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Q13206

- DDX10_HUMAN

UniProt

Q13206 - DDX10_HUMAN

Protein

Probable ATP-dependent RNA helicase DDX10

Gene

DDX10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Putative ATP-dependent RNA helicase.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi89 – 913ATP
    Nucleotide bindingi113 – 1208ATP

    GO - Molecular functioni

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

    GO - Biological processi

    1. metabolic process Source: GOC

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ATP-dependent RNA helicase DDX10 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 10
    Gene namesi
    Name:DDX10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2735. DDX10.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875Probable ATP-dependent RNA helicase DDX10PRO_0000055083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphothreonine1 Publication
    Modified residuei539 – 5391Phosphoserine3 Publications
    Modified residuei555 – 5551N6-acetyllysineBy similarity
    Modified residuei780 – 7801Phosphoserine1 Publication
    Modified residuei831 – 8311Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13206.
    PaxDbiQ13206.
    PeptideAtlasiQ13206.
    PRIDEiQ13206.

    2D gel databases

    SWISS-2DPAGEQ13206.

    PTM databases

    PhosphoSiteiQ13206.

    Expressioni

    Tissue specificityi

    High in testis but widely expressed.

    Gene expression databases

    ArrayExpressiQ13206.
    BgeeiQ13206.
    CleanExiHS_DDX10.
    GenevestigatoriQ13206.

    Organism-specific databases

    HPAiHPA004691.

    Interactioni

    Protein-protein interaction databases

    BioGridi108027. 6 interactions.
    IntActiQ13206. 1 interaction.
    MINTiMINT-2806286.
    STRINGi9606.ENSP00000314348.

    Structurei

    Secondary structure

    1
    875
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi47 – 5812
    Turni59 – 624
    Helixi65 – 673
    Helixi71 – 733
    Helixi78 – 869
    Helixi94 – 10411
    Beta strandi109 – 1124
    Helixi119 – 13315
    Helixi138 – 1403
    Beta strandi144 – 1474
    Helixi151 – 16414
    Turni165 – 1673
    Beta strandi172 – 1754
    Helixi182 – 1887
    Beta strandi192 – 1965
    Helixi198 – 20710
    Beta strandi218 – 2214
    Helixi224 – 2296
    Turni230 – 2323
    Helixi233 – 2419
    Beta strandi247 – 2559
    Helixi258 – 2669
    Beta strandi272 – 2754

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PL3X-ray2.15A47-280[»]
    ProteinModelPortaliQ13206.
    SMRiQ13206. Positions 47-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13206.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 274175Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 448162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi69 – 9729Q motifAdd
    BLAST
    Motifi222 – 2254DEAD box

    Domaini

    The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268801.
    HOVERGENiHBG102756.
    InParanoidiQ13206.
    KOiK14776.
    OMAiCCKEVQY.
    OrthoDBiEOG7GFB4K.
    PhylomeDBiQ13206.
    TreeFamiTF315215.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR025313. DUF4217.
    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.
    PF13959. DUF4217. 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]

    Sequencei

    Sequence statusi: Complete.

    Q13206-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKTANSPGS GARPDPVRSF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER    50
    ESISRLMQNY EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI 100
    GLALQGKDVL GAAKTGSGKT LAFLVPVLEA LYRLQWTSTD GLGVLIISPT 150
    RELAYQTFEV LRKVGKNHDF SAGLIIGGKD LKHEAERINN INILVCTPGR 200
    LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAVI ENLPKKRQTL 250
    LFSATQTKSV KDLARLSLKN PEYVWVHEKA KYSTPATLEQ NYIVCELQQK 300
    ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGV SILALHGRQQ 350
    QMRRMEVYNE FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI 400
    HRAGRTARYK EDGEALLILL PSEKAMVQQL LQKKVPVKEI KINPEKLIDV 450
    QKKLESILAQ DQDLKERAQR CFVSYVRSVY LMKDKEVFDV SKLPIPEYAL 500
    SLGLAVAPRV RFLQKMQKQP TKELVRSQAD KVIEPRAPSL TNDEVEEFRA 550
    YFNEKMSILQ KGGKRLEGTE HRQDNDTGNE EQEEEEDDEE EMEEKLAKAK 600
    GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKD 650
    EKTLQKKEPS KSSIKKKMTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW 700
    PQMQKSAIKD AEEDDDTGGI NLHKAKERLQ EEDKFDKEEY RKKIKAKHRE 750
    KRLKEREARR EANKRQAKAK DEEEAFLDWS DDDDDDDDGF DPSTLPDPDK 800
    YRSSEDSDSE DMENKISDTK KKQGMKKRSN SEVEDVGPTS HNRKKARWDT 850
    LEPLDTGLSL AEDEELVLHL LRSQS 875
    Length:875
    Mass (Da):100,888
    Last modified:September 27, 2005 - v2
    Checksum:iB61BF325921C62FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti647 – 6471D → A in AAC50823. (PubMed:8660968)Curated
    Sequence conflicti658 – 6581E → D in AAC50823. (PubMed:8660968)Curated
    Sequence conflicti661 – 6611K → N in AAC50823. (PubMed:8660968)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti566 – 5661L → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035840

