GenomeNet

Database: UniProt
Entry: Q9BQ39
LinkDB: Q9BQ39
Original site: Q9BQ39 
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   16-OCT-2019, entry version 170.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   II/Gu: detection of pseudogenes and multiple alternatively spliced
RT   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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
RP   MASS 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-
RT   modification 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.,
RA   Kobayashi N., Harada T., Watanabe S., Muto Y., Guntert P., Tanaka A.,
RA   Kigawa T., Yokoyama S.;
RT   "Solution structure of the GUCT domain from human RNA helicase II/Gu
RT   beta 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
CC       {ECO:0000269|PubMed:12429849}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC       subfamily. {ECO:0000305}.
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   SMR; Q9BQ39; -.
DR   BioGrid; 122480; 78.
DR   IntAct; Q9BQ39; 34.
DR   MINT; Q9BQ39; -.
DR   STRING; 9606.ENSP00000362687; -.
DR   iPTMnet; 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   DNASU; 79009; -.
DR   Ensembl; ENST00000373585; ENSP00000362687; ENSG00000107625.
DR   GeneID; 79009; -.
DR   KEGG; hsa:79009; -.
DR   UCSC; uc001jou.3; human.
DR   CTD; 79009; -.
DR   GeneCards; DDX50; -.
DR   HGNC; HGNC:17906; DDX50.
DR   HPA; HPA037388; -.
DR   HPA; HPA037389; -.
DR   HPA; HPA058196; -.
DR   MIM; 610373; gene.
DR   neXtProt; NX_Q9BQ39; -.
DR   OpenTargets; ENSG00000107625; -.
DR   PharmGKB; PA134948525; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000155901; -.
DR   HOGENOM; HOG000268805; -.
DR   InParanoid; Q9BQ39; -.
DR   KO; K13183; -.
DR   OMA; VCFYQPR; -.
DR   OrthoDB; 1139373at2759; -.
DR   PhylomeDB; Q9BQ39; -.
DR   TreeFam; TF328622; -.
DR   ChiTaRS; DDX50; human.
DR   EvolutionaryTrace; Q9BQ39; -.
DR   GeneWiki; DDX50; -.
DR   GenomeRNAi; 79009; -.
DR   Pharos; Q9BQ39; -.
DR   PRO; PR:Q9BQ39; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000107625; Expressed in 99 organ(s), highest expression level in colon.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Helicase; Hydrolase;
KW   Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Ubl conjugation.
FT   CHAIN         1    737       ATP-dependent RNA helicase DDX50.
FT                                /FTId=PRO_0000055054.
FT   DOMAIN      168    347       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      380    524       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     181    188       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       137    165       Q motif.
FT   MOTIF       290    293       DEVD box.
FT   COMPBIAS    677    728       Arg-rich.
FT   MOD_RES      41     41       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      82     82       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      86     86       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     121    121       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JIK5}.
FT   MOD_RES     122    122       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JIK5}.
FT   MOD_RES     247    247       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES     518    518       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   CROSSLNK    125    125       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CONFLICT    680    680       S -> I (in Ref. 4; AAH18637).
FT                                {ECO:0000305}.
FT   STRAND      587    593       {ECO:0000244|PDB:2E29}.
FT   HELIX       602    611       {ECO:0000244|PDB:2E29}.
FT   HELIX       614    617       {ECO:0000244|PDB:2E29}.
FT   STRAND      621    625       {ECO:0000244|PDB:2E29}.
FT   STRAND      629    637       {ECO:0000244|PDB:2E29}.
FT   HELIX       638    647       {ECO:0000244|PDB:2E29}.
FT   STRAND      650    652       {ECO:0000244|PDB:2E29}.
FT   STRAND      654    656       {ECO:0000244|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
//
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