DDX11_HUMAN
ID DDX11_HUMAN Reviewed; 970 AA.
AC Q96FC9; Q13333; Q86VQ4; Q86W62; Q92498; Q92770; Q92998; Q92999;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP-dependent DNA helicase DDX11 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:27477908};
DE AltName: Full=CHL1-related protein 1 {ECO:0000303|PubMed:9013641};
DE Short=hCHLR1 {ECO:0000303|PubMed:9013641};
DE AltName: Full=DEAD/H-box protein 11 {ECO:0000312|HGNC:HGNC:2736};
DE AltName: Full=Keratinocyte growth factor-regulated gene 2 protein {ECO:0000303|PubMed:8798685};
DE Short=KRG-2 {ECO:0000303|PubMed:8798685};
GN Name=DDX11 {ECO:0000312|HGNC:HGNC:2736};
GN Synonyms=CHL1, CHLR1 {ECO:0000303|PubMed:9013641},
GN KRG2 {ECO:0000303|PubMed:8798685};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT SER-39.
RC TISSUE=Keratinocyte;
RX PubMed=8798685; DOI=10.1074/jbc.271.40.24337;
RA Frank S., Werner S.;
RT "The human homologue of the yeast CHL1 gene is a novel keratinocyte growth
RT factor regulated gene.";
RL J. Biol. Chem. 271:24337-24340(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANT GLU-567.
RX PubMed=9013641; DOI=10.1074/jbc.272.6.3823;
RA Amann J., Kidd V.J., Lahti J.M.;
RT "Characterization of putative human homologues of the yeast chromosome
RT transmission fidelity gene, CHL1.";
RL J. Biol. Chem. 272:3823-3832(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND VARIANTS GLU-567 AND
RP MET-575.
RA Ouellette M.M., Wright W.E., Shay J.W.;
RT "Isolation and characterization of the human homologue of the yeast CHL1
RT gene.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CATALYTIC ACTIVITY, ENZYME ACTIVITY, FUNCTION, AND MUTAGENESIS OF LYS-50.
RX PubMed=10648783; DOI=10.1093/nar/28.4.917;
RA Hirota Y., Lahti J.M.;
RT "Characterization of the enzymatic activity of hChlR1, a novel human DNA
RT helicase.";
RL Nucleic Acids Res. 28:917-924(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH A COHESIN COMPLEX, AND
RP INTERACTION WITH RAD21; SMC1 PROTEINS AND SMC3.
RX PubMed=17105772; DOI=10.1242/jcs.03262;
RA Parish J.L., Rosa J., Wang X., Lahti J.M., Doxsey S.J., Androphy E.J.;
RT "The DNA helicase ChlR1 is required for sister chromatid cohesion in
RT mammalian cells.";
RL J. Cell Sci. 119:4857-4865(2006).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH BOVINE PAPILLOMAVIRUS TYPE
RP 1 REGULATORY PROTEIN E2 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION
RP (MICROBIAL INFECTION).
RX PubMed=17189189; DOI=10.1016/j.molcel.2006.11.005;
RA Parish J.L., Bean A.M., Park R.B., Androphy E.J.;
RT "ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes
RT and viral genome maintenance.";
RL Mol. Cell 24:867-876(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ASSOCIATES WITH THE
RP CTF18-RFC COMPLEX, INTERACTION WITH CHTF18; DSCC1; FEN1; PCNA AND RFC2, AND
RP MUTAGENESIS OF LYS-50.
RX PubMed=18499658; DOI=10.1074/jbc.m802696200;
RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA Hurwitz J.;
RT "Studies with the human cohesin establishment factor, ChlR1. Association of
RT ChlR1 with Ctf18-RFC and Fen1.";
RL J. Biol. Chem. 283:20925-20936(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INVOLVEMENT IN WBRS.
