Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UHI6

- DDX20_HUMAN

UniProt

Q9UHI6 - DDX20_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX20

Gene

DDX20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841ATP; via carbonyl oxygen
    Binding sitei89 – 891ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi109 – 1146ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent RNA helicase activity Source: ProtInc
    3. DNA binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. gene expression Source: Reactome
    3. ncRNA metabolic process Source: Reactome
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. oogenesis Source: Ensembl
    6. positive regulation of apoptotic process Source: UniProtKB
    7. regulation of steroid biosynthetic process Source: Ensembl
    8. RNA metabolic process Source: Reactome
    9. RNA processing Source: ProtInc
    10. spliceosomal snRNP assembly Source: UniProtKB
    11. spliceosomal tri-snRNP complex assembly Source: ProtInc

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX20 (EC:3.6.4.13)
    Alternative name(s):
    Component of gems 3
    DEAD box protein 20
    DEAD box protein DP 103
    Gemin-3
    Gene namesi
    Name:DDX20
    Synonyms:DP103, GEMIN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2743. DDX20.

    Subcellular locationi

    Cytoplasm. Nucleusgem
    Note: Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: ProtInc
    3. cytosol Source: UniProtKB
    4. Gemini of coiled bodies Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: HPA
    8. SMN complex Source: UniProtKB
    9. SMN-Sm protein complex Source: UniProtKB
    10. transcriptional repressor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27209.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 824824Probable ATP-dependent RNA helicase DDX20PRO_0000055025Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei505 – 5051Phosphoserine1 Publication
    Modified residuei532 – 5321Phosphoserine1 Publication
    Modified residuei552 – 5521Phosphothreonine2 Publications
    Modified residuei652 – 6521Phosphoserine1 Publication
    Modified residuei654 – 6541Phosphoserine1 Publication
    Modified residuei656 – 6561Phosphoserine1 Publication
    Modified residuei672 – 6721Phosphoserine2 Publications
    Modified residuei677 – 6771Phosphoserine3 Publications
    Modified residuei678 – 6781Phosphoserine4 Publications
    Modified residuei688 – 6881Phosphothreonine1 Publication
    Modified residuei703 – 7031Phosphoserine2 Publications
    Modified residuei705 – 7051Phosphothreonine1 Publication
    Modified residuei714 – 7141Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHI6.
    PaxDbiQ9UHI6.
    PeptideAtlasiQ9UHI6.
    PRIDEiQ9UHI6.

    PTM databases

    PhosphoSiteiQ9UHI6.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9UHI6.
    BgeeiQ9UHI6.
    CleanExiHS_DDX20.
    GenevestigatoriQ9UHI6.

    Organism-specific databases

    HPAiCAB015427.
    HPA005516.
    HPA023541.

    Interactioni

    Subunit structurei

    Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2. Interacts with EBV EBNA2 and EBNA3C. Interacts with NANOS1 and PUM2.8 Publications

    Protein-protein interaction databases

    BioGridi116387. 51 interactions.
    DIPiDIP-32606N.
    IntActiQ9UHI6. 16 interactions.
    MINTiMINT-96973.
    STRINGi9606.ENSP00000358716.

    Structurei

    Secondary structure

    1
    824
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 674
    Helixi71 – 799
    Helixi87 – 9711
    Beta strandi102 – 1054
    Helixi112 – 12312
    Beta strandi133 – 1364
    Helixi140 – 15314
    Turni154 – 1563
    Beta strandi162 – 1654
    Helixi171 – 1777
    Beta strandi182 – 1865
    Helixi188 – 1969
    Helixi202 – 2043
    Beta strandi207 – 2126
    Helixi213 – 2175
    Helixi223 – 23210
    Beta strandi238 – 2447
    Helixi248 – 2547
    Turni255 – 2573
    Beta strandi262 – 2643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OXCX-ray1.30A/B41-268[»]
    3B7GX-ray1.90A/B41-268[»]
    ProteinModelPortaliQ9UHI6.
    SMRiQ9UHI6. Positions 30-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHI6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 264172Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini299 – 448150Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni456 – 54893SMN interactingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi62 – 9029Q motifAdd
    BLAST
    Motifi211 – 2144DEAD box

