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Q96FC9 (DDX11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable ATP-dependent RNA helicase DDX11

EC=3.6.4.13
Alternative name(s):
CHL1-related protein 1
Short name=hCHLR1
DEAD/H box protein 11
Keratinocyte growth factor-regulated gene 2 protein
Short name=KRG-2
Gene names
Name:DDX11
Synonyms:CHL1, CHLR1, KRG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length970 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitment of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA. Ref.2 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.5

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Enzyme regulation

Helicase shows maximal activity with magnesium ions at low concentrations (0.5-1mM) whereas is markedly inhibited at higher levels (5 mM and above). Stimulated by 25-50 mM potassium acetate, stimulated to a lesser extent by 25 mM of ammonium acetate, and markedly inhibited by sodium acetate. The ATPase activity is stimulated by high salt levels (up to a 0.1 M) and potassium salts (glutamate, chloride or acetate) are more effective than the corresponding sodium salts. Ref.8

Subunit structure

Interacts with the CTF18-RFC complex, PCNA and FEN1. Forms a complex with RAD21, SMC1 and SMC3. Interacts with bovine papillomavirus type 1 regulatory protein E2. Ref.7 Ref.8

Subcellular location

Nucleus. Nucleusnucleolus. Note: During the early stages of mitosis, localizes to condensed chromatin and is released from the chromatin with progression to metaphase. Also localizes to the spindle poles throughout mitosis and at the midbody at later stages of mitosis (metaphase to telophase). Co-localizes with bovine papillomavirus type 1 regulatory protein E2 at early stages of mitosis. Ref.6

Tissue specificity

Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes. Ref.1 Ref.2

Involvement in disease

Warsaw breakage syndrome (WBRS) [MIM:613398]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.12

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.

Contains 1 helicase ATP-binding domain.

Sequence caution

The sequence CAA67895.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA67895.1 differs from that shown. Reason: Frameshift at positions 644 and 648.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Ligand4Fe-4S
ATP-binding
DNA-binding
Iron
Iron-sulfur
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.8. Source: GOC

DNA duplex unwinding

Traceable author statement Ref.2. Source: GOC

G2/M transition of mitotic cell cycle

Traceable author statement Ref.2. Source: ProtInc

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

mitotic S phase

Traceable author statement Ref.2. Source: ProtInc

mitotic sister chromatid segregation

Traceable author statement Ref.2. Source: ProtInc

positive regulation of cell proliferation

Traceable author statement Ref.2. Source: ProtInc

sister chromatid cohesion

Inferred from direct assay Ref.6. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmidbody

Inferred from direct assay Ref.6. Source: UniProtKB

nuclear chromatin

Inferred from direct assay Ref.6. Source: UniProtKB

nucleolus

Traceable author statement Ref.2. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spindle pole

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Traceable author statement Ref.2. Source: ProtInc

DNA-dependent ATPase activity

Inferred from direct assay Ref.8. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

helicase activity

Inferred from direct assay Ref.8. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96FC9-1)

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.
Isoform 2 (identifier: Q96FC9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.
Isoform 3 (identifier: Q96FC9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.
Isoform 4 (identifier: Q96FC9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     685-734: Missing.
     820-906: SPRPGTPREG...SPGEVGLFLM → PRAPGQAPPG...KFHREKSASS
     907-970: Missing.
Isoform 5 (identifier: Q96FC9-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 970970Probable ATP-dependent RNA helicase DDX11
PRO_0000055136

Regions

Domain9 – 445437Helicase ATP-binding
Nucleotide binding44 – 518ATP By similarity
Motif393 – 3964DEAH
Compositional bias163 – 22462Glu-rich

Sites

Metal binding2671Iron-sulfur (4Fe-4S) By similarity
Metal binding2851Iron-sulfur (4Fe-4S) By similarity
Metal binding3151Iron-sulfur (4Fe-4S) By similarity
Metal binding3501Iron-sulfur (4Fe-4S) By similarity