RX PubMed=20137776; DOI=10.1016/j.ajhg.2010.01.008;
RA van der Lelij P., Chrzanowska K.H., Godthelp B.C., Rooimans M.A.,
RA Oostra A.B., Stumm M., Zdzienicka M.Z., Joenje H., de Winter J.P.;
RT "Warsaw breakage syndrome, a cohesinopathy associated with mutations in the
RT XPD helicase family member DDX11/ChlR1.";
RL Am. J. Hum. Genet. 86:262-266(2010).
RN [11]
RP FUNCTION, AND INTERACTION WITH TIMELESS.
RX PubMed=20124417; DOI=10.1242/jcs.057984;
RA Leman A.R., Noguchi C., Lee C.Y., Noguchi E.;
RT "Human Timeless and Tipin stabilize replication forks and facilitate
RT sister-chromatid cohesion.";
RL J. Cell Sci. 123:660-670(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION.
RX PubMed=21854770; DOI=10.1016/j.yexcr.2011.08.006;
RA Inoue A., Hyle J., Lechner M.S., Lahti J.M.;
RT "Mammalian ChlR1 has a role in heterochromatin organization.";
RL Exp. Cell Res. 317:2522-2535(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-50.
RX PubMed=22102414; DOI=10.1074/jbc.m111.276022;
RA Wu Y., Sommers J.A., Khan I., de Winter J.P., Brosh R.M. Jr.;
RT "Biochemical characterization of Warsaw breakage syndrome helicase.";
RL J. Biol. Chem. 287:1007-1021(2012).
RN [15]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23116066; DOI=10.1186/1476-4598-11-82;
RA Bhattacharya C., Wang X., Becker D.;
RT "The DEAD/DEAH box helicase, DDX11, is essential for the survival of
RT advanced melanomas.";
RL Mol. Cancer 11:82-82(2012).
RN [16]
RP FUNCTION.
RX PubMed=23797032; DOI=10.1016/j.yexcr.2013.06.005;
RA Shah N., Inoue A., Woo Lee S., Beishline K., Lahti J.M., Noguchi E.;
RT "Roles of ChlR1 DNA helicase in replication recovery from DNA damage.";
RL Exp. Cell Res. 319:2244-2253(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH POLR1A AND UBTF, SUBCELLULAR
RP LOCATION, INDUCTION, VARIANT WBRS GLN-263, AND CHARACTERIZATION OF VARIANT
RP WBRS GLN-263.
RX PubMed=26089203; DOI=10.1093/hmg/ddv213;
RA Sun X., Chen H., Deng Z., Hu B., Luo H., Zeng X., Han L., Cai G., Ma L.;
RT "The Warsaw breakage syndrome-related protein DDX11 is required for
RT ribosomal RNA synthesis and embryonic development.";
RL Hum. Mol. Genet. 24:4901-4915(2015).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, CHROMATIN-BINDING, AND
RP RNA-BINDING.
RX PubMed=27477908; DOI=10.1016/j.molcel.2016.06.031;
RA Marchese F.P., Grossi E., Marin-Bejar O., Bharti S.K., Raimondi I.,
RA Gonzalez J., Martinez-Herrera D.J., Athie A., Amadoz A., Brosh R.M. Jr.,
RA Huarte M.;
RT "A Long Noncoding RNA Regulates Sister Chromatid Cohesion.";
RL Mol. Cell 63:397-407(2016).
RN [20]
RP FUNCTION, AND INTERACTION WITH TIMELESS.
RX PubMed=26503245; DOI=10.1093/nar/gkv1112;
RA Cali F., Bharti S.K., Di Perna R., Brosh R.M. Jr., Pisani F.M.;
RT "Tim/Timeless, a member of the replication fork protection complex,
RT operates with the Warsaw breakage syndrome DNA helicase DDX11 in the same
RT fork recovery pathway.";
RL Nucleic Acids Res. 44:705-717(2016).
RN [21]
RP VARIANT WBRS GLN-263, AND CHARACTERIZATION OF VARIANT WBRS GLN-263.
