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Q9BQ39

- DDX50_HUMAN

UniProt

Q9BQ39 - DDX50_HUMAN

Protein

ATP-dependent RNA helicase DDX50

Gene

DDX50

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi181 – 1888ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. helicase activity Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DDX50 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 50
    Gu-beta
    Nucleolar protein Gu2
    Gene namesi
    Name:DDX50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17906. DDX50.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleolus Source: HPA
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134948525.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 737737ATP-dependent RNA helicase DDX50PRO_0000055054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei82 – 821Phosphoserine2 Publications
    Modified residuei86 – 861Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQ39.
    PaxDbiQ9BQ39.
    PeptideAtlasiQ9BQ39.
    PRIDEiQ9BQ39.

    2D gel databases

    SWISS-2DPAGEQ9BQ39.

    PTM databases

    PhosphoSiteiQ9BQ39.

    Expressioni

    Gene expression databases

    BgeeiQ9BQ39.
    CleanExiHS_DDX50.
    GenevestigatoriQ9BQ39.

    Organism-specific databases

    HPAiHPA037388.

    Interactioni

    Subunit structurei

    Interacts with C1QBP.1 Publication

    Protein-protein interaction databases

    BioGridi122480. 17 interactions.
    IntActiQ9BQ39. 9 interactions.
    MINTiMINT-4727989.
    STRINGi9606.ENSP00000362687.

    Structurei

    Secondary structure

    1
    737
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi587 – 5937
    Helixi602 – 61110
    Helixi614 – 6174
    Beta strandi621 – 6255
    Beta strandi629 – 6379
    Helixi638 – 64710
    Beta strandi650 – 6523
    Beta strandi654 – 6563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E29NMR-A575-659[»]
    ProteinModelPortaliQ9BQ39.
    SMRiQ9BQ39. Positions 123-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BQ39.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 347180Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini380 – 524145Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi137 – 16529Q motifAdd
    BLAST
    Motifi290 – 2934DEVD box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi677 – 72852Arg-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268805.
    HOVERGENiHBG051331.
    InParanoidiQ9BQ39.
    KOiK13183.
    OMAiNSHKSSD.
    OrthoDBiEOG77HDD6.
    PhylomeDBiQ9BQ39.
    TreeFamiTF328622.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR012562. GUCT.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF08152. GUCT. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BQ39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGKLLWGDI MELEAPLEES ESQKKERQKS DRRKSRHHYD SDEKSETREN    50
    GVTDDLDAPK AKKSKMKEKL NGDTEEGFNR LSDEFSKSHK SRRKDLPNGD 100
    IDEYEKKSKR VSSLDTSTHK SSDNKLEETL TREQKEGAFS NFPISEETIK 150
    LLKGRGVTYL FPIQVKTFGP VYEGKDLIAQ ARTGTGKTFS FAIPLIERLQ 200
    RNQETIKKSR SPKVLVLAPT RELANQVAKD FKDITRKLSV ACFYGGTSYQ 250
    SQINHIRNGI DILVGTPGRI KDHLQSGRLD LSKLRHVVLD EVDQMLDLGF 300
    AEQVEDIIHE SYKTDSEDNP QTLLFSATCP QWVYKVAKKY MKSRYEQVDL 350
    VGKMTQKAAT TVEHLAIQCH WSQRPAVIGD VLQVYSGSEG RAIIFCETKK 400
    NVTEMAMNPH IKQNAQCLHG DIAQSQREIT LKGFREGSFK VLVATNVAAR 450
    GLDIPEVDLV IQSSPPQDVE SYIHRSGRTG RAGRTGICIC FYQPRERGQL 500
    RYVEQKAGIT FKRVGVPSTM DLVKSKSMDA IRSLASVSYA AVDFFRPSAQ 550
    RLIEEKGAVD ALAAALAHIS GASSFEPRSL ITSDKGFVTM TLESLEEIQD 600
    VSCAWKELNR KLSSNAVSQI TRMCLLKGNM GVCFDVPTTE SERLQAEWHD 650
    SDWILSVPAK LPEIEEYYDG NTSSNSRQRS GWSSGRSGRS GRSGGRSGGR 700
    SGRQSRQGSR SGSRQDGRRR SGNRNRSRSG GHKRSFD 737
    Length:737
    Mass (Da):82,565
    Last modified:June 1, 2001 - v1
    Checksum:i9B7EF72EEC7C504E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti680 – 6801S → I in AAH18637. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF334103 mRNA. Translation: AAK29402.1.
    AL359844 Genomic DNA. Translation: CAH72376.1.
    CH471083 Genomic DNA. Translation: EAW54304.1.
    BC000210 mRNA. Translation: AAH00210.1.
    BC000272 mRNA. Translation: AAH00272.1.
    BC018637 mRNA. Translation: AAH18637.2.
    CCDSiCCDS7283.1.
    RefSeqiNP_076950.1. NM_024045.1.
    UniGeneiHs.522984.

