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Protein

ATP-dependent DNA helicase DDX11

Gene

DDX11

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

Functioni

DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis (PubMed:10648783, PubMed:21854770, PubMed:23797032, PubMed:26089203, PubMed:26503245). Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction (PubMed:18499658, PubMed:22102414). The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities (PubMed:18499658). Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules (PubMed:22102414, PubMed:26503245). Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage (PubMed:23797032). Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (PubMed:26503245). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17105772, PubMed:18499658, PubMed:20124417, PubMed:23116066, PubMed:23797032). Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis (PubMed:18499658). Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (PubMed:27477908). Plays also a role in heterochromatin organization (PubMed:21854770). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (PubMed:26089203). Plays a role in embryonic development and prevention of aneuploidy (By similarity). Involved in melanoma cell proliferation and survival (PubMed:23116066). Associates with chromatin at DNA replication fork regions (PubMed:27477908). Binds to single- and double-stranded DNAs (PubMed:9013641, PubMed:18499658, PubMed:22102414).By similarity11 Publications
(Microbial infection) Required for bovine papillomavirus type 1 regulatory protein E2 loading onto mitotic chromosomes during DNA replication for the viral genome to be maintained and segragated.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.5 Publications

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Enzyme regulationi

ATPase activity is stimulated by high magnesium salt levels (up to a 0.1 M), and potassium salts (glutamate, chloride or acetate) are more effective than the corresponding sodium salts (PubMed:10648783, PubMed:18499658). ATPase activity is enhanced by the long non-coding RNA (lncRNA) cohesion regulator noncoding RNA (CONCR) (PubMed:27477908). Double-stranded DNA helicase activity is maximal with magnesium ions at low concentrations (0.5-1 mM) whereas is markedly inhibited at higher levels (5 mM and above) (PubMed:10648783, PubMed:18499658). Double-stranded DNA helicase activity is stimulated by 25-50 mM potassium acetate, stimulated to a lesser extent by 25 mM of ammonium acetate, and markedly inhibited by sodium acetate (PubMed:18499658).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi267Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi285Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi315Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi350Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 51ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • ATP-dependent helicase activity Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-dependent ATPase activity Source: UniProtKB
  • DNA replication origin binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • G-quadruplex DNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA-dependent ATPase activity Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • triplex DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to bleomycin Source: UniProtKB
  • cellular response to cisplatin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydroxyurea Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
  • DNA repair Source: UniProtKB-KW
  • G-quadruplex DNA unwinding Source: UniProtKB
  • IRE1-mediated unfolded protein response Source: Reactome
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of protein binding Source: UniProtKB
  • nucleolar chromatin organization Source: UniProtKB
  • positive regulation of chromatin binding Source: UniProtKB
  • positive regulation of double-strand break repair Source: UniProtKB
  • positive regulation of endodeoxyribonuclease activity Source: UniProtKB
  • positive regulation of sister chromatid cohesion Source: UniProtKB
  • positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProtKB
  • replication fork processing Source: UniProtKB
  • sister chromatid cohesion Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase DDX11Curated (EC:3.6.4.125 Publications)
Alternative name(s):
CHL1-related protein 11 Publication
Short name:
hCHLR11 Publication
DEAD/H-box protein 11Imported
Keratinocyte growth factor-regulated gene 2 protein1 Publication
Short name:
KRG-21 Publication
Gene namesi
Name:DDX11Imported
Synonyms:CHL1, CHLR11 Publication, KRG21 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2736. DDX11.

Subcellular locationi

  • Chromosome 1 Publication

  • Note: (Microbial infection) Colocalizes with bovine papillomavirus type 1 regulatory protein E2 on mitotic chromosomes at early stages of mitosis.1 Publication

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • extracellular exosome Source: UniProtKB
  • midbody Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Warsaw breakage syndrome (WBRS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by severe microcephaly, pre- and postnatal growth retardation, facial dysmorphism and abnormal skin pigmentation. Additional features include high arched palate, coloboma of the right optic disk, deafness, ventricular septal defect, toes and fingers abnormalities. At cellular level, drug-induced chromosomal breakage, a feature of Fanconi anemia, and sister chromatid cohesion defects, a feature of Roberts syndrome, coexist.
See also OMIM:613398
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069099263R → Q in WBRS; impairs the helicase activity by perturbing its DNA binding and DNA-dependent ATPase activity; reduces binding to rDNA promoter and promotion of rDNA transcription. 2 PublicationsCorresponds to variant rs201968272dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi50K → R: Loss of both DNA-dependent ATPase and ATP-dependent helicase activities. 3 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1663.
MalaCardsiDDX11.
MIMi613398. phenotype.
OpenTargetsiENSG00000013573.
Orphaneti280558. Warsaw breakage syndrome.
PharmGKBiPA27201.