RX PubMed=23033317; DOI=10.1002/humu.22226;
RA Capo-Chichi J.M., Bharti S.K., Sommers J.A., Yammine T., Chouery E.,
RA Patry L., Rouleau G.A., Samuels M.E., Hamdan F.F., Michaud J.L.,
RA Brosh R.M. Jr., Megarbane A., Kibar Z.;
RT "Identification and biochemical characterization of a novel mutation in
RT DDX11 causing warsaw breakage syndrome.";
RL Hum. Mutat. 34:103-107(2013).
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent DNA helicase that
CC participates in various functions in genomic stability, including DNA
CC replication, DNA repair and heterochromatin organization as well as in
CC ribosomal RNA synthesis (PubMed:10648783, PubMed:21854770,
CC PubMed:23797032, PubMed:26089203, PubMed:26503245). Its double-stranded
CC DNA helicase activity requires either a minimal 5'-single-stranded tail
CC length of approximately 15 nt (flap substrates) or 10 nt length single-
CC stranded gapped DNA substrates of a partial duplex DNA structure for
CC helicase loading and translocation along DNA in a 5' to 3' direction
CC (PubMed:18499658, PubMed:22102414). The helicase activity is capable of
CC displacing duplex regions up to 100 bp, which can be extended up to 500
CC bp by the replication protein A (RPA) or the cohesion CTF18-replication
CC factor C (Ctf18-RFC) complex activities (PubMed:18499658). Shows also
CC ATPase- and helicase activities on substrates that mimic key DNA
CC intermediates of replication, repair and homologous recombination
CC reactions, including forked duplex, anti-parallel G-quadruplex and
CC three-stranded D-loop DNA molecules (PubMed:22102414, PubMed:26503245).
CC Plays a role in DNA double-strand break (DSB) repair at the DNA
CC replication fork during DNA replication recovery from DNA damage
CC (PubMed:23797032). Recruited with TIMELESS factor upon DNA-replication
CC stress response at DNA replication fork to preserve replication fork
CC progression, and hence ensure DNA replication fidelity
CC (PubMed:26503245). Cooperates also with TIMELESS factor during DNA
CC replication to regulate proper sister chromatid cohesion and mitotic
CC chromosome segregation (PubMed:17105772, PubMed:18499658,
CC PubMed:20124417, PubMed:23116066, PubMed:23797032). Stimulates 5'-
CC single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and
CC helicase-independent manner; and hence it may contribute in Okazaki
CC fragment processing at DNA replication fork during lagging strand DNA
CC synthesis (PubMed:18499658). Its ability to function at DNA replication
CC fork is modulated by its binding to long non-coding RNA (lncRNA)
CC cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to
CC increase both DDX11 ATPase activity and binding to DNA replicating
CC regions (PubMed:27477908). Also plays a role in heterochromatin
CC organization (PubMed:21854770). Involved in rRNA transcription
CC activation through binding to active hypomethylated rDNA gene loci by
CC recruiting UBTF and the RNA polymerase Pol I transcriptional machinery
CC (PubMed:26089203). Plays a role in embryonic development and prevention
CC of aneuploidy (By similarity). Involved in melanoma cell proliferation
CC and survival (PubMed:23116066). Associates with chromatin at DNA
CC replication fork regions (PubMed:27477908). Binds to single- and
CC double-stranded DNAs (PubMed:9013641, PubMed:18499658,
CC PubMed:22102414). {ECO:0000250|UniProtKB:Q6AXC6,
CC ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:17105772,
CC ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:20124417,
CC ECO:0000269|PubMed:21854770, ECO:0000269|PubMed:22102414,
CC ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:23797032,
CC ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:26503245,
CC ECO:0000269|PubMed:27477908}.
CC -!- FUNCTION: (Microbial infection) Required for bovine papillomavirus type
CC 1 regulatory protein E2 loading onto mitotic chromosomes during DNA
CC replication for the viral genome to be maintained and segregated.
