ID RECQ1_HUMAN Reviewed; 649 AA. AC P46063; A8K6G2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 3. DT 27-MAR-2024, entry version 224. DE RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000305|PubMed:7527136, ECO:0000305|PubMed:8056767}; DE EC=5.6.2.4 {ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:8056767, ECO:0000305|PubMed:7527136}; DE AltName: Full=DNA 3'-5' helicase Q1 {ECO:0000305}; DE AltName: Full=DNA helicase, RecQ-like type 1; DE Short=RecQ1; DE AltName: Full=DNA-dependent ATPase Q1 {ECO:0000303|PubMed:8056767}; DE AltName: Full=RecQ protein-like 1; GN Name=RECQL {ECO:0000303|PubMed:7961977}; Synonyms=RECQ1, RECQL1; 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], PROTEIN SEQUENCE OF 34-38; 186-193; 293-304; RP 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND VARIANT THR-487. RC TISSUE=Cervix carcinoma; RX PubMed=7961977; DOI=10.1016/s0021-9258(18)43957-9; RA Puranam K.L., Blackshear P.J.; RT "Cloning and characterization of RECQL, a potential human homologue of the RT Escherichia coli DNA helicase RecQ."; RL J. Biol. Chem. 269:29838-29845(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS A RP HELICASE, AND CATALYTIC ACTIVITY. RX PubMed=7527136; DOI=10.1093/nar/22.22.4566; RA Seki M., Miyazawa H., Tada S., Yanagisawa J., Yamaoka T., Hoshino S., RA Ozawa K., Eki T., Nogami M., Okumura K., Taguchi H., Hanaoka F., RA Enomoto T.; RT "Molecular cloning of cDNA encoding human DNA helicase Q1 which has RT homology to Escherichia coli Rec Q helicase and localization of the gene at RT chromosome 12p12."; RL Nucleic Acids Res. 22:4566-4573(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [8] RP FUNCTION AS A 3'-5' HELICASE, FUNCTION AS AN ATPASE, CATALYTIC ACTIVITY, RP AND COFACTOR. RX PubMed=8056767; DOI=10.1093/oxfordjournals.jbchem.a124369; RA Seki M., Yanagisawa J., Kohda T., Sonoyama T., Ui M., Enomoto T.; RT "Purification of two DNA-dependent adenosinetriphosphatases having DNA RT helicase activity from HeLa cells and comparison of the properties of the RT two enzymes."; RL J. Biochem. 115:523-531(1994). RN [9] RP FUNCTION, INTERACTION WITH EXO1 AND MLH1, AND MUTAGENESIS OF LYS-119. RX PubMed=15886194; DOI=10.1074/jbc.m500265200; RA Doherty K.M., Sharma S., Uzdilla L.A., Wilson T.M., Cui S., Vindigni A., RA Brosh R.M. Jr.; RT "RECQ1 helicase interacts with human mismatch repair factors that regulate RT genetic recombination."; RL J. Biol. Chem. 280:28085-28094(2005). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-514 AND LYS-522, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP INVOLVEMENT IN RECON, VARIANT RECON SER-459, CHARACTERIZATION OF VARIANT RP RECON SER-459, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH RP PARP1, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=35025765; DOI=10.1172/jci147301; RA Abu-Libdeh B., Jhujh S.S., Dhar S., Sommers J.A., Datta A., Longo G.M., RA Grange L.J., Reynolds J.J., Cooke S.L., McNee G.S., Hollingworth R., RA Woodward B.L., Ganesh A.N., Smerdon S.J., Nicolae C.M., RA Durlacher-Betzer K., Molho-Pessach V., Abu-Libdeh A., Meiner V., RA Moldovan G.L., Roukos V., Harel T., Brosh R.M. Jr., Stewart G.S.; RT "RECON syndrome is a genome instability disorder caused by mutations in the RT DNA helicase RECQL1."; RL J. Clin. Invest. 132:0-0(2022). RN [16] {ECO:0007744|PDB:2V1X} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 49-616 IN COMPLEX WITH ADP AND RP ZN(2+), FUNCTION, SUBSTRATE SPECIFICITY, POSSIBLE ACTIVE SITE, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, DOMAIN, AND MUTAGENESIS RP OF 555-LEU--ILE-572; 560-SER--ILE-567 AND TYR-564. RX PubMed=19151156; DOI=10.1073/pnas.0806908106; RA Pike A.C., Shrestha B., Popuri V., Burgess-Brown N., Muzzolini L., RA Costantini S., Vindigni A., Gileadi O.; RT "Structure of the human RECQ1 helicase reveals a putative strand-separation RT pin."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1039-1044(2009). RN [17] {ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 48-619 IN COMPLEX WITH ZN(2+) AND RP DNA, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 511-THR--LYS-514 AND RP ARG-528. RX PubMed=25831490; DOI=10.1073/pnas.1417594112; RA Pike A.C., Gomathinayagam S., Swuec P., Berti M., Zhang Y., Schnecke C., RA Marino F., von Delft F., Renault L., Costa A., Gileadi O., Vindigni A.; RT "Human RECQ1 helicase-driven DNA unwinding, annealing, and branch RT migration: insights from DNA complex structures."