Natural variations

Alternative sequence1 – 2626Missing in isoform 3.
VSP_016860
Alternative sequence214 – 28875VDEDE…RCVDM → APSDATSSRHPPDASFPAAL NFLQRTRPSSVLSEDLLMQR AVAKHPALLPWQMSSSPLRP GSEWMRMRMTWRKNT in isoform 5.
VSP_016861
Alternative sequence289 – 970682Missing in isoform 5.
VSP_016862
Alternative sequence685 – 73450Missing in isoform 4.
VSP_016863
Alternative sequence820 – 90687SPRPG…GLFLM → PRAPGQAPPGKALVENLCMK AVNQSIGRAIRHQKDFASVV LLDQRYARPPVLAKLPAWIR ARVEVKATFGPAIAAVQKFH REKSASS in isoform 2, isoform 3 and isoform 4.
VSP_016864
Alternative sequence907 – 97064Missing in isoform 2, isoform 3 and isoform 4.
VSP_016865
Natural variant391I → S. Ref.1
Corresponds to variant rs1046454 [ dbSNP | Ensembl ].
VAR_024808
Natural variant2631R → Q in WBRS; impairs the enzyme helicase activity by perturbing its DNA binding and DNA-dependent ATP hydrolysis. Ref.12
VAR_069099
Natural variant5671Q → E. Ref.2 Ref.3
Corresponds to variant rs2075322 [ dbSNP | Ensembl ].
VAR_024809
Natural variant5751T → M. Ref.3
Corresponds to variant rs17857386 [ dbSNP | Ensembl ].
VAR_024810
Natural variant8561R → H.
Corresponds to variant rs1046457 [ dbSNP | Ensembl ].
VAR_052175
Natural variant8641C → R.
Corresponds to variant rs3893679 [ dbSNP | Ensembl ].
VAR_052176
Natural variant9511C → R.
Corresponds to variant rs1046458 [ dbSNP | Ensembl ].
VAR_052177
Natural variant9661W → C.
Corresponds to variant rs14330 [ dbSNP | Ensembl ].
VAR_052178

Experimental info

Mutagenesis501K → R: Loss of both helicase and ATPase activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 5BF49FE74E912B48

FASTA970108,313
        10         20         30         40         50         60 
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK SLSLICGALS 

        70         80         90        100        110        120 
WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG AAGTPRPAGE PAWVTQFVQK 

       130        140        150        160        170        180 
KEERDLVDRL KAEQARRKQR EERLQQLQHR VQLKYAAKRL RQEEEERENL LRLSREMLET 

       190        200        210        220        230        240 
GPEAERLEQL ESGEEELVLA EYESDEEKKV ASRVDEDEDD LEEEHITKIY YCSRTHSQLA 

       250        260        270        280        290        300 
QFVHEVKKSP FGKDVRLVSL GSRQNLCVNE DVKSLGSVQL INDRCVDMQR SRHEKKKGAE 

       310        320        330        340        350        360 
EEKPKRRRQE KQAACPFYNH EQMGLLRDEA LAEVKDMEQL LALGKEARAC PYYGSRLAIP 

       370        380        390        400        410        420 
AAQLVVLPYQ MLLHAATRQA AGIRLQDQVV IIDEAHNLID TITGMHSVEV SGSQLCQAHS 

       430        440        450        460        470        480 
QLLQYVERYG KRLKAKNLMY LKQILYLLEK FVAVLGGNIK QNPNTQSLSQ TGTELKTIND 

       490        500        510        520        530        540 
FLFQSQIDNI NLFKVQRYCE KSMISRKLFG FTERYGAVFS SREQPKLAGF QQFLQSLQPR 

       550        560        570        580        590        600 
TTEALAAPAD ESQASTLRPA SPLMHIQGFL AALTTANQDG RVILSRQGSL SQSTLKFLLL 

       610        620        630        640        650        660 
NPAVHFAQVV KECRAVVIAG GTMQPVSDFR QQLLACAGVE AERVVEFSCG HVIPPDNILP 

       670        680        690        700        710        720 
LVICSGISNQ PLEFTFQKRE LPQMMDEVGR ILCNLCGVVP GGVVCFFPSY EYLRQVHAHW 

       730        740        750        760        770        780 
EKGGLLGRLA ARKKIFQEPK SAHQVEQVLL AYSRCIQACG QERGQVTGAL LLSVVGGKMS 

       790        800        810        820        830        840 
EGINFSDNLG RCVVMVGMPF PNIRSAELQE KMAYLDQTLS PRPGTPREGS GGEPVHEGRQ 

       850        860        870        880        890        900 
PVHRQGHQAP EGFCQRSAPG PAICPAPCPG QAAGLDPSPC GGQSYLWPRH CCCAEVSPGE 

       910        920        930        940        950        960 
VGLFLMGNHT TAWRRALPLS CPLETVFVVG VVCGDPVTKV KPRRRVWSPE CCQDPGTGVS 

       970 
SRRRKWGNPE 

« Hide

Isoform 2 [UniParc].

Checksum: BC51D55CB3186C91
Show »

FASTA906101,685
Isoform 3 [UniParc].

Checksum: E0D7B88158ABA02A
Show »

FASTA88098,687
Isoform 4 [UniParc].

Checksum: 30C866F69D6ABD34
Show »

FASTA85696,128
Isoform 5 [UniParc].