CC {ECO:0000269|PubMed:17189189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:10648783, ECO:0000269|PubMed:18499658,
CC ECO:0000269|PubMed:22102414, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:27477908};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by high magnesium
CC salt levels (up to a 0.1 M), and potassium salts (glutamate, chloride
CC or acetate) are more effective than the corresponding sodium salts
CC (PubMed:10648783, PubMed:18499658). ATPase activity is enhanced by the
CC long non-coding RNA (lncRNA) cohesion regulator noncoding RNA (CONCR)
CC (PubMed:27477908). Double-stranded DNA helicase activity is maximal
CC with magnesium ions at low concentrations (0.5-1 mM) whereas is
CC markedly inhibited at higher levels (5 mM and above) (PubMed:10648783,
CC PubMed:18499658). Double-stranded DNA helicase activity is stimulated
CC by 25-50 mM potassium acetate, stimulated to a lesser extent by 25 mM
CC of ammonium acetate, and markedly inhibited by sodium acetate
CC (PubMed:18499658). {ECO:0000269|PubMed:10648783,
CC ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:27477908}.
CC -!- SUBUNIT: Associates with the CTF18-RFC complex (PubMed:18499658).
CC Associates with a cohesin complex composed of RAD21, SMC1 proteins and
CC SMC3 (PubMed:17105772). Interacts with CHTF18 (PubMed:18499658).
CC Interacts with DSCC1 (PubMed:18499658). Interacts with FEN1; this
CC interaction is direct and increases flap endonuclease activity of FEN1
CC (PubMed:18499658). Interacts with PCNA (PubMed:18499658). Interacts
CC with POLR1A and UBTF (PubMed:26089203). Interacts with RAD21, SMC1
CC proteins and SMC3 (PubMed:17105772). Interacts with RFC2
CC (PubMed:18499658). Interacts with TIMELESS; this interaction increases
CC recruitment of both proteins onto chromatin in response to replication
CC stress induction by hydroxyurea (PubMed:20124417, PubMed:26503245).
CC {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:18499658,
CC ECO:0000269|PubMed:20124417, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:26503245}.
CC -!- SUBUNIT: (Microbial infection) Interacts with bovine papillomavirus
CC type 1 regulatory protein E2; this interaction stimulates the
CC recruitment of E2 onto mitotic chromosomes.
CC {ECO:0000269|PubMed:17189189}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17105772}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:9013641}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:17105772}. Midbody {ECO:0000269|PubMed:17105772}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17105772}. Note=During the early stages of mitosis,
CC localizes to condensed chromatin and is released from the chromatin
CC with progression to metaphase. Also localizes to the spindle poles
CC throughout mitosis and at the midbody at later stages of mitosis
CC (metaphase to telophase) (PubMed:17105772). In interphase, colocalizes
CC with nucleolin in the nucleolus (PubMed:26089203).
CC {ECO:0000269|PubMed:17105772, ECO:0000269|PubMed:26089203}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17189189}.
CC Note=(Microbial infection) Colocalizes with bovine papillomavirus type
CC 1 regulatory protein E2 on mitotic chromosomes at early stages of
CC mitosis. {ECO:0000269|PubMed:17189189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96FC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FC9-2; Sequence=VSP_016864, VSP_016865;
CC Name=3;
CC IsoId=Q96FC9-3; Sequence=VSP_016860, VSP_016864, VSP_016865;
CC Name=4;
CC IsoId=Q96FC9-4; Sequence=VSP_016863, VSP_016864, VSP_016865;
CC Name=5;
CC IsoId=Q96FC9-5; Sequence=VSP_016861, VSP_016862;
CC -!- TISSUE SPECIFICITY: Expressed in melanoma cells. Not detected in
CC epidermal melanocytes of normal skin (at protein level)
CC (PubMed:23116066). Highly expressed in spleen, B-cells, thymus, testis,
CC ovary, small intestine and pancreas (PubMed:9013641). Very low
CC expression seen in brain (PubMed:9013641). Expressed in dividing cells
CC and/or cells undergoing high levels of recombination (PubMed:9013641).
CC No expression detected in cells signaled to terminally differentiate
CC (PubMed:9013641). Expressed weakly in keratinocytes (PubMed:8798685).
CC {ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:8798685,
CC ECO:0000269|PubMed:9013641}.
