DDX50_MOUSE
ID DDX50_MOUSE Reviewed; 734 AA.
AC Q99MJ9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP-dependent RNA helicase DDX50;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 50;
DE AltName: Full=Gu-beta;
DE AltName: Full=Nucleolar protein Gu2;
GN Name=Ddx50;
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=11891046; DOI=10.1016/s0378-1119(01)00888-5;
RA Valdez B.C., Yang H., Hong E., Sequitin A.M.;
RT "Genomic structure of newly identified paralogue of RNA helicase II/Gu:
RT detection of pseudogenes and multiple alternatively spliced mRNAs.";
RL Gene 284:53-61(2002).
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 with C1QBP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
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DR EMBL; AF334104; AAK29403.1; -; mRNA.
DR CCDS; CCDS23892.1; -.
DR RefSeq; NP_444413.1; NM_053183.2.
DR AlphaFoldDB; Q99MJ9; -.
DR SMR; Q99MJ9; -.
DR BioGRID; 220470; 2.
DR STRING; 10090.ENSMUSP00000020270; -.
DR iPTMnet; Q99MJ9; -.
DR PhosphoSitePlus; Q99MJ9; -.
DR EPD; Q99MJ9; -.
DR jPOST; Q99MJ9; -.
DR MaxQB; Q99MJ9; -.
DR PaxDb; Q99MJ9; -.
DR PeptideAtlas; Q99MJ9; -.
DR PRIDE; Q99MJ9; -.
DR ProteomicsDB; 279855; -.
DR Antibodypedia; 14671; 178 antibodies from 30 providers.
DR DNASU; 94213; -.
DR Ensembl; ENSMUST00000020270; ENSMUSP00000020270; ENSMUSG00000020076.
DR GeneID; 94213; -.
DR KEGG; mmu:94213; -.
DR UCSC; uc007fho.1; mouse.
DR CTD; 79009; -.
DR MGI; MGI:2182303; Ddx50.
DR VEuPathDB; HostDB:ENSMUSG00000020076; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000155901; -.
DR HOGENOM; CLU_003041_20_0_1; -.
DR InParanoid; Q99MJ9; -.
DR OMA; VCFYQPR; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q99MJ9; -.
DR TreeFam; TF328622; -.
DR BioGRID-ORCS; 94213; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ddx50; mouse.
DR PRO; PR:Q99MJ9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99MJ9; protein.
DR Bgee; ENSMUSG00000020076; Expressed in vestibular epithelium and 244 other tissues.
DR ExpressionAtlas; Q99MJ9; baseline and differential.
DR Genevisible; Q99MJ9; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..734
FT /note="ATP-dependent RNA helicase DDX50"
FT /id="PRO_0000055055"
FT DOMAIN 165..344
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 377..521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..162
FT /note="Q motif"
FT MOTIF 287..290
FT /note="DEVD box"
FT COMPBIAS 17..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ39"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ39"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ39"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ39"
SQ SEQUENCE 734 AA; 82175 MW; E816B0B2555EE20A CRC64;
MPGKLLWGDI MELEAPLEES ESQRKERQKS DRRKSRHHSE SEERTETREN GVTDDLDAPK
PKKAKMREKL NGDTKEGLRF SDEFSPSHKS RRKDLPNGDV DEYEKRSKRV SSSENSHKSS
DKAEETLTRE QKEGAFSNFS ISEETIKLLK GRGVTYLFPI QVKTFGPVYE GKDLIAQART
GTGKTFSFAI PLIERLQRNQ ETIKKSRSPK VLVLAPTREL ANQVAKDFKD ITRKLSVACF
YGGTSYQSQI NQIRNGIDIL VGTPGRIKDH LQSGRLDLSK LRHVVLDEVD QMLDLGFAEQ
VEDIIHESYK TDSEDNPQTL LFSATCPQWV YKVAKKYMKS RYEQVDLVGK MTQKAATTVE
HLAIQCHWSQ RPAVIGDVLQ VYSGSEGRAI IFCETKKNVT EMAMNPHIKQ NAQCLHGDIA
QSQREITLKG FREGSFKVLV ATNVAARGLD IPEVDLVIQS SPPQDVESYI HRSGRTGRAG
RTGICVCFYQ PRERGQLRYV EQKAGITFKR VGVPSTMDLV KSKSMDAIRS LASVSYAAVD
FFRPSAQRLI EEKGAVDALA AALAHISGAS SFEPRSLITS DKGFVTMTLE SPEEIQDVSC
AWKELNRKLS SNAVSHVTRM CLLKGNMGVC FDVPTSESER LQAEWHDSDW ILSVPAKLPE
IEEYYDGNTS SNPRQRSGWS GGRSGRSGRS GGRSGGRSGR QSRQGSRSGS RQDGRRRSGN
RNRSRSGGHK RNFD
