Q96FC9 (DDX11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	970 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nucleolus. 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 process	Cell cycle Host-virus interaction
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	4Fe-4S ATP-binding DNA-binding Iron Iron-sulfur Metal-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement Ref.2. Source: ProtInc S phase 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 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	midbody 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 spindle pole Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	4 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 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 970	970	Probable ATP-dependent RNA helicase DDX11		PRO_0000055136
Regions
	Domain	9 – 445	437	Helicase ATP-binding
	Nucleotide binding	44 – 51	8	ATP By similarity
	Motif	393 – 396	4	DEAH
	Compositional bias	163 – 224	62	Glu-rich
Sites
	Metal binding	267	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	285	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	315	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	350	1	Iron-sulfur (4Fe-4S) By similarity
Natural variations
	Alternative sequence	1 – 26	26	Missing in isoform 3.		VSP_016860
	Alternative sequence	214 – 288	75	VDEDE…RCVDM → APSDATSSRHPPDASFPAAL NFLQRTRPSSVLSEDLLMQR AVAKHPALLPWQMSSSPLRP GSEWMRMRMTWRKNT in isoform 5.		VSP_016861
	Alternative sequence	289 – 970	682	Missing in isoform 5.		VSP_016862
	Alternative sequence	685 – 734	50	Missing in isoform 4.		VSP_016863
	Alternative sequence	820 – 906	87	SPRPG…GLFLM → PRAPGQAPPGKALVENLCMK AVNQSIGRAIRHQKDFASVV LLDQRYARPPVLAKLPAWIR ARVEVKATFGPAIAAVQKFH REKSASS in isoform 2, isoform 3 and isoform 4.		VSP_016864
	Alternative sequence	907 – 970	64	Missing in isoform 2, isoform 3 and isoform 4.		VSP_016865
	Natural variant	39	1	I → S. Ref.1 Corresponds to variant rs1046454 [ dbSNP | Ensembl ].		VAR_024808
	Natural variant	263	1	R → Q in WBRS; impairs the enzyme helicase activity by perturbing its DNA binding and DNA-dependent ATP hydrolysis. Ref.12		VAR_069099
	Natural variant	567	1	Q → E. Ref.2 Ref.3 Corresponds to variant rs2075322 [ dbSNP | Ensembl ].		VAR_024809
	Natural variant	575	1	T → M. Ref.3 Corresponds to variant rs17857386 [ dbSNP | Ensembl ].		VAR_024810
	Natural variant	856	1	R → H. Corresponds to variant rs1046457 [ dbSNP | Ensembl ].		VAR_052175
	Natural variant	864	1	C → R. Corresponds to variant rs3893679 [ dbSNP | Ensembl ].		VAR_052176
	Natural variant	951	1	C → R. Corresponds to variant rs1046458 [ dbSNP | Ensembl ].		VAR_052177
	Natural variant	966	1	W → C. Corresponds to variant rs14330 [ dbSNP | Ensembl ].		VAR_052178
Experimental info
	Mutagenesis	50	1	K → R: Loss of both helicase and ATPase activity. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 5BF49FE74E912B48	FASTA	970	108,313
	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
	Isoform 2 [UniParc]. Checksum: BC51D55CB3186C91	FASTA	906	101,685
	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 KMAYLDQTLP RAPGQAPPGK ALVENLCMKA 850 860 870 880 890 900 VNQSIGRAIR HQKDFASVVL LDQRYARPPV LAKLPAWIRA RVEVKATFGP AIAAVQKFHR EKSASS
	Isoform 3 [UniParc]. Checksum: E0D7B88158ABA02A	FASTA	880	98,687
	10 20 30 40 50 60 MAELYRVLEA GKIGIFESPT GTGKSLSLIC GALSWLRDFE QKKREEEARL LETGTGPLHD 70 80 90 100 110 120 EKDESLCLSS SCEGAAGTPR PAGEPAWVTQ FVQKKEERDL VDRLKAEQAR RKQREERLQQ 130 140 150 160 170 180 LQHRVQLKYA AKRLRQEEEE RENLLRLSRE MLETGPEAER LEQLESGEEE LVLAEYESDE 190 200 210 220 230 240 EKKVASRVDE DEDDLEEEHI TKIYYCSRTH SQLAQFVHEV KKSPFGKDVR LVSLGSRQNL 250 260 270 280 290 300 CVNEDVKSLG SVQLINDRCV DMQRSRHEKK KGAEEEKPKR RRQEKQAACP FYNHEQMGLL 310 320 330 340 350 360 RDEALAEVKD MEQLLALGKE ARACPYYGSR LAIPAAQLVV LPYQMLLHAA TRQAAGIRLQ 370 380 390 400 410 420 DQVVIIDEAH NLIDTITGMH SVEVSGSQLC QAHSQLLQYV ERYGKRLKAK NLMYLKQILY 430 440 450 460 470 480 LLEKFVAVLG GNIKQNPNTQ SLSQTGTELK TINDFLFQSQ IDNINLFKVQ RYCEKSMISR 490 500 510 520 530 540 KLFGFTERYG AVFSSREQPK LAGFQQFLQS LQPRTTEALA APADESQAST LRPASPLMHI 550 560 570 580 590 600 QGFLAALTTA NQDGRVILSR QGSLSQSTLK FLLLNPAVHF AQVVKECRAV VIAGGTMQPV 610 620 630 640 650 660 SDFRQQLLAC AGVEAERVVE FSCGHVIPPD NILPLVICSG ISNQPLEFTF QKRELPQMMD 670 680 690 700 710 720 EVGRILCNLC GVVPGGVVCF FPSYEYLRQV HAHWEKGGLL GRLAARKKIF QEPKSAHQVE 730 740 750 760 770 780 QVLLAYSRCI QACGQERGQV TGALLLSVVG GKMSEGINFS DNLGRCVVMV GMPFPNIRSA 790 800 810 820 830 840 ELQEKMAYLD QTLPRAPGQA PPGKALVENL CMKAVNQSIG RAIRHQKDFA SVVLLDQRYA 850 860 870 880 RPPVLAKLPA WIRARVEVKA TFGPAIAAVQ KFHREKSASS
	Isoform 4 [UniParc]. Checksum: 30C866F69D6ABD34	FASTA	856	96,128
	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 LPQMIFQEPK SAHQVEQVLL AYSRCIQACG QERGQVTGAL 730 740 750 760 770 780 LLSVVGGKMS EGINFSDNLG RCVVMVGMPF PNIRSAELQE KMAYLDQTLP RAPGQAPPGK 790 800 810 820 830 840 ALVENLCMKA VNQSIGRAIR HQKDFASVVL LDQRYARPPV LAKLPAWIRA RVEVKATFGP 850 AIAAVQKFHR EKSASS
	Isoform 5 [UniParc]. Checksum: 78E0917712BBC6B0	FASTA	288	32,951
	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 ASRAPSDATS SRHPPDASFP AALNFLQRTR 250 260 270 280 PSSVLSEDLL MQRAVAKHPA LLPWQMSSSP LRPGSEWMRM RMTWRKNT

