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ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (DEAD box protein 1) (DEAD box protein retinoblastoma) (DBP-RB)

 DDX1_HUMAN              Reviewed;         740 AA.
Q92499; B4DME8; B4DPN6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=ATP-dependent RNA helicase DDX1;
EC=3.6.4.13;
AltName: Full=DEAD box protein 1;
AltName: Full=DEAD box protein retinoblastoma;
Short=DBP-RB;
Name=DDX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Retinoblastoma;
PubMed=7689221; DOI=10.1073/pnas.90.16.7578;
Godbout R., Squire J.;
"Amplification of a DEAD box protein gene in retinoblastoma cell
lines.";
Proc. Natl. Acad. Sci. U.S.A. 90:7578-7582(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Liver;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH CSTF2, AND SUBCELLULAR LOCATION.
PubMed=11598190; DOI=10.1091/mbc.12.10.3046;
Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.;
"Association of human DEAD box protein DDX1 with a cleavage
stimulation factor involved in 3'-end processing of pre-MRNA.";
Mol. Biol. Cell 12:3046-3059(2001).
[5]
FUNCTION, INTERACTION WITH HNRNPK, AND RNA-BINDING.
PubMed=12183465; DOI=10.1074/jbc.M206981200;
Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.;
"An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous
nuclear ribonucleoprotein K.";
J. Biol. Chem. 277:40403-40409(2002).
[6]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH REV OF HIV-1
(MICROBIAL INFECTION), RNA-BINDING (MICROBIAL INFECTION), AND
SUBCELLULAR LOCATION (MICROBIAL INFECTION).
PubMed=15567440; DOI=10.1016/j.virol.2004.09.039;
Fang J., Kubota S., Yang B., Zhou N., Zhang H., Godbout R.,
Pomerantz R.J.;
"A DEAD box protein facilitates HIV-1 replication as a cellular co-
factor of Rev.";
Virology 330:471-480(2004).
[7]
FUNCTION, INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18335541; DOI=10.1002/jnr.21655;
Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.;
"MBNL1 associates with YB-1 in cytoplasmic stress granules.";
J. Neurosci. Res. 86:1994-2002(2008).
[8]
FUNCTION, INTERACTION WITH ATM, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
PubMed=18710941; DOI=10.1128/MCB.01053-08;
Li L., Monckton E.A., Godbout R.;
"A role for DEAD box 1 at DNA double-strand breaks.";
Mol. Cell. Biol. 28:6413-6425(2008).
[9]
INTERACTION WITH RELA, MUTAGENESIS OF GLU-371, AND SUBCELLULAR
LOCATION.
PubMed=19058135; DOI=10.1002/jcb.22004;
Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.;
"The DEAD-box RNA helicase DDX1 interacts with RelA and enhances
nuclear factor kappaB-mediated transcription.";
J. Cell. Biochem. 106:296-305(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-268 AND LYS-281,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH REPLICASE POLYPROTEIN
1AB NSP14 OF IBV AND SARS-COV (MICROBIAL INFECTION), AND SUBCELLULAR
LOCATION (MICROBIAL INFECTION).
PubMed=20573827; DOI=10.1128/JVI.00392-10;
Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.;
"The cellular RNA helicase DDX1 interacts with coronavirus
nonstructural protein 14 and enhances viral replication.";
J. Virol. 84:8571-8583(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH PQBP1.
PubMed=21933836; DOI=10.1093/hmg/ddr430;
Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E.,
Wanker E.E., Kalscheuer V.M.;
"The X-chromosome-linked intellectual disability protein PQBP1 is a
component of neuronal RNA granules and regulates the appearance of
stress granules.";
Hum. Mol. Genet. 20:4916-4931(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
PubMed=21311021; DOI=10.1126/science.1197847;
Popow J., Englert M., Weitzer S., Schleiffer A., Mierzwa B.,
Mechtler K., Trowitzsch S., Will C.L., Luhrmann R., Soll D.,
Martinez J.;
"HSPC117 is the essential subunit of a human tRNA splicing ligase
complex.";
Science 331:760-764(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
FUNCTION, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX, AND
MUTAGENESIS OF LYS-52 AND GLU-371.
PubMed=24870230; DOI=10.1038/nature13284;
Popow J., Jurkin J., Schleiffer A., Martinez J.;
"Analysis of orthologous groups reveals archease and DDX1 as tRNA
splicing factors.";
Nature 511:104-107(2014).
[20]
SUBCELLULAR LOCATION.