Polymorphism and mutation databases

BioMutaiDDX11.
DMDMi74731686.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551361 – 970ATP-dependent DNA helicase DDX11Add BLAST970

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei262PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96FC9.
MaxQBiQ96FC9.
PaxDbiQ96FC9.
PeptideAtlasiQ96FC9.
PRIDEiQ96FC9.

PTM databases

iPTMnetiQ96FC9.
PhosphoSitePlusiQ96FC9.

Expressioni

Tissue specificityi

Expressed in melanoma cells. Not detected in epidermal melanocytes of normal skin (at protein level) (PubMed:23116066). Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine and pancreas (PubMed:9013641). Very low expression seen in brain (PubMed:9013641). Expressed in dividing cells and/or cells undergoing high levels of recombination (PubMed:9013641). No expression detected in cells signaled to terminally differentiate (PubMed:9013641). Expressed weakly in keratinocytes (PubMed:8798685).3 Publications

Inductioni

Up-regulated by serum (at protein level) (PubMed:26089203). Up-regulated by fibroblast growth factor FGF7 (PubMed:8798685). Expressed in keratinocyte growth factor-stimulated cells but not in EGF and IL1-beta-treated keratinocytes (PubMed:8798685). Up-regulated with progression from noninvasive to invasive melanoma (PubMed:23116066).3 Publications

Gene expression databases

BgeeiENSG00000013573.
CleanExiHS_CHL1.
HS_DDX11.
ExpressionAtlasiQ96FC9. baseline and differential.
GenevisibleiQ96FC9. HS.

Organism-specific databases

HPAiHPA047228.
HPA065197.

Interactioni

Subunit structurei

Associates with the CTF18-RFC complex (PubMed:18499658). Associates with a cohesin complex composed of RAD21, SMC1 proteins and SMC3 (PubMed:17105772). Interacts with CHTF18 (PubMed:18499658). Interacts with DSCC1 (PubMed:18499658). Interacts with FEN1; this interaction is direct and increases flap endonuclease activity of FEN1 (PubMed:18499658). Interacts with PCNA (PubMed:18499658). Interacts with POLR1A and UBTF (PubMed:26089203). Interacts with RAD21, SMC1 proteins and SMC3 (PubMed:17105772). Interacts with RFC2 (PubMed:18499658). Interacts with TIMELESS; this interaction increases recruitment of both proteins onto chromatin in response to replication stress induction by hydroxyurea (PubMed:20124417, PubMed:26503245).5 Publications
(Microbial infection) Interacts with bovine papillomavirus type 1 regulatory protein E2; this interaction stimulates the recruitment of E2 onto mitotic chromosomes.1 Publication

Protein-protein interaction databases

BioGridi108028. 30 interactors.
IntActiQ96FC9. 5 interactors.
MINTiMINT-1371028.
STRINGi9606.ENSP00000384703.

Structurei

3D structure databases

ProteinModelPortaliQ96FC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 445Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST437

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi393 – 396DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi163 – 224Glu-richAdd BLAST62

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1133. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
HOVERGENiHBG058884.
InParanoidiQ96FC9.
KOiK11273.
OMAiNLCQVIP.
OrthoDBiEOG091G034C.
PhylomeDBiQ96FC9.
TreeFamiTF300435.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96FC9-1) [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

        10         20         30         40         50
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK
60 70 80 90 100
SLSLICGALS WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG
110 120 130 140 150
AAGTPRPAGE PAWVTQFVQK KEERDLVDRL KAEQARRKQR EERLQQLQHR
160 170 180 190 200
VQLKYAAKRL RQEEEERENL LRLSREMLET GPEAERLEQL ESGEEELVLA
210 220 230 240 250
EYESDEEKKV ASRVDEDEDD LEEEHITKIY YCSRTHSQLA QFVHEVKKSP
260 270 280 290 300
FGKDVRLVSL GSRQNLCVNE DVKSLGSVQL INDRCVDMQR SRHEKKKGAE
310 320 330 340 350
EEKPKRRRQE KQAACPFYNH EQMGLLRDEA LAEVKDMEQL LALGKEARAC
360 370 380 390 400
PYYGSRLAIP AAQLVVLPYQ MLLHAATRQA AGIRLQDQVV IIDEAHNLID
410 420 430 440 450
TITGMHSVEV SGSQLCQAHS QLLQYVERYG KRLKAKNLMY LKQILYLLEK
460 470 480 490 500
FVAVLGGNIK QNPNTQSLSQ TGTELKTIND FLFQSQIDNI NLFKVQRYCE
510 520 530 540 550
KSMISRKLFG FTERYGAVFS SREQPKLAGF QQFLQSLQPR TTEALAAPAD
560 570 580 590 600
ESQASTLRPA SPLMHIQGFL AALTTANQDG RVILSRQGSL SQSTLKFLLL
610 620 630 640 650
NPAVHFAQVV KECRAVVIAG GTMQPVSDFR QQLLACAGVE AERVVEFSCG
660 670 680 690 700
HVIPPDNILP LVICSGISNQ PLEFTFQKRE LPQMMDEVGR ILCNLCGVVP
710 720 730 740 750
GGVVCFFPSY EYLRQVHAHW EKGGLLGRLA ARKKIFQEPK SAHQVEQVLL
760 770 780 790 800
AYSRCIQACG QERGQVTGAL LLSVVGGKMS EGINFSDNLG RCVVMVGMPF
810 820 830 840 850
PNIRSAELQE KMAYLDQTLS PRPGTPREGS GGEPVHEGRQ PVHRQGHQAP
860 870 880 890 900
EGFCQRSAPG PAICPAPCPG QAAGLDPSPC GGQSYLWPRH CCCAEVSPGE
910 920 930 940 950
VGLFLMGNHT TAWRRALPLS CPLETVFVVG VVCGDPVTKV KPRRRVWSPE
960 970
CCQDPGTGVS SRRRKWGNPE
Length:970
Mass (Da):108,313
Last modified:December 1, 2001 - v1
Checksum:i5BF49FE74E912B48
GO
Isoform 2 (identifier: Q96FC9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.