CC -!- INDUCTION: Up-regulated by serum (at protein level) (PubMed:26089203).
CC Up-regulated by fibroblast growth factor FGF7 (PubMed:8798685).
CC Expressed in keratinocyte growth factor-stimulated cells but not in EGF
CC and IL1-beta-treated keratinocytes (PubMed:8798685). Up-regulated with
CC progression from noninvasive to invasive melanoma (PubMed:23116066).
CC {ECO:0000269|PubMed:23116066, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:8798685}.
CC -!- DISEASE: Warsaw breakage syndrome (WBRS) [MIM:613398]: A syndrome
CC characterized by severe microcephaly, pre- and postnatal growth
CC retardation, facial dysmorphism and abnormal skin pigmentation.
CC Additional features include high arched palate, coloboma of the right
CC optic disk, deafness, ventricular septal defect, toes and fingers
CC abnormalities. At cellular level, drug-induced chromosomal breakage, a
CC feature of Fanconi anemia, and sister chromatid cohesion defects, a
CC feature of Roberts syndrome, coexist. {ECO:0000269|PubMed:20137776,
CC ECO:0000269|PubMed:23033317, ECO:0000269|PubMed:26089203}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67895.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67895.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=DEAD/H (Asp-Glu-Ala-Asp/His) box helicase 11
CC (DDX11); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/DDX11";
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DR EMBL; X99583; CAA67895.1; ALT_SEQ; mRNA.
DR EMBL; U33833; AAB06962.1; -; mRNA.
DR EMBL; U75967; AAB18749.1; -; mRNA.
DR EMBL; U75968; AAB18750.1; -; mRNA.
DR EMBL; BC050069; AAH50069.1; -; mRNA.
DR EMBL; BC050522; AAH50522.1; -; mRNA.
DR CCDS; CCDS41767.1; -. [Q96FC9-2]
DR CCDS; CCDS44856.1; -. [Q96FC9-1]
DR CCDS; CCDS58224.1; -. [Q96FC9-3]
DR CCDS; CCDS8721.1; -. [Q96FC9-4]
DR PIR; G02071; G02071.
DR RefSeq; NP_001244073.1; NM_001257144.1. [Q96FC9-1]
DR RefSeq; NP_001244074.1; NM_001257145.1. [Q96FC9-3]
DR RefSeq; NP_004390.3; NM_004399.2. [Q96FC9-4]
DR RefSeq; NP_689651.1; NM_152438.1. [Q96FC9-1]
DR RefSeq; XP_016874421.1; XM_017018932.1. [Q96FC9-2]
DR AlphaFoldDB; Q96FC9; -.
DR BioGRID; 108028; 64.
DR CORUM; Q96FC9; -.
DR IntAct; Q96FC9; 27.
DR STRING; 9606.ENSP00000440402; -.
DR iPTMnet; Q96FC9; -.
DR PhosphoSitePlus; Q96FC9; -.
DR BioMuta; DDX11; -.
DR DMDM; 74731686; -.
DR EPD; Q96FC9; -.
DR jPOST; Q96FC9; -.
DR MassIVE; Q96FC9; -.
DR MaxQB; Q96FC9; -.
DR PaxDb; Q96FC9; -.
DR PeptideAtlas; Q96FC9; -.
DR PRIDE; Q96FC9; -.
DR ProteomicsDB; 76511; -. [Q96FC9-1]
DR ProteomicsDB; 76512; -. [Q96FC9-2]
DR ProteomicsDB; 76513; -. [Q96FC9-3]
DR ProteomicsDB; 76514; -. [Q96FC9-4]
DR ProteomicsDB; 76515; -. [Q96FC9-5]
DR Antibodypedia; 24573; 235 antibodies from 25 providers.
DR DNASU; 1663; -.