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000112184.
    HOVERGENiHBG051330.
    InParanoidiQ9UHI6.
    KOiK13131.
    OMAiQYYKIVN.
    OrthoDBiEOG7PGDPX.
    PhylomeDBiQ9UHI6.
    TreeFamiTF352222.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. 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: Q9UHI6-1) [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

    MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR    50
    TRTGDVLLAE PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL 100
    DLIVQAKSGT GKTCVFSTIA LDSLVLENLS TQILILAPTR EIAVQIHSVI 150
    TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK CHIAVGSPGR IKQLIELDYL 200
    NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML AVSATYPEFL 250
    ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL 300
    QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD 350
    AMAKLKHFHC RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA 400
    GRFGTLGLTV TYCCRGEEEN MMMRIAQKCN INLLPLPDPI PSGLMEECVD 450
    WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE RTLQIQKAHG DHMASSRNNS 500
    VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR QSEEQMKNSV 550
    QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH 600
    YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG 650
    DSESDSDSYS SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP 700
    NGSDTPNPEK YQESPGIQMK TRLKEGASQR AKQSRRNLPR RSSFRLQTEA 750
    QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY YRAWQEYYAA ASHSYYWNAQ 800
    RHPSWMAAYH MNTIYLQEMM HSNQ 824
    Length:824
    Mass (Da):92,241
    Last modified:December 1, 2000 - v2
    Checksum:i76712F014B2A0CF2
    GO
    Isoform 2 (identifier: Q9UHI6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         133-138: ILILAP → AELSNS
         139-824: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:138
    Mass (Da):14,272
    Checksum:iA3075B1CEE1AF15C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51F → V in AAD42744. (PubMed:10383418)Curated
    Sequence conflicti279 – 2791Y → C in BAA91727. (PubMed:14702039)Curated
    Sequence conflicti639 – 6391R → K in AAF14544. (PubMed:10601333)Curated
    Sequence conflicti659 – 6591Y → H in AAD42744. (PubMed:10383418)Curated
    Sequence conflicti676 – 6761G → S in AAF14544. (PubMed:10601333)Curated
    Sequence conflicti703 – 7031S → T in AAF14544. (PubMed:10601333)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti636 – 6361I → T.1 Publication
    Corresponds to variant rs197412 [ dbSNP | Ensembl ].
    VAR_057231
    Natural varianti693 – 6931R → S.
    Corresponds to variant rs197414 [ dbSNP | Ensembl ].
    VAR_057232
    Natural varianti762 – 7621I → T.
    Corresponds to variant rs85276 [ dbSNP | Ensembl ].
    VAR_057233

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei133 – 1386ILILAP → AELSNS in isoform 2. 1 PublicationVSP_056505
    Alternative sequencei139 – 824686Missing in isoform 2. 1 PublicationVSP_056506Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171063 mRNA. Translation: AAF14544.1.
    AF106019 mRNA. Translation: AAD42744.1.
    AK001506 mRNA. Translation: BAA91727.1.
    AK301697 mRNA. Translation: BAG63169.1.
    AL049557 Genomic DNA. Translation: CAB55686.2.
    BC011556 mRNA. Translation: AAH11556.1.
    AL133598 mRNA. Translation: CAB63734.2.
    CCDSiCCDS842.1.
    PIRiT43476.
    RefSeqiNP_009135.4. NM_007204.4.
    UniGeneiHs.591405.

    Genome annotation databases

    EnsembliENST00000369702; ENSP00000358716; ENSG00000064703.
    ENST00000533164; ENSP00000434085; ENSG00000064703.
    GeneIDi11218.
    KEGGihsa:11218.
    UCSCiuc001ebs.3. human.

