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Q9NR30

- DDX21_HUMAN

UniProt

Q9NR30 - DDX21_HUMAN

Protein

Nucleolar RNA helicase 2

Gene

DDX21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 5 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription. Involved in rRNA processing.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi230 – 2378ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent RNA helicase activity Source: ProtInc
    3. double-stranded RNA binding Source: Ensembl
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. osteoblast differentiation Source: UniProt
    3. response to exogenous dsRNA Source: Ensembl
    4. response to virus Source: Ensembl

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar RNA helicase 2 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 21
    Gu-alpha
    Nucleolar RNA helicase Gu
    Nucleolar RNA helicase II
    RH II/Gu
    Gene namesi
    Name:DDX21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2744. DDX21.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27210.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 783783Nucleolar RNA helicase 2PRO_0000055027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine4 Publications
    Modified residuei71 – 711Phosphoserine4 Publications
    Modified residuei89 – 891Phosphoserine5 Publications
    Modified residuei121 – 1211Phosphoserine6 Publications
    Modified residuei147 – 1471PhosphoserineBy similarity
    Modified residuei171 – 1711PhosphoserineBy similarity
    Modified residuei296 – 2961Phosphothreonine1 Publication
    Modified residuei567 – 5671Phosphoserine1 Publication
    Modified residuei779 – 7791N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NR30.
    PaxDbiQ9NR30.
    PeptideAtlasiQ9NR30.
    PRIDEiQ9NR30.

    2D gel databases

    SWISS-2DPAGEQ9NR30.

    PTM databases

    PhosphoSiteiQ9NR30.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NR30.
    BgeeiQ9NR30.
    CleanExiHS_DDX21.
    GenevestigatoriQ9NR30.

    Organism-specific databases

    HPAiHPA036592.
    HPA036593.

    Interactioni

    Subunit structurei

    Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with C1QBP.2 Publications

    Protein-protein interaction databases

    BioGridi114625. 96 interactions.
    IntActiQ9NR30. 33 interactions.
    MINTiMINT-231639.
    STRINGi9606.ENSP00000346120.

    Structurei

    Secondary structure

    1
    783
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi631 – 64212
    Helixi651 – 66010
    Turni664 – 6674
    Helixi676 – 6783
    Beta strandi679 – 6868
    Helixi687 – 6937
    Beta strandi704 – 7074

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M3DNMR-A617-710[»]
    ProteinModelPortaliQ9NR30.
    SMRiQ9NR30. Positions 148-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 396180Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini429 – 573145Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati724 – 72851
    Repeati734 – 73852
    Repeati744 – 74853

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni724 – 748253 X 5 AA repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi186 – 21429Q motifAdd
    BLAST
    Motifi339 – 3424DEVD box

