRIDE; O00148; -.
DR ProteomicsDB; 3400; -.
DR ProteomicsDB; 47735; -. [O00148-1]
DR ProteomicsDB; 72073; -.
DR Antibodypedia; 13684; 148 antibodies from 26 providers.
DR DNASU; 10212; -.
DR Ensembl; ENST00000242776.9; ENSP00000242776.3; ENSG00000123136.15. [O00148-1]
DR Ensembl; ENST00000324340.13; ENSP00000322749.8; ENSG00000123136.15. [O00148-2]
DR Ensembl; ENST00000454233.6; ENSP00000392929.2; ENSG00000123136.15. [O00148-3]
DR Ensembl; ENST00000588692.5; ENSP00000467862.1; ENSG00000123136.15. [O00148-3]
DR GeneID; 10212; -.
DR KEGG; hsa:10212; -.
DR MANE-Select; ENST00000242776.9; ENSP00000242776.3; NM_005804.4; NP_005795.2.
DR UCSC; uc002myo.4; human. [O00148-1]
DR UCSC; uc010dzm.2; human.
DR CTD; 10212; -.
DR DisGeNET; 10212; -.
DR GeneCards; DDX39A; -.
DR HGNC; HGNC:17821; DDX39A.
DR HPA; ENSG00000123136; Tissue enhanced (testis).
DR neXtProt; NX_O00148; -.
DR OpenTargets; ENSG00000123136; -.
DR PharmGKB; PA27226; -.
DR VEuPathDB; HostDB:ENSG00000123136; -.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000154912; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; O00148; -.
DR OMA; VCKKFMT; -.
DR OrthoDB; 779000at2759; -.
DR PhylomeDB; O00148; -.
DR TreeFam; TF300442; -.
DR PathwayCommons; O00148; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; O00148; -.
DR BioGRID-ORCS; 10212; 43 hits in 1080 CRISPR screens.
DR ChiTaRS; DDX39A; human.
DR GeneWiki; DDX39; -.
DR GenomeRNAi; 10212; -.
DR Pharos; O00148; Tbio.
DR PRO; PR:O00148; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00148; protein.
DR Bgee; ENSG00000123136; Expressed in left testis and 193 other tissues.
DR ExpressionAtlas; O00148; baseline and differential.
DR Genevisible; O00148; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IGI:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
DR Gene3D; 3.40.50.300; -; 2.
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; Cytoplasm; Helicase;
KW Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT CHAIN 2..427
FT /note="ATP-dependent RNA helicase DDX39A"
FT /id="PRO_0000055067"
FT DOMAIN 75..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 260..421
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..72
FT /note="Q motif"
FT MOTIF 195..198
FT /note="DECD box"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 162
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 245..267
FT /note="PMEVFVDDETKLTLHGLQQYYVK -> VLWEVSHKGVAHWKVLGRRDAQR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17548965"
FT /id="VSP_057426"
FT VAR_SEQ 268..427
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17548965"
FT /id="VSP_057427"
FT VAR_SEQ 289..322
FT /note="VIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQ -> PVTLSAVQGFPAAD
FT PGGHQSVWPGDGHRASQHRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046559"
FT VAR_SEQ 323..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046560"
FT VARIANT 142
FT /note="V -> I (in dbSNP:rs36127505)"
FT /id="VAR_052166"
FT CONFLICT 38
FT /note="Y -> H (in Ref. 3; BAB15509)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="F -> L (in Ref. 1; AAB50231)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="L -> M (in Ref. 1; AAB50231)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="A -> G (in Ref. 1; AAB50231)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="D -> H (in Ref. 1; AAB50231)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="F -> C (in Ref. 1; AAB50231)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 49130 MW; 38D02D4234995574 CRC64;
MAEQDVENDL LDYDEEEEPQ APQESTPAPP KKDIKGSYVS IHSSGFRDFL LKPELLRAIV
DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL ATLQQIEPVN GQVTVLVMCH
TRELAFQISK EYERFSKYMP SVKVSVFFGG LSIKKDEEVL KKNCPHVVVG TPGRILALVR
NRSFSLKNVK HFVLDECDKM LEQLDMRRDV QEIFRLTPHE KQCMMFSATL SKDIRPVCRK
FMQDPMEVFV DDETKLTLHG LQQYYVKLKD SEKNRKLFDL LDVLEFNQVI IFVKSVQRCM
ALAQLLVEQN FPAIAIHRGM AQEERLSRYQ QFKDFQRRIL VATNLFGRGM DIERVNIVFN
YDMPEDSDTY LHRVARAGRF GTKGLAITFV SDENDAKILN DVQDRFEVNV AELPEEIDIS
TYIEQSR
