DDX54_MOUSE
ID DDX54_MOUSE Reviewed; 874 AA.
AC Q8K4L0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-dependent RNA helicase DDX54;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 54;
GN Name=Ddx54;
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=12080145; DOI=10.1073/pnas.142287799;
RA Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA Brinton M.A.;
RT "Positional cloning of the murine flavivirus resistance gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-40, AND
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-30; SER-33; SER-38; SER-40;
RP SER-74 AND SER-774, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC 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: Has RNA-dependent ATPase activity. Represses the
CC transcriptional activity of nuclear receptors (By similarity).
CC {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: Interacts in a hormone-dependent manner with nuclear
CC receptors. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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DR EMBL; AF319547; AAM47540.1; -; mRNA.
DR EMBL; BC043699; AAH43699.1; -; mRNA.
DR CCDS; CCDS39241.1; -.
DR RefSeq; NP_082317.1; NM_028041.2.
DR AlphaFoldDB; Q8K4L0; -.
DR SMR; Q8K4L0; -.
DR BioGRID; 215078; 4.
DR STRING; 10090.ENSMUSP00000031598; -.
DR iPTMnet; Q8K4L0; -.
DR PhosphoSitePlus; Q8K4L0; -.
DR EPD; Q8K4L0; -.
DR jPOST; Q8K4L0; -.
DR MaxQB; Q8K4L0; -.
DR PaxDb; Q8K4L0; -.
DR PRIDE; Q8K4L0; -.
DR ProteomicsDB; 279330; -.
DR Antibodypedia; 18719; 169 antibodies from 28 providers.
DR DNASU; 71990; -.
DR Ensembl; ENSMUST00000031598; ENSMUSP00000031598; ENSMUSG00000029599.
DR GeneID; 71990; -.
DR KEGG; mmu:71990; -.
DR UCSC; uc008zhq.1; mouse.
DR CTD; 79039; -.
DR MGI; MGI:1919240; Ddx54.
DR VEuPathDB; HostDB:ENSMUSG00000029599; -.
DR eggNOG; KOG0337; Eukaryota.
DR GeneTree; ENSGT00550000075100; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; Q8K4L0; -.
DR OMA; MRWDKKS; -.
DR OrthoDB; 268859at2759; -.
DR PhylomeDB; Q8K4L0; -.
DR TreeFam; TF105707; -.
DR BioGRID-ORCS; 71990; 30 hits in 77 CRISPR screens.
DR ChiTaRS; Ddx54; mouse.
DR PRO; PR:Q8K4L0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K4L0; protein.
DR Bgee; ENSMUSG00000029599; Expressed in paneth cell and 259 other tissues.
DR Genevisible; Q8K4L0; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0016070; P:RNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006396; P:RNA processing; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10.
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 PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 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; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..874
FT /note="ATP-dependent RNA helicase DDX54"
FT /id="PRO_0000055057"
FT DOMAIN 126..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 328..472
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..123
FT /note="Q motif"
FT MOTIF 246..249
FT /note="DEAD box"
FT COMPBIAS 590..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDD1"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDD1"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDD1"
SQ SEQUENCE 874 AA; 97748 MW; D25A478879368494 CRC64;
MAAGRRVGPG PPSRPTMAPW KKKRLRKRRT GASQGRDSDS DDGEFEIQAE DDARARKLGP
GRALPSFPTS ECVSDVEPDT REMVRAQNKK KKKSGGFQSM GLSYPVFKGI MKKGYKVPTP
IQRKTIPVIL DGKDVVAMAR TGSGKTACFL LPMFERLKAR SAQTGARALI LSPTRELALQ
TMKFTKELGK FTGLKTALIL GGDKMEDQFA ALHENPDIII ATPGRLVHVA VEMNLKLQSV
EYVVFDEADR LFEMGFAEQL QEIIGRLPGG HQTVLFSATL PKLLVEFARA GLTEPVLIRL
DVDSKLNEQL KTSFLLVRED TKAAVLLYLL QNVVRPQDQT VVFVATKHHA EYLTELLMGQ
GVSCAHIYSA LDQTARKINL AKFTHNKCST LIVTDLAARG LDIPLLDNVI NYSFPAKGKL
FLHRVGRVAR AGRSGTAYSL VAPDEVPYLL DLHLFLGRSV TLARPCEEPS VADAVGRDGV
LGRVPQSVVD DEDSSLQTAM GASLDLQGLH RVANNAQQQY VRSRPAPSPE SIKRAKELDL
AELGLHPLFS SCFEEGELQR LRLVDSIKNY RTRTTIFEIN ASSKDPSSQM MRAKRQRDRK
AVASFQQRRQ ERQEGPADPA PQRELPQEEE EEMVETVEGV FTEVVGQKRP RPGPSQGAKR
RRMETRQRDQ EFYVPYRPKD FDSERGLSVS GAGGAFEQQV AGAVLDLMGD EAQNMSRGQQ
QLKWDRKKKR FVGQSGQEDK KKIKTESGRF ISSSYKRDLY QKWKQKQKID DRDSEEEGPS
NQRGPGPRRG GKRGRSQGTS QPRASSVPAG RMRSELKTKE QILKQRRQAQ KQRFLQRGGL
KQLSARNRRR AQELRQGAFG RGAPSRKGKM RKRM