    Polymorphism databases

    DMDMi12643886.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171063 mRNA. Translation: AAF14544.1 .
    AF106019 mRNA. Translation: AAD42744.1 .
    AK001506 mRNA. Translation: BAA91727.1 .
    AK301697 mRNA. Translation: BAG63169.1 .
    AL049557 Genomic DNA. Translation: CAB55686.2 .
    BC011556 mRNA. Translation: AAH11556.1 .
    AL133598 mRNA. Translation: CAB63734.2 .
    CCDSi CCDS842.1.
    PIRi T43476.
    RefSeqi NP_009135.4. NM_007204.4.
    UniGenei Hs.591405.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OXC X-ray 1.30 A/B 41-268 [» ]
    3B7G X-ray 1.90 A/B 41-268 [» ]
    ProteinModelPortali Q9UHI6.
    SMRi Q9UHI6. Positions 30-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116387. 51 interactions.
    DIPi DIP-32606N.
    IntActi Q9UHI6. 16 interactions.
    MINTi MINT-96973.
    STRINGi 9606.ENSP00000358716.

    PTM databases

    PhosphoSitei Q9UHI6.

    Polymorphism databases

    DMDMi 12643886.

    Proteomic databases

    MaxQBi Q9UHI6.
    PaxDbi Q9UHI6.
    PeptideAtlasi Q9UHI6.
    PRIDEi Q9UHI6.

    Protocols and materials databases

    DNASUi 11218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369702 ; ENSP00000358716 ; ENSG00000064703 .
    ENST00000533164 ; ENSP00000434085 ; ENSG00000064703 .
    GeneIDi 11218.
    KEGGi hsa:11218.
    UCSCi uc001ebs.3. human.

    Organism-specific databases

    CTDi 11218.
    GeneCardsi GC01P112298.
    HGNCi HGNC:2743. DDX20.
    HPAi CAB015427.
    HPA005516.
    HPA023541.
    MIMi 606168. gene.
    neXtProti NX_Q9UHI6.
    PharmGKBi PA27209.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000112184.
    HOVERGENi HBG051330.
    InParanoidi Q9UHI6.
    KOi K13131.
    OMAi QYYKIVN.
    OrthoDBi EOG7PGDPX.
    PhylomeDBi Q9UHI6.
    TreeFami TF352222.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.

    Miscellaneous databases

    EvolutionaryTracei Q9UHI6.
    GeneWikii DDX20.
    GenomeRNAii 11218.
    NextBioi 42699.
    PROi Q9UHI6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHI6.
    Bgeei Q9UHI6.
    CleanExi HS_DDX20.
    Genevestigatori Q9UHI6.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 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 PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and a component of gems."
      Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M., Dreyfuss G.
      J. Cell Biol. 147:1181-1194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE CORE SMN COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, IDENTIFICATION BY MASS SPECTROMETRY.
    2. "Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C."
      Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., Atz J., Mueller-Lantzsch N., Schubach W.H., Grasser F.A.
      J. Biol. Chem. 274:19136-19144(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EBV EBNA2 AND EBV EBNA3C.
    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] (ISOFORMS 1 AND 2).
      Tissue: Esophagus.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT THR-636.
      Tissue: Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275 (ISOFORM 1).
      Tissue: Testis.
    7. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
      Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
      Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNUPN; SMN1 AND SNRPB.
    8. "Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs."
      Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W.
      J. Cell Sci. 116:1905-1913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP4R2.
    9. "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis."
      Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y., Bae J.
      Biochem. Biophys. Res. Commun. 336:876-881(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXL2.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
      Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
      Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-552 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532; THR-552; SER-652; SER-654; SER-656; SER-677; SER-678; SER-703; THR-705 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "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-677; SER-678 AND SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-672; SER-678 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within chromatoid body in human germ cells."
      Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A., Kupryjanczyk J., Jaruzelska J.
      Histochem. Cell Biol. 136:279-287(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PUM2 AND NANOS1.
    19. "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-505; SER-672; SER-677 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein."
      Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., Schuler H.
      J. Mol. Biol. 400:768-782(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP, ADP-BINDING.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268.

    Entry informationi

    Entry nameiDDX20_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHI6
    Secondary accession number(s): B4DWV7
    , Q96F72, Q9NVM3, Q9UF59, Q9UIY0, Q9Y659
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 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 1
      Human chromosome 1: 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