    Domaini

    The two enzymatic activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus.
    The 3 X 5 AA repeats seem to be critical for the RNA folding activity.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268805.
    HOVERGENiHBG051331.
    InParanoidiQ9NR30.
    KOiK16911.
    OMAiSQNDISP.
    OrthoDBiEOG77HDD6.
    PhylomeDBiQ9NR30.
    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. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR30-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPGKLRSDAG LESDTAMKKG ETLRKQTEEK EKKEKPKSDK TEEIAEEEET    50
    VFPKAKQVKK KAEPSEVDMN SPKSKKAKKK EEPSQNDISP KTKSLRKKKE 100
    PIEKKVVSSK TKKVTKNEEP SEEEIDAPKP KKMKKEKEMN GETREKSPKL 150
    KNGFPHPEPD CNPSEAASEE SNSEIEQEIP VEQKEGAFSN FPISEETIKL 200
    LKGRGVTFLF PIQAKTFHHV YSGKDLIAQA RTGTGKTFSF AIPLIEKLHG 250
    ELQDRKRGRA PQVLVLAPTR ELANQVSKDF SDITKKLSVA CFYGGTPYGG 300
    QFERMRNGID ILVGTPGRIK DHIQNGKLDL TKLKHVVLDE VDQMLDMGFA 350
    DQVEEILSVA YKKDSEDNPQ TLLFSATCPH WVFNVAKKYM KSTYEQVDLI 400
    GKKTQKTAIT VEHLAIKCHW TQRAAVIGDV IRVYSGHQGR TIIFCETKKE 450
    AQELSQNSAI KQDAQSLHGD IPQKQREITL KGFRNGSFGV LVATNVAARG 500
    LDIPEVDLVI QSSPPKDVES YIHRSGRTGR AGRTGVCICF YQHKEEYQLV 550
    QVEQKAGIKF KRIGVPSATE IIKASSKDAI RLLDSVPPTA ISHFKQSAEK 600
    LIEEKGAVEA LAAALAHISG ATSVDQRSLI NSNVGFVTMI LQCSIEMPNI 650
    SYAWKELKEQ LGEEIDSKVK GMVFLKGKLG VCFDVPTASV TEIQEKWHDS 700
    RRWQLSVATE QPELEGPREG YGGFRGQREG SRGFRGQRDG NRRFRGQREG 750
    SRGPRGQRSG GGNKSNRSQN KGQKRSFSKA FGQ 783
    Length:783
    Mass (Da):87,344
    Last modified:September 27, 2005 - v5
    Checksum:i4F6673E38686644F
    GO
    Isoform 2 (identifier: Q9NR30-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: Missing.

    Show »
    Length:715
    Mass (Da):79,657
    Checksum:i8CB8E8BE914EA9DB
    GO

    Sequence cautioni

    The sequence AAB02546.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti273 – 2731A → C(PubMed:11237763)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271T → I.2 Publications
    Corresponds to variant rs17556220 [ dbSNP | Ensembl ].
    VAR_052161

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6868Missing in isoform 2. 2 PublicationsVSP_015716Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41387 mRNA. Translation: AAB02546.1. Different initiation.
    AF261903 Genomic DNA. No translation available.
    AF261917
    , AF261904, AF261905, AF261906, AF261907, AF261908, AF261909, AF261910, AF261911, AF261912, AF261913, AF261914, AF261915, AF261916 Genomic DNA. Translation: AAF78930.2.
    AK315585 mRNA. Translation: BAG37957.1.
    CR749598 mRNA. Translation: CAH18395.1.
    AL359844 Genomic DNA. Translation: CAH72377.1.
    CH471083 Genomic DNA. Translation: EAW54307.1.
    BC008071 mRNA. Translation: AAH08071.2.
    CCDSiCCDS31211.1. [Q9NR30-1]
    PIRiPC6010.
    RefSeqiNP_001243839.1. NM_001256910.1. [Q9NR30-2]
    NP_004719.2. NM_004728.3. [Q9NR30-1]
    UniGeneiHs.223141.

    Genome annotation databases

    EnsembliENST00000354185; ENSP00000346120; ENSG00000165732. [Q9NR30-1]
    GeneIDi9188.
    KEGGihsa:9188.
    UCSCiuc001jov.2. human. [Q9NR30-1]

    Polymorphism databases

    DMDMi76803555.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41387 mRNA. Translation: AAB02546.1 . Different initiation.
    AF261903 Genomic DNA. No translation available.
    AF261917
    , AF261904 , AF261905 , AF261906 , AF261907 , AF261908 , AF261909 , AF261910 , AF261911 , AF261912 , AF261913 , AF261914 , AF261915 , AF261916 Genomic DNA. Translation: AAF78930.2 .
    AK315585 mRNA. Translation: BAG37957.1 .
    CR749598 mRNA. Translation: CAH18395.1 .
    AL359844 Genomic DNA. Translation: CAH72377.1 .
    CH471083 Genomic DNA. Translation: EAW54307.1 .
    BC008071 mRNA. Translation: AAH08071.2 .
    CCDSi CCDS31211.1. [Q9NR30-1 ]
    PIRi PC6010.
    RefSeqi NP_001243839.1. NM_001256910.1. [Q9NR30-2 ]
    NP_004719.2. NM_004728.3. [Q9NR30-1 ]
    UniGenei Hs.223141.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M3D NMR - A 617-710 [» ]
    ProteinModelPortali Q9NR30.
    SMRi Q9NR30. Positions 148-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114625. 96 interactions.
    IntActi Q9NR30. 33 interactions.
    MINTi MINT-231639.
    STRINGi 9606.ENSP00000346120.