DR Ensembl; ENST00000228264.10; ENSP00000228264.6; ENSG00000013573.17. [Q96FC9-3]
DR Ensembl; ENST00000350437.8; ENSP00000309965.5; ENSG00000013573.17. [Q96FC9-4]
DR Ensembl; ENST00000435753.6; ENSP00000406799.2; ENSG00000013573.17. [Q96FC9-5]
DR Ensembl; ENST00000542838.6; ENSP00000443426.1; ENSG00000013573.17. [Q96FC9-2]
DR Ensembl; ENST00000545668.5; ENSP00000440402.1; ENSG00000013573.17. [Q96FC9-1]
DR GeneID; 1663; -.
DR KEGG; hsa:1663; -.
DR MANE-Select; ENST00000542838.6; ENSP00000443426.1; NM_030653.4; NP_085911.2. [Q96FC9-2]
DR UCSC; uc001rjr.2; human. [Q96FC9-1]
DR CTD; 1663; -.
DR DisGeNET; 1663; -.
DR GeneCards; DDX11; -.
DR GeneReviews; DDX11; -.
DR HGNC; HGNC:2736; DDX11.
DR HPA; ENSG00000013573; Low tissue specificity.
DR MalaCards; DDX11; -.
DR MIM; 601150; gene.
DR MIM; 613398; phenotype.
DR neXtProt; NX_Q96FC9; -.
DR OpenTargets; ENSG00000013573; -.
DR Orphanet; 280558; Warsaw breakage syndrome.
DR PharmGKB; PA27201; -.
DR VEuPathDB; HostDB:ENSG00000013573; -.
DR eggNOG; KOG1133; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_2_1_1; -.
DR InParanoid; Q96FC9; -.
DR OMA; QTHQFRD; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q96FC9; -.
DR TreeFam; TF300435; -.
DR BRENDA; 3.6.4.12; 2681.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q96FC9; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q96FC9; -.
DR BioGRID-ORCS; 1663; 545 hits in 1051 CRISPR screens.
DR GeneWiki; DDX11; -.
DR GenomeRNAi; 1663; -.
DR Pharos; Q96FC9; Tbio.
DR PRO; PR:Q96FC9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96FC9; protein.
DR Bgee; ENSG00000013573; Expressed in lower esophagus mucosa and 129 other tissues.
DR ExpressionAtlas; Q96FC9; baseline and differential.
DR Genevisible; Q96FC9; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IMP:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0045142; F:triplex DNA binding; IDA:UniProtKB.
DR GO; GO:1904976; P:cellular response to bleomycin; IMP:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034085; P:establishment of sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:1990700; P:nucleolar chromatin organization; IMP:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IDA:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR028331; CHL1/DDX11.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF41; PTHR11472:SF41; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Activator; Alternative splicing; ATP-binding; Chromosome;
KW Cytoplasm; Cytoskeleton; Developmental protein; Disease variant;
KW DNA damage; DNA repair; DNA replication; DNA-binding; Helicase;
KW Host-virus interaction; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..970
FT /note="ATP-dependent DNA helicase DDX11"
FT /id="PRO_0000055136"
FT DOMAIN 9..445
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 393..396
FT /note="DEAH box"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016860"
FT VAR_SEQ 214..288
FT /note="VDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKDVRLVSLGSRQN
FT LCVNEDVKSLGSVQLINDRCVDM -> APSDATSSRHPPDASFPAALNFLQRTRPSSVL