PubMed=24608264; DOI=10.1371/journal.pone.0090957;
Perez-Gonzalez A., Pazo A., Navajas R., Ciordia S.,
Rodriguez-Frandsen A., Nieto A.;
"hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel
transcription-dependent shuttling RNA-transporting complex.";
PLoS ONE 9:E90957-E90957(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
INTERACTION WITH FAM98A, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=28040436; DOI=10.1016/j.biocel.2016.12.013;
Akter K.A., Mansour M.A., Hyodo T., Senga T.;
"FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex
involved in colorectal cancer progression.";
Int. J. Biochem. Cell Biol. 84:1-13(2017).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-281, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 72-283.
PubMed=26323305; DOI=10.1107/S2053230X15013709;
Kellner J.N., Meinhart A.;
"Structure of the SPRY domain of the human RNA helicase DDX1, a
putative interaction platform within a DEAD-box protein.";
Acta Crystallogr. F 71:1176-1188(2015).
-!- FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind
both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded
RNA overhang nuclease activity. Possesses ATPase activity on
various RNA, but not DNA polynucleotides. May play a role in RNA
clearance at DNA double-strand breaks (DSBs), thereby facilitating
the template-guided repair of transcriptionally active regions of
the genome. Together with RELA, acts as a coactivator to enhance
NF-kappa-B-mediated transcriptional activation. Acts as a positive
transcriptional regulator of cyclin CCND2 expression. Binds to the
cyclin CCND2 promoter region. Associates with chromatin at the NF-
kappa-B promoter region via association with RELA. Binds to
poly(A) RNA. May be involved in 3'-end cleavage and
polyadenylation of pre-mRNAs. Component of the tRNA-splicing
ligase complex required to facilitate the enzymatic turnover of
catalytic subunit RTCB: together with archease (ZBTB8OS), acts by
facilitating the guanylylation of RTCB, a key intermediate step in
tRNA ligation (PubMed:24870230). {ECO:0000269|PubMed:12183465,
ECO:0000269|PubMed:15567440, ECO:0000269|PubMed:18335541,
ECO:0000269|PubMed:18710941, ECO:0000269|PubMed:20573827,
ECO:0000269|PubMed:24870230}.
-!- FUNCTION: (Microbial infection) Required for HIV-1 Rev function as
well as for HIV-1 and coronavirus IBV replication
(PubMed:15567440, PubMed:20573827). Binds to the RRE sequence of
HIV-1 mRNAs (PubMed:15567440). {ECO:0000269|PubMed:15567440,
ECO:0000269|PubMed:20573827}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Interacts with FAM98A (via N- and C-terminus)
(PubMed:28040436). Interacts with MBNL1 (PubMed:18335541).
Interacts with CSTF2 (PubMed:11598190). Interacts with HNRNPK
(PubMed:12183465). Interacts with ATM (PubMed:18710941). Interacts
with RELA (via C-terminus) (PubMed:19058135). Component of the
tRNA-splicing ligase complex (PubMed:21311021, PubMed:24870230).
Interacts with PQBP1 (PubMed:21933836). Interacts with PHF5A (via
C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q91VR5,
ECO:0000269|PubMed:11598190, ECO:0000269|PubMed:12183465,
ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18710941,
ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:21311021,
ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:24870230,
ECO:0000269|PubMed:28040436}.
-!- SUBUNIT: (Microbial infection) Interacts with Rev of HIV-1
(PubMed:15567440). Interacts with severe acute respiratory
syndrome coronavirus (SARS-CoV) (via N-terminus)
(PubMed:20573827). Interacts (via C-terminus) with the replicase
polyprotein 1ab Nsp14 of the avian infectious bronchitis virus
(IBV) (PubMed:20573827). {ECO:0000269|PubMed:15567440,
ECO:0000269|PubMed:20573827}.
-!- INTERACTION:
P04618:rev (xeno); NbExp=6; IntAct=EBI-15532186, EBI-6164309;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule.
Note=Localized with MBNL1, TIAL1 and YBX1 in stress granules upon
stress. Localized with CSTF2 in cleavage bodies. Forms large
aggregates called DDX1 bodies. Relocalized into multiple foci (IR-
induced foci or IRIF) after IR treatment, a process that depends
on the presence of chromosomal DNA and/or RNA-DNA duplexes.
Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-
dependent manner after IR treatment. Colocalized with RELA in the
nucleus upon TNF-alpha induction. Enters into the nucleus in case
of active transcription while it accumulates in cytosol when
transcription level is low (PubMed:24608264).
{ECO:0000269|PubMed:24608264}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20573827}.
Note=(Microbial infection) Relocalized to the cytoplasm with a
perinuclear staining pattern in avian infectious bronchitis virus
(IBV)-infected cells (PubMed:20573827). Required for proper
localization of HIV-1 Rev (PubMed:15567440).
{ECO:0000269|PubMed:15567440, ECO:0000269|PubMed:20573827}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92499-1; Sequence=Displayed;
Name=2;
IsoId=Q92499-2; Sequence=VSP_055454, VSP_055455;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q92499-3; Sequence=VSP_055453;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest levels of transcription in 2
retinoblastoma cell lines and in tissues of neuroectodermal origin
including the retina, brain, and spinal cord.
{ECO:0000269|PubMed:7689221}.
-!- DOMAIN: The helicase domain is involved in the stimulation of RELA
transcriptional activity.
-!- PTM: Phosphorylated. Phosphorylated by ATM kinase; phosphorylation
is increased in response to ionizing radiation (IR).
{ECO:0000269|PubMed:18710941}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1
subfamily. {ECO:0000305}.
-!- CAUTION: According to some authors the unwinding activity is ADP-
dependent and not ATP-dependent. {ECO:0000305|PubMed:18710941}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DDX1ID40283ch2p24.html";
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EMBL; X70649; CAA49992.1; -; mRNA.
EMBL; AK297432; BAG59860.1; -; mRNA.
EMBL; AK298426; BAG60648.1; -; mRNA.
EMBL; BC012132; AAH12132.1; -; mRNA.
EMBL; BC053673; AAH53673.1; -; mRNA.
CCDS; CCDS1686.1; -. [Q92499-1]
RefSeq; NP_004930.1; NM_004939.2. [Q92499-1]
UniGene; Hs.440599; -.
PDB; 4XW3; X-ray; 2.00 A; A/B=72-283.
PDBsum; 4XW3; -.
ProteinModelPortal; Q92499; -.
SMR; Q92499; -.
BioGrid; 108019; 144.
CORUM; Q92499; -.
DIP; DIP-38163N; -.
IntAct; Q92499; 41.
MINT; MINT-5005493; -.
STRING; 9606.ENSP00000233084; -.
BindingDB; Q92499; -.
ChEMBL; CHEMBL2010634; -.
iPTMnet; Q92499; -.
PhosphoSitePlus; Q92499; -.
SwissPalm; Q92499; -.
BioMuta; DDX1; -.
DMDM; 6919862; -.
REPRODUCTION-2DPAGE; IPI00293655; -.
EPD; Q92499; -.
MaxQB; Q92499; -.
PaxDb; Q92499; -.
PeptideAtlas; Q92499; -.
PRIDE; Q92499; -.
Ensembl; ENST00000233084; ENSP00000233084; ENSG00000079785. [Q92499-1]
Ensembl; ENST00000381341; ENSP00000370745; ENSG00000079785. [Q92499-1]
GeneID; 1653; -.
KEGG; hsa:1653; -.
UCSC; uc002rce.5; human. [Q92499-1]
CTD; 1653; -.
DisGeNET; 1653; -.
EuPathDB; HostDB:ENSG00000079785.14; -.
GeneCards; DDX1; -.
HGNC; HGNC:2734; DDX1.
HPA; CAB012280; -.
HPA; HPA034502; -.
HPA; HPA034503; -.
MIM; 601257; gene.
neXtProt; NX_Q92499; -.
OpenTargets; ENSG00000079785; -.
PharmGKB; PA27199; -.
eggNOG; KOG0349; Eukaryota.
eggNOG; COG0513; LUCA.
GeneTree; ENSGT00900000140856; -.
HOGENOM; HOG000251633; -.
HOVERGEN; HBG005462; -.
InParanoid; Q92499; -.
KO; K13177; -.
OMA; TLNNVKQ; -.
OrthoDB; EOG091G03WJ; -.
PhylomeDB; Q92499; -.
TreeFam; TF106114; -.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
ChiTaRS; DDX1; human.
GeneWiki; DDX1; -.
GenomeRNAi; 1653; -.
PRO; PR:Q92499; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000079785; -.
CleanEx; HS_DDX1; -.
ExpressionAtlas; Q92499; baseline and differential.
Genevisible; Q92499; HS.
GO; GO:0071920; C:cleavage body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0072669; C:tRNA-splicing ligase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IDA:UniProtKB.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0033677; F:DNA/RNA helicase activity; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEP:UniProtKB.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006446; P:regulation of translational initiation; NAS:UniProtKB.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
InterPro; IPR003877; SPRY_dom.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00622; SPRY; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF52540; SSF52540; 3.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Exonuclease;
Helicase; Hydrolase; Isopeptide bond; mRNA processing; Nuclease;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Transcription; Transcription regulation; tRNA processing;
Ubl conjugation.
CHAIN 1 740 ATP-dependent RNA helicase DDX1.
/FTId=PRO_0000054986.
DOMAIN 2 428 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 70 247 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
DOMAIN 493 681 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 46 53 ATP. {ECO:0000305}.
REGION 1 525 Necessary for interaction with RELA.
{ECO:0000269|PubMed:19058135}.
REGION 1 295 Necessary for interaction with HNRNPK.
{ECO:0000269|PubMed:12183465}.
REGION 525 740 Necessary for interaction with HNRNPK.
{ECO:0000269|PubMed:12183465}.
REGION 536 631 Necessary for interaction with replicase
polyprotein 1ab nsp14 of IBV.
MOTIF 370 373 DEAD box.
MOD_RES 239 239 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 268 268 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 281 281 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 281 281 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 128 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055453.
VAR_SEQ 98 113 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055454.
VAR_SEQ 630 740 VCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTI
SQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPT
VQELAALEKEAQTSFLHLGYLPNQLFRTF -> MVQRDAVT
I (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055455.
MUTAGEN 52 52 K->N: Abolishes ability to promote
guanylylation of RTCB.
{ECO:0000269|PubMed:24870230}.
MUTAGEN 371 371 E->G: Inhibits the transcriptional
activity of RELA and attenuates NF-kappa-
B-mediated gene expression.
{ECO:0000269|PubMed:19058135,
ECO:0000269|PubMed:24870230}.
MUTAGEN 371 371 E->Q: Abolishes ability to promote
guanylylation of RTCB.
{ECO:0000269|PubMed:19058135,
ECO:0000269|PubMed:24870230}.
STRAND 90 98 {ECO:0000244|PDB:4XW3}.
STRAND 102 104 {ECO:0000244|PDB:4XW3}.
STRAND 110 113 {ECO:0000244|PDB:4XW3}.
STRAND 120 139 {ECO:0000244|PDB:4XW3}.
STRAND 141 150 {ECO:0000244|PDB:4XW3}.
STRAND 164 168 {ECO:0000244|PDB:4XW3}.
TURN 169 171 {ECO:0000244|PDB:4XW3}.
STRAND 172 175 {ECO:0000244|PDB:4XW3}.
STRAND 178 181 {ECO:0000244|PDB:4XW3}.
STRAND 191 197 {ECO:0000244|PDB:4XW3}.
TURN 198 201 {ECO:0000244|PDB:4XW3}.
STRAND 202 207 {ECO:0000244|PDB:4XW3}.
STRAND 210 217 {ECO:0000244|PDB:4XW3}.
HELIX 220 222 {ECO:0000244|PDB:4XW3}.
STRAND 227 245 {ECO:0000244|PDB:4XW3}.
HELIX 258 260 {ECO:0000244|PDB:4XW3}.
HELIX 263 265 {ECO:0000244|PDB:4XW3}.
STRAND 266 268 {ECO:0000244|PDB:4XW3}.
SEQUENCE 740 AA; 82432 MW; C6D0179F83BD8C73 CRC64;
MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
IQIVYETLKD QQEGKKGKTT IKTGASVLNK WQMNPYDRGS AFAIGSDGLC CQSREVKEWH
GCRATKGLMK GKHYYEVSCH DQGLCRVGWS TMQASLDLGT DKFGFGFGGT GKKSHNKQFD
NYGEEFTMHD TIGCYLDIDK GHVKFSKNGK DLGLAFEIPP HMKNQALFPA CVLKNAELKF
NFGEEEFKFP PKDGFVALSK APDGYIVKSQ HSGNAQVTQT KFLPNAPKAL IVEPSRELAE
QTLNNIKQFK KYIDNPKLRE LLIIGGVAAR DQLSVLENGV DIVVGTPGRL DDLVSTGKLN
LSQVRFLVLD EADGLLSQGY SDFINRMHNQ IPQVTSDGKR LQVIVCSATL HSFDVKKLSE
KIMHFPTWVD LKGEDSVPDT VHHVVVPVNP KTDRLWERLG KSHIRTDDVH AKDNTRPGAN
SPEMWSEAIK ILKGEYAVRA IKEHKMDQAI IFCRTKIDCD NLEQYFIQQG GGPDKKGHQF
SCVCLHGDRK PHERKQNLER FKKGDVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
HRIGRVGRAE RMGLAISLVA TEKEKVWYHV CSSRGKGCYN TRLKEDGGCT IWYNEMQLLS
EIEEHLNCTI SQVEPDIKVP VDEFDGKVTY GQKRAAGGGS YKGHVDILAP TVQELAALEK
EAQTSFLHLG YLPNQLFRTF


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