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00012188. IPI00332293. IPI00657836. IPI00658184. IPI00942296.
PIR	G02071.
RefSeq	NP_001244073.1. NM_001257144.1. NP_001244074.1. NM_001257145.1. NP_004390.3. NM_004399.2. NP_689651.1. NM_152438.1.
UniGene	Hs.443960.
3D structure databases
ProteinModelPortal	Q96FC9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96FC9. 2 interactions.
MINT	MINT-1371028.
STRING	9606.ENSP00000384703.
PTM databases
PhosphoSite	Q96FC9.
Polymorphism databases
DMDM	74731686.
Proteomic databases
PaxDb	Q96FC9.
PRIDE	Q96FC9.
Protocols and materials databases
DNASU	1663.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228264; ENSP00000228264; ENSG00000013573. ENST00000251758; ENSP00000251758; ENSG00000013573. ENST00000350437; ENSP00000309965; ENSG00000013573. ENST00000407793; ENSP00000384703; ENSG00000013573. ENST00000435753; ENSP00000406799; ENSG00000013573. ENST00000542838; ENSP00000443426; ENSG00000013573. ENST00000545668; ENSP00000440402; ENSG00000013573.
GeneID	1663.
KEGG	hsa:1663.
UCSC	uc001rjr.1. human. uc001rjs.1. human. uc001rjt.1. human. uc001rju.1. human.
Organism-specific databases
CTD	1663.
GeneCards	GC12P031226.
HGNC	HGNC:2736. DDX11.
MIM	601150. gene. 613398. phenotype.
neXtProt	NX_Q96FC9.
Orphanet	280558. Warsaw breakage syndrome.
PharmGKB	PA27201.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1199.
HOVERGEN	HBG058884.
InParanoid	Q96FC9.
KO	K11273.
OMA	NLGRCVV.
OrthoDB	EOG4B5P4M.
PhylomeDB	Q96FC9.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q96FC9.
Bgee	Q96FC9.
CleanEx	HS_CHL1. HS_DDX11.
Genevestigator	Q96FC9.
GermOnline	ENSG00000013573. Homo sapiens.
Family and domain databases
InterPro	IPR006555. ATP-dep_Helicase_C. IPR027076. DDX11/CHL1. IPR010614. DEAD_2. IPR013020. DNA_helicase_DNA-repair_Rad3. IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3. IPR006554. Helicase-like_DEXD_c2. [Graphical view]
PANTHER	PTHR11472:SF5. PTHR11472:SF5. 1 hit.
Pfam	PF06733. DEAD_2. 1 hit. PF13307. Helicase_C_2. 1 hit. [Graphical view]
SMART	SM00488. DEXDc2. 1 hit. SM00491. HELICc2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00604. rad3. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. False negative. PS51193. HELICASE_ATP_BIND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1663.
NextBio	6842.
SOURCE	Search...

Entry information

Entry name

DDX11_HUMAN

Accession

Primary (citable) accession number: Q96FC9
Secondary accession number(s): Q13333 , Q86VQ4, Q86W62, Q92498, Q92770, Q92998, Q92999

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.