Show »
Length:906
Mass (Da):101,685
Checksum:iBC51D55CB3186C91
GO
Isoform 3 (identifier: Q96FC9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.

Show »
Length:880
Mass (Da):98,687
Checksum:iE0D7B88158ABA02A
GO
Isoform 4 (identifier: Q96FC9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     685-734: Missing.
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.

Show »
Length:856
Mass (Da):96,128
Checksum:i30C866F69D6ABD34
GO
Isoform 5 (identifier: Q96FC9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     214-288: VDEDEDDLEE...QLINDRCVDM → APSDATSSRH...RMRMTWRKNT
     289-970: Missing.

Show »
Length:288
Mass (Da):32,951
Checksum:i78E0917712BBC6B0
GO

Sequence cautioni

The sequence CAA67895 differs from that shown. Reason: Frameshift at positions 644 and 648.Curated
The sequence CAA67895 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02480839I → S.1 PublicationCorresponds to variant rs1046454dbSNPEnsembl.1
Natural variantiVAR_069099263R → Q in WBRS; impairs the helicase activity by perturbing its DNA binding and DNA-dependent ATPase activity; reduces binding to rDNA promoter and promotion of rDNA transcription. 2 PublicationsCorresponds to variant rs201968272dbSNPEnsembl.1
Natural variantiVAR_024809567Q → E.2 PublicationsCorresponds to variant rs2075322dbSNPEnsembl.1
Natural variantiVAR_024810575T → M.1 PublicationCorresponds to variant rs17857386dbSNPEnsembl.1
Natural variantiVAR_052175856R → H.Corresponds to variant rs1046457dbSNPEnsembl.1
Natural variantiVAR_052176864C → R.Corresponds to variant rs3893679dbSNPEnsembl.1
Natural variantiVAR_052177951C → R.Corresponds to variant rs1046458dbSNPEnsembl.1
Natural variantiVAR_052178966W → C.Corresponds to variant rs14330dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0168601 – 26Missing in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_016861214 – 288VDEDE…RCVDM → APSDATSSRHPPDASFPAAL NFLQRTRPSSVLSEDLLMQR AVAKHPALLPWQMSSSPLRP GSEWMRMRMTWRKNT in isoform 5. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_016862289 – 970Missing in isoform 5. 1 PublicationAdd BLAST682
Alternative sequenceiVSP_016863685 – 734Missing in isoform 4. 1 PublicationAdd BLAST50
Alternative sequenceiVSP_016864820 – 906SPRPG…GLFLM → PRAPGQAPPGKALVENLCMK AVNQSIGRAIRHQKDFASVV LLDQRYARPPVLAKLPAWIR ARVEVKATFGPAIAAVQKFH REKSASS in isoform 2, isoform 3 and isoform 4. 4 PublicationsAdd BLAST87
Alternative sequenceiVSP_016865907 – 970Missing in isoform 2, isoform 3 and isoform 4. 4 PublicationsAdd BLAST64

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99583 mRNA. Translation: CAA67895.1. Sequence problems.
U33833 mRNA. Translation: AAB06962.1.
U75967 mRNA. Translation: AAB18749.1.
U75968 mRNA. Translation: AAB18750.1.
BC050069 mRNA. Translation: AAH50069.1.
BC050522 mRNA. Translation: AAH50522.1.
CCDSiCCDS41767.1. [Q96FC9-2]
CCDS44856.1. [Q96FC9-1]
CCDS58224.1. [Q96FC9-3]
CCDS8721.1. [Q96FC9-4]
PIRiG02071.
RefSeqiNP_001244073.1. NM_001257144.1. [Q96FC9-1]
NP_001244074.1. NM_001257145.1. [Q96FC9-3]
NP_004390.3. NM_004399.2. [Q96FC9-4]
NP_689651.1. NM_152438.1. [Q96FC9-1]
XP_016874421.1. XM_017018932.1. [Q96FC9-2]
UniGeneiHs.443960.

