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 27-MAR-2024, entry version 183. 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}, KRG2 GN {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 INTERACTION WITH TIMELESS. RX PubMed=32705708; DOI=10.15252/embj.2019104185; RA Lerner L.K., Holzer S., Kilkenny M.L., Svikovic S., Murat P., Schiavone D., RA Eldridge C.B., Bittleston A., Maman J.D., Branzei D., Stott K., RA Pellegrini L., Sale J.E.; RT "Timeless couples G-quadruplex detection with processing by DDX11 helicase RT during DNA replication."; RL EMBO J. 39:e104185-e104185(2020). RN [22] 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, ECO:0000269|PubMed:32705708}. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR AlphaFoldDB; Q96FC9; -. DR BioGRID; 108028; 69. DR CORUM; Q96FC9; -. DR IntAct; Q96FC9; 29. 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; 9606-ENSP00000440402; -. DR PeptideAtlas; 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 Pumba; Q96FC9; -. DR Antibodypedia; 24573; 281 antibodies from 25 providers. DR CPTC; Q96FC9; 1 antibody. 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 AGR; HGNC:2736; -. 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; 124793at2759; -. 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; 569 hits in 1127 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 131 other cell types or tissues. DR ExpressionAtlas; Q96FC9; baseline and differential. 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:HPA. 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:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB. DR GO; GO:0006974; P:DNA damage response; 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; P-loop containing nucleotide triphosphate hydrolases; 3. DR InterPro; IPR006555; ATP-dep_Helicase_C. 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; IPR010614; RAD3-like_helicase_DEAD. DR InterPro; IPR013020; Rad3/Chl1-like. DR NCBIfam; TIGR00604; rad3; 1. DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1. DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. DR Genevisible; Q96FC9; HS. 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 FT ATP-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 //