DDX50_HUMAN
ID DDX50_HUMAN Reviewed; 737 AA.
AC Q9BQ39; Q5VX37; Q8WV76; Q9BWI8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 185.
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 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].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Skin;
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8]
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 [9]
RP INTERACTION WITH C1QBP.
RX PubMed=21536856; DOI=10.1074/mcp.m110.006148;
RA Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
RA Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Splicing factor 2-associated protein p32 participates in ribosome
RT biogenesis by regulating the binding of Nop52 and fibrillarin to
RT preribosome particles.";
RL Mol. Cell. Proteomics 10:0-0(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-82, 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
RN [13]
RP STRUCTURE BY NMR OF 570-659.
RX PubMed=18615715; DOI=10.1002/prot.22138;
RA Ohnishi S., Paakkonen K., Koshiba S., Tochio N., Sato M., Kobayashi N.,
RA Harada T., Watanabe S., Muto Y., Guntert P., Tanaka A., Kigawa T.,
RA Yokoyama S.;
RT "Solution structure of the GUCT domain from human RNA helicase II/Gu beta
RT reveals the RRM fold, but implausible RNA interactions.";
RL Proteins 74:133-144(2009).
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:0000269|PubMed:21536856}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
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DR EMBL; AF334103; AAK29402.1; -; mRNA.
DR EMBL; AL359844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54304.1; -; Genomic_DNA.
DR EMBL; BC000210; AAH00210.1; -; mRNA.
DR EMBL; BC000272; AAH00272.1; -; mRNA.
DR EMBL; BC018637; AAH18637.2; -; mRNA.
DR CCDS; CCDS7283.1; -.
DR RefSeq; NP_076950.1; NM_024045.1.
DR RefSeq; XP_016872115.1; XM_017016626.1.
DR PDB; 2E29; NMR; -; A=575-659.
DR PDBsum; 2E29; -.
DR AlphaFoldDB; Q9BQ39; -.
DR BMRB; Q9BQ39; -.
DR SMR; Q9BQ39; -.
DR BioGRID; 122480; 256.
DR IntAct; Q9BQ39; 59.
DR MINT; Q9BQ39; -.
DR STRING; 9606.ENSP00000362687; -.
DR GlyGen; Q9BQ39; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ39; -.
DR MetOSite; Q9BQ39; -.
DR PhosphoSitePlus; Q9BQ39; -.
DR SwissPalm; Q9BQ39; -.
DR BioMuta; DDX50; -.
DR DMDM; 55976580; -.
DR SWISS-2DPAGE; Q9BQ39; -.
DR EPD; Q9BQ39; -.
DR jPOST; Q9BQ39; -.
DR MassIVE; Q9BQ39; -.
DR MaxQB; Q9BQ39; -.
DR PaxDb; Q9BQ39; -.
DR PeptideAtlas; Q9BQ39; -.
DR PRIDE; Q9BQ39; -.
DR ProteomicsDB; 78619; -.
DR Antibodypedia; 14671; 178 antibodies from 30 providers.
DR DNASU; 79009; -.
DR Ensembl; ENST00000373585.8; ENSP00000362687.3; ENSG00000107625.14.
DR GeneID; 79009; -.
DR KEGG; hsa:79009; -.
DR MANE-Select; ENST00000373585.8; ENSP00000362687.3; NM_024045.2; NP_076950.1.
DR UCSC; uc001jou.3; human.
DR CTD; 79009; -.
DR DisGeNET; 79009; -.
DR GeneCards; DDX50; -.
DR HGNC; HGNC:17906; DDX50.
DR HPA; ENSG00000107625; Low tissue specificity.
DR MIM; 610373; gene.
DR neXtProt; NX_Q9BQ39; -.
DR OpenTargets; ENSG00000107625; -.
DR PharmGKB; PA134948525; -.
DR VEuPathDB; HostDB:ENSG00000107625; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000155901; -.
DR HOGENOM; CLU_003041_20_0_1; -.
DR InParanoid; Q9BQ39; -.
DR OMA; VCFYQPR; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q9BQ39; -.
DR TreeFam; TF328622; -.
DR PathwayCommons; Q9BQ39; -.
DR SignaLink; Q9BQ39; -.
DR BioGRID-ORCS; 79009; 28 hits in 1070 CRISPR screens.
DR ChiTaRS; DDX50; human.
DR EvolutionaryTrace; Q9BQ39; -.
DR GeneWiki; DDX50; -.
DR GenomeRNAi; 79009; -.
DR Pharos; Q9BQ39; Tbio.
DR PRO; PR:Q9BQ39; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BQ39; protein.
DR Bgee; ENSG00000107625; Expressed in cartilage tissue and 204 other tissues.
DR ExpressionAtlas; Q9BQ39; baseline and differential.
DR Genevisible; Q9BQ39; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; HDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..737
FT /note="ATP-dependent RNA helicase DDX50"
FT /id="PRO_0000055054"
FT DOMAIN 168..347
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 380..524
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 668..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..165
FT /note="Q motif"
FT MOTIF 290..293
FT /note="DEVD box"
FT COMPBIAS 17..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
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:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 680
FT /note="S -> I (in Ref. 4; AAH18637)"
FT /evidence="ECO:0000305"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:2E29"
FT HELIX 602..611
FT /evidence="ECO:0007829|PDB:2E29"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:2E29"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:2E29"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:2E29"
FT HELIX 638..647
FT /evidence="ECO:0007829|PDB:2E29"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:2E29"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:2E29"
SQ SEQUENCE 737 AA; 82565 MW; 9B7EF72EEC7C504E CRC64;
MPGKLLWGDI MELEAPLEES ESQKKERQKS DRRKSRHHYD SDEKSETREN GVTDDLDAPK
AKKSKMKEKL NGDTEEGFNR LSDEFSKSHK SRRKDLPNGD IDEYEKKSKR VSSLDTSTHK
SSDNKLEETL TREQKEGAFS NFPISEETIK LLKGRGVTYL FPIQVKTFGP VYEGKDLIAQ
ARTGTGKTFS FAIPLIERLQ RNQETIKKSR SPKVLVLAPT RELANQVAKD FKDITRKLSV
ACFYGGTSYQ SQINHIRNGI DILVGTPGRI KDHLQSGRLD LSKLRHVVLD EVDQMLDLGF
AEQVEDIIHE SYKTDSEDNP QTLLFSATCP QWVYKVAKKY MKSRYEQVDL VGKMTQKAAT
TVEHLAIQCH WSQRPAVIGD VLQVYSGSEG RAIIFCETKK NVTEMAMNPH IKQNAQCLHG
DIAQSQREIT LKGFREGSFK VLVATNVAAR GLDIPEVDLV IQSSPPQDVE SYIHRSGRTG
RAGRTGICIC FYQPRERGQL RYVEQKAGIT FKRVGVPSTM DLVKSKSMDA IRSLASVSYA
AVDFFRPSAQ RLIEEKGAVD ALAAALAHIS GASSFEPRSL ITSDKGFVTM TLESLEEIQD
VSCAWKELNR KLSSNAVSQI TRMCLLKGNM GVCFDVPTTE SERLQAEWHD SDWILSVPAK
LPEIEEYYDG NTSSNSRQRS GWSSGRSGRS GRSGGRSGGR SGRQSRQGSR SGSRQDGRRR
SGNRNRSRSG GHKRSFD