Genome annotation databases

EnsembliENST00000228264; ENSP00000228264; ENSG00000013573. [Q96FC9-3]
ENST00000350437; ENSP00000309965; ENSG00000013573. [Q96FC9-4]
ENST00000435753; ENSP00000406799; ENSG00000013573. [Q96FC9-5]
ENST00000542838; ENSP00000443426; ENSG00000013573. [Q96FC9-2]
ENST00000545668; ENSP00000440402; ENSG00000013573. [Q96FC9-1]
GeneIDi1663.
KEGGihsa:1663.
UCSCiuc001rjr.2. human. [Q96FC9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

DEAD/H (Asp-Glu-Ala-Asp/His) box helicase 11 (DDX11)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99583 mRNA. Translation: CAA67895.1. Sequence problems.
U33833 mRNA. Translation: AAB06962.1.
U75967 mRNA. Translation: AAB18749.1.
U75968 mRNA. Translation: AAB18750.1.
BC050069 mRNA. Translation: AAH50069.1.
BC050522 mRNA. Translation: AAH50522.1.
CCDSiCCDS41767.1. [Q96FC9-2]
CCDS44856.1. [Q96FC9-1]
CCDS58224.1. [Q96FC9-3]
CCDS8721.1. [Q96FC9-4]
PIRiG02071.
RefSeqiNP_001244073.1. NM_001257144.1. [Q96FC9-1]
NP_001244074.1. NM_001257145.1. [Q96FC9-3]
NP_004390.3. NM_004399.2. [Q96FC9-4]
NP_689651.1. NM_152438.1. [Q96FC9-1]
XP_016874421.1. XM_017018932.1. [Q96FC9-2]
UniGeneiHs.443960.

3D structure databases

ProteinModelPortaliQ96FC9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108028. 30 interactors.
IntActiQ96FC9. 5 interactors.
MINTiMINT-1371028.
STRINGi9606.ENSP00000384703.

PTM databases

iPTMnetiQ96FC9.
PhosphoSitePlusiQ96FC9.

Polymorphism and mutation databases

BioMutaiDDX11.
DMDMi74731686.

Proteomic databases

EPDiQ96FC9.
MaxQBiQ96FC9.
PaxDbiQ96FC9.
PeptideAtlasiQ96FC9.
PRIDEiQ96FC9.

Protocols and materials databases

DNASUi1663.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228264; ENSP00000228264; ENSG00000013573. [Q96FC9-3]
ENST00000350437; ENSP00000309965; ENSG00000013573. [Q96FC9-4]
ENST00000435753; ENSP00000406799; ENSG00000013573. [Q96FC9-5]
ENST00000542838; ENSP00000443426; ENSG00000013573. [Q96FC9-2]
ENST00000545668; ENSP00000440402; ENSG00000013573. [Q96FC9-1]
GeneIDi1663.
KEGGihsa:1663.
UCSCiuc001rjr.2. human. [Q96FC9-1]

Organism-specific databases

CTDi1663.
DisGeNETi1663.
GeneCardsiDDX11.
HGNCiHGNC:2736. DDX11.
HPAiHPA047228.
HPA065197.
MalaCardsiDDX11.
MIMi601150. gene.
613398. phenotype.
neXtProtiNX_Q96FC9.
OpenTargetsiENSG00000013573.
Orphaneti280558. Warsaw breakage syndrome.
PharmGKBiPA27201.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1133. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
HOVERGENiHBG058884.
InParanoidiQ96FC9.
KOiK11273.
OMAiNLCQVIP.
OrthoDBiEOG091G034C.
PhylomeDBiQ96FC9.
TreeFamiTF300435.

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

GeneWikiiDDX11.
GenomeRNAii1663.
PROiQ96FC9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000013573.
CleanExiHS_CHL1.
HS_DDX11.
ExpressionAtlasiQ96FC9. baseline and differential.
GenevisibleiQ96FC9. HS.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDX11_HUMAN
AccessioniPrimary (citable) accession number: Q96FC9
Secondary accession number(s): Q13333
, Q86VQ4, Q86W62, Q92498, Q92770, Q92998, Q92999
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 137 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.