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Protein

Probable ATP-dependent RNA helicase DDX10

Gene

DDX10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • RNA helicase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2735. DDX10.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27200.

Polymorphism and mutation databases

BioMutaiDDX10.
DMDMi76803554.

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

BgeeiQ13206.
CleanExiHS_DDX10.
ExpressionAtlasiQ13206. baseline and differential.
GenevisibleiQ13206. HS.

Organism-specific databases

HPAiHPA004691.

Interactioni

Protein-protein interaction databases

BioGridi108027. 20 interactions.
IntActiQ13206. 3 interactions.
MINTiMINT-2806286.
STRINGi9606.ENSP00000314348.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PL3X-ray2.15A47-280[»]
ProteinModelPortaliQ13206.
SMRiQ13206. Positions 23-516.
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.
GeneTreeiENSGT00550000074980.
HOGENOMiHOG000268801.
HOVERGENiHBG102756.
InParanoidiQ13206.
KOiK14776.
OMAiTSHNRKK.
OrthoDBiEOG7GFB4K.
PhylomeDBiQ13206.
TreeFamiTF315215.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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

        10         20         30         40         50
MGKTANSPGS GARPDPVRSF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER
60 70 80 90 100
ESISRLMQNY EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI
110 120 130 140 150
GLALQGKDVL GAAKTGSGKT LAFLVPVLEA LYRLQWTSTD GLGVLIISPT
160 170 180 190 200
RELAYQTFEV LRKVGKNHDF SAGLIIGGKD LKHEAERINN INILVCTPGR
210 220 230 240 250
LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAVI ENLPKKRQTL
260 270 280 290 300
LFSATQTKSV KDLARLSLKN PEYVWVHEKA KYSTPATLEQ NYIVCELQQK
310 320 330 340 350
ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGV SILALHGRQQ
360 370 380 390 400
QMRRMEVYNE FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI
410 420 430 440 450
HRAGRTARYK EDGEALLILL PSEKAMVQQL LQKKVPVKEI KINPEKLIDV
460 470 480 490 500
QKKLESILAQ DQDLKERAQR CFVSYVRSVY LMKDKEVFDV SKLPIPEYAL
510 520 530 540 550
SLGLAVAPRV RFLQKMQKQP TKELVRSQAD KVIEPRAPSL TNDEVEEFRA
560 570 580 590 600
YFNEKMSILQ KGGKRLEGTE HRQDNDTGNE EQEEEEDDEE EMEEKLAKAK
610 620 630 640 650
GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKD
660 670 680 690 700
EKTLQKKEPS KSSIKKKMTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW
710 720 730 740 750
PQMQKSAIKD AEEDDDTGGI NLHKAKERLQ EEDKFDKEEY RKKIKAKHRE
760 770 780 790 800
KRLKEREARR EANKRQAKAK DEEEAFLDWS DDDDDDDDGF DPSTLPDPDK
810 820 830 840 850
YRSSEDSDSE DMENKISDTK KKQGMKKRSN SEVEDVGPTS HNRKKARWDT
860 870
LEPLDTGLSL AEDEELVLHL LRSQS
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PL3X-ray2.15A47-280[»]
ProteinModelPortaliQ13206.
SMRiQ13206. Positions 23-516.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108027. 20 interactions.
IntActiQ13206. 3 interactions.
MINTiMINT-2806286.
STRINGi9606.ENSP00000314348.

PTM databases

PhosphoSiteiQ13206.

Polymorphism and mutation databases

BioMutaiDDX10.
DMDMi76803554.

2D gel databases

SWISS-2DPAGEQ13206.

Proteomic databases

MaxQBiQ13206.
PaxDbiQ13206.
PeptideAtlasiQ13206.
PRIDEiQ13206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1662.
GeneCardsiGC11P108569.
HGNCiHGNC:2735. DDX10.
HPAiHPA004691.
MIMi601235. gene.
neXtProtiNX_Q13206.
PharmGKBiPA27200.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00550000074980.
HOGENOMiHOG000268801.
HOVERGENiHBG102756.
InParanoidiQ13206.
KOiK14776.
OMAiTSHNRKK.
OrthoDBiEOG7GFB4K.
PhylomeDBiQ13206.
TreeFamiTF315215.

Miscellaneous databases

ChiTaRSiDDX10. human.
EvolutionaryTraceiQ13206.
GeneWikiiDDX10.
GenomeRNAii1662.
NextBioi6838.
PROiQ13206.
SOURCEiSearch...

Gene expression databases

BgeeiQ13206.
CleanExiHS_DDX10.
ExpressionAtlasiQ13206. baseline and differential.
GenevisibleiQ13206. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.