FT SEDLLMQRAVAKHPALLPWQMSSSPLRPGSEWMRMRMTWRKNT (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_016861"
FT VAR_SEQ 289..970
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_016862"
FT VAR_SEQ 685..734
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8798685"
FT /id="VSP_016863"
FT VAR_SEQ 820..906
FT /note="SPRPGTPREGSGGEPVHEGRQPVHRQGHQAPEGFCQRSAPGPAICPAPCPGQ
FT AAGLDPSPCGGQSYLWPRHCCCAEVSPGEVGLFLM -> PRAPGQAPPGKALVENLCMK
FT AVNQSIGRAIRHQKDFASVVLLDQRYARPPVLAKLPAWIRARVEVKATFGPAIAAVQKF
FT HREKSASS (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8798685, ECO:0000303|PubMed:9013641,
FT ECO:0000303|Ref.3"
FT /id="VSP_016864"
FT VAR_SEQ 907..970
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8798685, ECO:0000303|PubMed:9013641,
FT ECO:0000303|Ref.3"
FT /id="VSP_016865"
FT VARIANT 39
FT /note="I -> S"
FT /evidence="ECO:0000269|PubMed:8798685"
FT /id="VAR_024808"
FT VARIANT 263
FT /note="R -> Q (in WBRS; impairs the helicase activity by
FT perturbing its DNA binding and DNA-dependent ATPase
FT activity; reduces binding to rDNA promoter and promotion of
FT rDNA transcription; dbSNP:rs201968272)"
FT /evidence="ECO:0000269|PubMed:23033317,
FT ECO:0000269|PubMed:26089203"
FT /id="VAR_069099"
FT VARIANT 567
FT /note="Q -> E (in dbSNP:rs2075322)"
FT /evidence="ECO:0000269|PubMed:9013641, ECO:0000269|Ref.3"
FT /id="VAR_024809"
FT VARIANT 575
FT /note="T -> M (in dbSNP:rs17857386)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_024810"
FT VARIANT 856
FT /note="R -> H (in dbSNP:rs1046457)"
FT /id="VAR_052175"
FT VARIANT 864
FT /note="C -> R (in dbSNP:rs3893679)"
FT /id="VAR_052176"
FT VARIANT 951
FT /note="C -> R (in dbSNP:rs1046458)"
FT /id="VAR_052177"
FT VARIANT 966
FT /note="W -> C (in dbSNP:rs14330)"
FT /id="VAR_052178"
FT MUTAGEN 50
FT /note="K->R: Loss of both DNA-dependent ATPase and ATP-
FT dependent helicase activities."
FT /evidence="ECO:0000269|PubMed:10648783,
FT ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:22102414"
SQ SEQUENCE 970 AA; 108313 MW; 5BF49FE74E912B48 CRC64;
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK SLSLICGALS
WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG AAGTPRPAGE PAWVTQFVQK
KEERDLVDRL KAEQARRKQR EERLQQLQHR VQLKYAAKRL RQEEEERENL LRLSREMLET
GPEAERLEQL ESGEEELVLA EYESDEEKKV ASRVDEDEDD LEEEHITKIY YCSRTHSQLA
QFVHEVKKSP FGKDVRLVSL GSRQNLCVNE DVKSLGSVQL INDRCVDMQR SRHEKKKGAE
EEKPKRRRQE KQAACPFYNH EQMGLLRDEA LAEVKDMEQL LALGKEARAC PYYGSRLAIP
AAQLVVLPYQ MLLHAATRQA AGIRLQDQVV IIDEAHNLID TITGMHSVEV SGSQLCQAHS
QLLQYVERYG KRLKAKNLMY LKQILYLLEK FVAVLGGNIK QNPNTQSLSQ TGTELKTIND
FLFQSQIDNI NLFKVQRYCE KSMISRKLFG FTERYGAVFS SREQPKLAGF QQFLQSLQPR
TTEALAAPAD ESQASTLRPA SPLMHIQGFL AALTTANQDG RVILSRQGSL SQSTLKFLLL
NPAVHFAQVV KECRAVVIAG GTMQPVSDFR QQLLACAGVE AERVVEFSCG HVIPPDNILP
LVICSGISNQ PLEFTFQKRE LPQMMDEVGR ILCNLCGVVP GGVVCFFPSY EYLRQVHAHW
EKGGLLGRLA ARKKIFQEPK SAHQVEQVLL AYSRCIQACG QERGQVTGAL LLSVVGGKMS
EGINFSDNLG RCVVMVGMPF PNIRSAELQE KMAYLDQTLS PRPGTPREGS GGEPVHEGRQ
PVHRQGHQAP EGFCQRSAPG PAICPAPCPG QAAGLDPSPC GGQSYLWPRH CCCAEVSPGE
VGLFLMGNHT TAWRRALPLS CPLETVFVVG VVCGDPVTKV KPRRRVWSPE CCQDPGTGVS
SRRRKWGNPE