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28042 mRNA. Translation: AAC50823.1.
    AB040537 mRNA. Translation: BAB18536.1.
    AK315216 mRNA. Translation: BAG37650.1.
    CH471065 Genomic DNA. Translation: EAW67122.1.
    BC091521 mRNA. Translation: AAH91521.1.
    BC093654 mRNA. Translation: AAH93654.1.
    BC093656 mRNA. Translation: AAH93656.1.
    CCDSiCCDS8342.1.
    RefSeqiNP_004389.2. NM_004398.3.
    UniGeneiHs.591931.

    Genome annotation databases

    EnsembliENST00000322536; ENSP00000314348; ENSG00000178105.
    GeneIDi1662.
    KEGGihsa:1662.
    UCSCiuc001pkm.3. human.

    Polymorphism databases

    DMDMi76803554.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28042 mRNA. Translation: AAC50823.1 .
    AB040537 mRNA. Translation: BAB18536.1 .
    AK315216 mRNA. Translation: BAG37650.1 .
    CH471065 Genomic DNA. Translation: EAW67122.1 .
    BC091521 mRNA. Translation: AAH91521.1 .
    BC093654 mRNA. Translation: AAH93654.1 .
    BC093656 mRNA. Translation: AAH93656.1 .
    CCDSi CCDS8342.1.
    RefSeqi NP_004389.2. NM_004398.3.
    UniGenei Hs.591931.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PL3 X-ray 2.15 A 47-280 [» ]
    ProteinModelPortali Q13206.
    SMRi Q13206. Positions 47-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108027. 6 interactions.
    IntActi Q13206. 1 interaction.
    MINTi MINT-2806286.
    STRINGi 9606.ENSP00000314348.

    PTM databases

    PhosphoSitei Q13206.

    Polymorphism databases

    DMDMi 76803554.

    2D gel databases

    SWISS-2DPAGE Q13206.

    Proteomic databases

    MaxQBi Q13206.
    PaxDbi Q13206.
    PeptideAtlasi Q13206.
    PRIDEi Q13206.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322536 ; ENSP00000314348 ; ENSG00000178105 .
    GeneIDi 1662.
    KEGGi hsa:1662.
    UCSCi uc001pkm.3. human.

    Organism-specific databases

    CTDi 1662.
    GeneCardsi GC11P108569.
    HGNCi HGNC:2735. DDX10.
    HPAi HPA004691.
    MIMi 601235. gene.
    neXtProti NX_Q13206.
    PharmGKBi PA27200.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268801.
    HOVERGENi HBG102756.
    InParanoidi Q13206.
    KOi K14776.
    OMAi CCKEVQY.
    OrthoDBi EOG7GFB4K.
    PhylomeDBi Q13206.
    TreeFami TF315215.

    Miscellaneous databases

    ChiTaRSi DDX10. human.
    EvolutionaryTracei Q13206.
    GeneWikii DDX10.
    GenomeRNAii 1662.
    NextBioi 6838.
    PROi Q13206.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13206.
    Bgeei Q13206.
    CleanExi HS_DDX10.
    Genevestigatori Q13206.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR025313. DUF4217.
    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.
    PF13959. DUF4217. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular analysis of the chromosomal breakpoints and identification of the repetitive sequences near the breakpoints of NUP98 in therapy-related leukemia with inv(11)(p15q22)."
      Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Cerebellum.
    4. 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].
      Tissue: Testis.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-831, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "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-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 47-280 IN COMPLEX WITH ADP.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-566.

    Entry informationi

    Entry nameiDDX10_HUMAN
    AccessioniPrimary (citable) accession number: Q13206
    Secondary accession number(s): B2RCQ3, Q5BJD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 133 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 11
      Human chromosome 11: 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