    Genome annotation databases

    EnsembliENST00000373585; ENSP00000362687; ENSG00000107625.
    GeneIDi79009.
    KEGGihsa:79009.
    UCSCiuc001jou.3. human.

    Polymorphism databases

    DMDMi55976580.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF334103 mRNA. Translation: AAK29402.1 .
    AL359844 Genomic DNA. Translation: CAH72376.1 .
    CH471083 Genomic DNA. Translation: EAW54304.1 .
    BC000210 mRNA. Translation: AAH00210.1 .
    BC000272 mRNA. Translation: AAH00272.1 .
    BC018637 mRNA. Translation: AAH18637.2 .
    CCDSi CCDS7283.1.
    RefSeqi NP_076950.1. NM_024045.1.
    UniGenei Hs.522984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E29 NMR - A 575-659 [» ]
    ProteinModelPortali Q9BQ39.
    SMRi Q9BQ39. Positions 123-659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122480. 17 interactions.
    IntActi Q9BQ39. 9 interactions.
    MINTi MINT-4727989.
    STRINGi 9606.ENSP00000362687.

    PTM databases

    PhosphoSitei Q9BQ39.

    Polymorphism databases

    DMDMi 55976580.

    2D gel databases

    SWISS-2DPAGE Q9BQ39.

    Proteomic databases

    MaxQBi Q9BQ39.
    PaxDbi Q9BQ39.
    PeptideAtlasi Q9BQ39.
    PRIDEi Q9BQ39.

    Protocols and materials databases

    DNASUi 79009.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373585 ; ENSP00000362687 ; ENSG00000107625 .
    GeneIDi 79009.
    KEGGi hsa:79009.
    UCSCi uc001jou.3. human.

    Organism-specific databases

    CTDi 79009.
    GeneCardsi GC10P070661.
    HGNCi HGNC:17906. DDX50.
    HPAi HPA037388.
    MIMi 610373. gene.
    neXtProti NX_Q9BQ39.
    PharmGKBi PA134948525.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268805.
    HOVERGENi HBG051331.
    InParanoidi Q9BQ39.
    KOi K13183.
    OMAi NSHKSSD.
    OrthoDBi EOG77HDD6.
    PhylomeDBi Q9BQ39.
    TreeFami TF328622.

    Miscellaneous databases

    ChiTaRSi DDX50. human.
    EvolutionaryTracei Q9BQ39.
    GeneWikii DDX50.
    GenomeRNAii 79009.
    NextBioi 67657.
    PROi Q9BQ39.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BQ39.
    CleanExi HS_DDX50.
    Genevestigatori Q9BQ39.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR012562. GUCT.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF08152. GUCT. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure of newly identified paralogue of RNA helicase II/Gu: detection of pseudogenes and multiple alternatively spliced mRNAs."
      Valdez B.C., Yang H., Hong E., Sequitin A.M.
      Gene 284:53-61(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye and Skin.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
      Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
      Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C1QBP.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of the GUCT domain from human RNA helicase II/Gu beta reveals the RRM fold, but implausible RNA interactions."
      Ohnishi S., Paakkonen K., Koshiba S., Tochio N., Sato M., Kobayashi N., Harada T., Watanabe S., Muto Y., Guntert P., Tanaka A., Kigawa T., Yokoyama S.
      Proteins 74:133-144(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 570-659.

    Entry informationi

    Entry nameiDDX50_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQ39
    Secondary accession number(s): Q5VX37, Q8WV76, Q9BWI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3