    PTM databases

    PhosphoSitei Q9NR30.

    Polymorphism databases

    DMDMi 76803555.

    2D gel databases

    SWISS-2DPAGE Q9NR30.

    Proteomic databases

    MaxQBi Q9NR30.
    PaxDbi Q9NR30.
    PeptideAtlasi Q9NR30.
    PRIDEi Q9NR30.

    Protocols and materials databases

    DNASUi 9188.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354185 ; ENSP00000346120 ; ENSG00000165732 . [Q9NR30-1 ]
    GeneIDi 9188.
    KEGGi hsa:9188.
    UCSCi uc001jov.2. human. [Q9NR30-1 ]

    Organism-specific databases

    CTDi 9188.
    GeneCardsi GC10P070715.
    H-InvDB HIX0008880.
    HGNCi HGNC:2744. DDX21.
    HPAi HPA036592.
    HPA036593.
    MIMi 606357. gene.
    neXtProti NX_Q9NR30.
    PharmGKBi PA27210.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268805.
    HOVERGENi HBG051331.
    InParanoidi Q9NR30.
    KOi K16911.
    OMAi SQNDISP.
    OrthoDBi EOG77HDD6.
    PhylomeDBi Q9NR30.
    TreeFami TF328622.

    Miscellaneous databases

    ChiTaRSi DDX21. human.
    GeneWikii DDX21.
    GenomeRNAii 9188.
    NextBioi 34453.
    PROi Q9NR30.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR30.
    Bgeei Q9NR30.
    CleanExi HS_DDX21.
    Genevestigatori Q9NR30.

    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. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A nucleolar RNA helicase recognized by autoimmune antibodies from a patient with watermelon stomach disease."
      Valdez B.C., Henning D., Busch R.K., Woods K., Flores-Rozas H., Hurwitz J., Perlaky L., Busch H.
      Nucleic Acids Res. 24:1220-1224(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT ILE-27.
    2. "Human RNA helicase II/Gu gene: genomic organization and promoter analysis."
      Zhu K., Henning D., Valdez B.C., Busch H.
      Biochem. Biophys. Res. Commun. 281:1006-1011(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-27.
      Tissue: Cervix adenocarcinoma.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Uterine endothelium.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Colon and Muscle.
    8. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 7-18; 117-131; 185-199; 205-215; 237-247; 258-270; 287-304; 307-318; 364-387; 392-402; 407-417; 424-432; 450-474; 485-499; 545-555; 606-627; 659-668; 679-696 AND 703-718, PHOSPHORYLATION AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    9. "The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
      Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
      EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 185-199; 260-270 AND 563-573, FUNCTION.
    10. "Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA production."
      Henning D., So R.B., Jin R., Lau L.F., Valdez B.C.
      J. Biol. Chem. 278:52307-52314(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
    13. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-13; SER-71; SER-89; SER-121; THR-296 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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.
    22. "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-13; SER-71; SER-89 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDDX21_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR30
    Secondary accession number(s): B2RDL0
    , Q13436, Q5VX41, Q68D35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 156 of the entry and version 5 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

    Miscellaneous

    Autoantibodies against DDX21 are found in patients with watermelon stomach disease, which is characterized by prominent stripes of ectatic vascular tissue in the stomach similar to stripes on a watermelon.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3