Checksum: 78E0917712BBC6B0
Show »

FASTA28832,951

References

« Hide 'large scale' references
[1]"The human homologue of the yeast CHL1 gene is a novel keratinocyte growth factor regulated gene."
Frank S., Werner S.
J. Biol. Chem. 271:24337-24340(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, INDUCTION, VARIANT SER-39.
Tissue: Keratinocyte.
[2]"Characterization of putative human homologues of the yeast chromosome transmission fidelity gene, CHL1."
Amann J., Kidd V.J., Lahti J.M.
J. Biol. Chem. 272:3823-3832(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, VARIANT GLU-567.
[3]"Isolation and characterization of the human homologue of the yeast CHL1 gene."
Ouellette M.M., Wright W.E., Shay J.W.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), VARIANTS GLU-567 AND MET-575.
[4]"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] (ISOFORMS 1 AND 3).
Tissue: Testis and Uterus.
[5]"Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase."
Hirota Y., Lahti J.M.
Nucleic Acids Res. 28:917-924(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, FUNCTION.
[6]"The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells."
Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J.
J. Cell Sci. 119:4857-4865(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, COMPLEX FORMATION WITH RAD21; SMC1 AND SMC3.
[7]"ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes and viral genome maintenance."
Parish J.L., Bean A.M., Park R.B., Androphy E.J.
Mol. Cell 24:867-876(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOVINE PAPILLOMAVIRUS TYPE 1 REGULATORY PROTEIN E2.
[8]"Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1."
Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., Hurwitz J.
J. Biol. Chem. 283:20925-20936(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH FEN1, PCNA AND CTF18-RFC COMPLEX, MUTAGENESIS OF LYS-50.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Warsaw breakage syndrome, a cohesinopathy associated with mutations in the XPD helicase family member DDX11/ChlR1."
van der Lelij P., Chrzanowska K.H., Godthelp B.C., Rooimans M.A., Oostra A.B., Stumm M., Zdzienicka M.Z., Joenje H., de Winter J.P.
Am. J. Hum. Genet. 86:262-266(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN WBRS.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Identification and biochemical characterization of a novel mutation in DDX11 causing warsaw breakage syndrome."
Capo-Chichi J.M., Bharti S.K., Sommers J.A., Yammine T., Chouery E., Patry L., Rouleau G.A., Samuels M.E., Hamdan F.F., Michaud J.L., Brosh R.M. Jr., Megarbane A., Kibar Z.
Hum. Mutat. 34:103-107(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WBRS GLN-263, CHARACTERIZATION OF VARIANT WBRS GLN-263.
+Additional computationally mapped references.

Web resources

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

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRG02071.
RefSeqNP_001244073.1. NM_001257144.1.
NP_001244074.1. NM_001257145.1.
NP_004390.3. NM_004399.2.
NP_689651.1. NM_152438.1.
UniGeneHs.443960.

3D structure databases

ProteinModelPortalQ96FC9.
SMRQ96FC9. Positions 14-53, 224-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108028. 9 interactions.
IntActQ96FC9. 2 interactions.
MINTMINT-1371028.
STRING9606.ENSP00000384703.

PTM databases

PhosphoSiteQ96FC9.

Polymorphism databases

DMDM74731686.

Proteomic databases

PaxDbQ96FC9.
PRIDEQ96FC9.

Protocols and materials databases

DNASU1663.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228264; ENSP00000228264; ENSG00000013573. [Q96FC9-3]
ENST00000251758; ENSP00000251758; ENSG00000013573. [Q96FC9-5]
ENST00000350437; ENSP00000309965; ENSG00000013573. [Q96FC9-4]
ENST00000407793; ENSP00000384703; ENSG00000013573. [Q96FC9-1]
ENST00000435753; ENSP00000406799; ENSG00000013573. [Q96FC9-5]
ENST00000542838; ENSP00000443426; ENSG00000013573. [Q96FC9-2]
ENST00000545668; ENSP00000440402; ENSG00000013573. [Q96FC9-1]
GeneID1663.
KEGGhsa:1663.
UCSCuc001rjr.1. human. [Q96FC9-2]
uc001rjs.1. human. [Q96FC9-4]
uc001rjt.1. human. [Q96FC9-1]
uc001rju.1. human. [Q96FC9-3]

Organism-specific databases

CTD1663.
GeneCardsGC12P031226.
HGNCHGNC:2736. DDX11.
HPAHPA047228.
HPA049167.
MIM601150. gene.
613398. phenotype.
neXtProtNX_Q96FC9.
Orphanet280558. Warsaw breakage syndrome.
PharmGKBPA27201.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1199.
HOVERGENHBG058884.
InParanoidQ96FC9.
KOK11273.
OMAELYENMC.
OrthoDBEOG7ZD1TW.
PhylomeDBQ96FC9.
TreeFamTF300435.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ96FC9.
BgeeQ96FC9.
CleanExHS_CHL1.
HS_DDX11.
GenevestigatorQ96FC9.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
InterProIPR006555. ATP-dep_Helicase_C.
IPR028331. DDX11-like.
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]
PANTHERPTHR11472:SF20. PTHR11472:SF20. 1 hit.
PfamPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00604. rad3. 1 hit.
PROSITEPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDDX11.
GenomeRNAi1663.
NextBio6842.
PROQ96FC9.
SOURCESearch...

Entry information

Entry nameDDX11_HUMAN
AccessionPrimary (citable) accession number: Q96FC9
Secondary accession number(s): Q13333 expand/collapse secondary AC list , Q86VQ4, Q86W62, Q92498, Q92770, Q92998, Q92999
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM