DDX24_MOUSE
ID DDX24_MOUSE Reviewed; 857 AA.
AC Q9ESV0; Q61119; Q7TM97;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent RNA helicase DDX24;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 24;
GN Name=Ddx24;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10936056; DOI=10.1006/geno.2000.6255;
RA Zhao Y., Yu L., Fu Q., Chen W., Jiang J., Gao J., Zhao S.;
RT "Cloning and characterization of human DDX24 and mouse Ddx24, two novel
RT putative DEAD-box proteins, and mapping DDX24 to human chromosome 14q32.";
RL Genomics 67:351-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 399-857.
RC STRAIN=BALB/cJ;
RA Drysdale B., Howard D.L., Johnson R.J.;
RT "Identification of a lipopolysaccharide inducible gene in murine
RT macrophages that putatively encodes an ATP-dependent RNA helicase.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-92 AND SER-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; AF214732; AAG02170.1; -; mRNA.
DR EMBL; CH466549; EDL18835.1; -; Genomic_DNA.
DR EMBL; BC055048; AAH55048.1; -; mRNA.
DR EMBL; BC055317; AAH55317.1; -; mRNA.
DR EMBL; U46690; AAB01091.1; -; mRNA.
DR CCDS; CCDS26129.1; -.
DR RefSeq; NP_001152974.1; NM_001159502.1.
DR RefSeq; NP_065240.2; NM_020494.3.
DR RefSeq; XP_006515995.1; XM_006515932.3.
DR RefSeq; XP_006515996.1; XM_006515933.1.
DR AlphaFoldDB; Q9ESV0; -.
DR SMR; Q9ESV0; -.
DR BioGRID; 205146; 15.
DR CORUM; Q9ESV0; -.
DR STRING; 10090.ENSMUSP00000105628; -.
DR iPTMnet; Q9ESV0; -.
DR PhosphoSitePlus; Q9ESV0; -.
DR SwissPalm; Q9ESV0; -.
DR EPD; Q9ESV0; -.
DR jPOST; Q9ESV0; -.
DR MaxQB; Q9ESV0; -.
DR PaxDb; Q9ESV0; -.
DR PRIDE; Q9ESV0; -.
DR ProteomicsDB; 279900; -.
DR Antibodypedia; 108; 197 antibodies from 25 providers.
DR DNASU; 27225; -.
DR Ensembl; ENSMUST00000044923; ENSMUSP00000040890; ENSMUSG00000041645.
DR GeneID; 27225; -.
DR KEGG; mmu:27225; -.
DR UCSC; uc007ovj.2; mouse.
DR CTD; 57062; -.
DR MGI; MGI:1351337; Ddx24.
DR VEuPathDB; HostDB:ENSMUSG00000041645; -.
DR eggNOG; KOG0347; Eukaryota.
DR GeneTree; ENSGT00550000074847; -.
DR HOGENOM; CLU_003041_13_1_1; -.
DR InParanoid; Q9ESV0; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR BioGRID-ORCS; 27225; 22 hits in 72 CRISPR screens.
DR ChiTaRS; Ddx24; mouse.
DR PRO; PR:Q9ESV0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ESV0; protein.
DR Bgee; ENSMUSG00000041645; Expressed in spermatocyte and 127 other tissues.
DR ExpressionAtlas; Q9ESV0; baseline and differential.
DR Genevisible; Q9ESV0; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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 ATP-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..857
FT /note="ATP-dependent RNA helicase DDX24"
FT /id="PRO_0000055030"
FT DOMAIN 225..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 576..723
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 61..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 193..221
FT /note="Q motif"
FT MOTIF 471..474
FT /note="DEAD box"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CONFLICT 556..557
FT /note="NE -> ER (in Ref. 1; AAG02170 and 4; AAB01091)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="T -> N (in Ref. 4; AAB01091)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="E -> EDIPLFPVHFKKIYKTLQKDE (in Ref. 4; AAB01091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 857 AA; 96429 MW; F3DCF47E9F27CAEC CRC64;
MKVKETNSKP KLASRGTFQR KGIKIVGKWK QVTIDPNLFA DGQMDDLVCF EELTDYRLVK
NPSRLFSSEE TKKRKAQAVS EEEEEEEGQS SSPKKKIKLK KQRDAARAAE GAAAQNEYEV
KASEPEAQGE VTACSDQKVG GAKSESLAQA APRKKKNKGK KKLDTFQSTS PKLPKKSKKT
WMAEVHDQKA DVSAWRDLFV PKAVLRALSF LGFSAPTPIQ ALTLAPAIRD KLDILGAAET
GSGKTLAFAI PMIHSVLQWH KMKAPPIPRS TGMPPREMRF GATAHLGSPC KDRTESGVLP
EEARIETEAQ PSDSGVQATP ETSASASAQT LLVCDDDAGE GPSSLEEKPV PKQNEDGEEK
FDAEQAGKLK QELCDQIAIY KVHPRRPLLG LVLTPTRELA IQVRQHIDAV AKFTGINTAI
LVGGMSTQKQ QRMLNRHPEI VIATPGRLWE LVKEKHPHLS NLRQLRCLVI DEADRMVEKG
HFAELSQLLE MLNDSQYNPS RQTLVFSATL TLVHQAPARI LHKKHVKKMD KTDKLDLLMQ
KVGMRGKPKV IDLTRNEGTV ETLTETKIHC ETDEKDLYLY YFLMQYPGRS LVFANSISCI
KRLSGLLKVL DVMPLTLHAC MHQKQRLRNL EQFARLQDCV LLATDVAARG LDIPKVQHVI
HYQVPRTSEI YIHRSGRTAR AASEGLSLML IGPEDVINFK KIYKTLQKDE DIPLFPVQSK
YMDVVKERIR LARQIEKAEY RNFQACLHNS WIEQAAAALE IELEEEMYKG GKADQQEERR
RQKQMKMLKQ ELRHLLSQPL FQENLKTRYP TQSGRPPQPV LASRNIESAL SCLSRQKRRR
KKPKEPRAPP QPGSSTS