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4286-4291(2015). CC -!- FUNCTION: DNA helicase that plays a role in DNA damage repair and CC genome stability (PubMed:7961977, PubMed:7527136, PubMed:8056767, CC PubMed:15886194, PubMed:35025765). Exhibits a magnesium- and ATP- CC dependent DNA-helicase activity that unwinds single- and double- CC stranded DNA in a 3'-5' direction (PubMed:7527136, PubMed:8056767, CC PubMed:35025765, PubMed:19151156). Full-length protein unwinds forked CC DNA substrates, resolves Holliday junctions, and has DNA strand CC annealing activity (PubMed:19151156, PubMed:25831490). Plays a role in CC restoring regressed replication forks (PubMed:35025765). Required to CC restart stalled replication forks induced by abortive topoisomerase 1 CC and 2 lesions (PubMed:35025765). May play a role in the repair of DNA CC that is damaged by ultraviolet light or other mutagens (PubMed:7961977, CC PubMed:15886194). {ECO:0000269|PubMed:15886194, CC ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490, CC ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:7527136, CC ECO:0000269|PubMed:7961977, ECO:0000269|PubMed:8056767}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:8056767}; 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; CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:7527136, CC ECO:0000269|PubMed:8056767}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000305|PubMed:8056767}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57667, ChEBI:CHEBI:61404; CC Evidence={ECO:0000269|PubMed:7527136, ECO:0000269|PubMed:8056767}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51909; CC Evidence={ECO:0000305|PubMed:8056767}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:8056767}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:8056767}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490, CC ECO:0000312|PDB:2V1X, ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D}; CC Note=Binds 1 Zn(2+) per monomer (PubMed:19151156). CC {ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=95.3 uM for ATP {ECO:0000269|PubMed:35025765}; CC KM=115 uM for ATP {ECO:0000269|PubMed:19151156}; CC Vmax=84 nmol/min/ng enzyme with ATP as substrate CC {ECO:0000269|PubMed:35025765}; CC Note=kcat is 103.5 sec(-1) for ATP (PubMed:35025765). kcat is 90 CC min(-1) (PubMed:19151156). {ECO:0000269|PubMed:19151156, CC ECO:0000269|PubMed:35025765}; CC -!- SUBUNIT: May form homodimers or higher order oligomers CC (PubMed:35025765, PubMed:19151156). Forms a dimer in complex with CC tailed duplex DNA; the DNA only mkaes contact with one of the monomers CC (PubMed:25831490). Probably forms flat tetramers on Holliday junction CC DNA (PubMed:25831490) (Probable). Interacts with EXO1 CC (PubMed:15886194). Interacts with MLH1 (PubMed:15886194). Interacts CC with PARP1 (PubMed:35025765, PubMed:19151156, PubMed:25831490). CC {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:19151156, CC ECO:0000269|PubMed:25831490, ECO:0000269|PubMed:35025765, CC ECO:0000305|PubMed:25831490}. CC -!- INTERACTION: CC P46063; P52292: KPNA2; NbExp=2; IntAct=EBI-2823728, EBI-349938; CC P46063; O00629: KPNA4; NbExp=2; IntAct=EBI-2823728, EBI-396343; CC P46063; P09874: PARP1; NbExp=8; IntAct=EBI-2823728, EBI-355676; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35025765, CC ECO:0000269|PubMed:7961977}. CC -!- TISSUE SPECIFICITY: High expression in heart, lung, skeletal muscle and CC kidney, low expression in brain. {ECO:0000269|PubMed:7961977}. CC -!- DOMAIN: A helical hairpin (residues 554-573) in the winged-helix proble CC DNA-binding domain couples the ATPase (and probably ssDNA CC translocation) to DNA unwinding (PubMed:19151156). The isolated WH CC domain (residues 481-624) anneals DNA as well as full-length protein CC (PubMed:25831490). {ECO:0000269|PubMed:19151156, CC ECO:0000269|PubMed:25831490}. CC -!- DISEASE: RECON progeroid syndrome (RECON) [MIM:620370]: An autosomal CC recessive syndrome characterized by short stature, progeroid facial CC features, a hypoplastic nose, xeroderma, skin photosensitivity, muscle CC wasting with reduced subcutaneous fat, and slender elongated thumbs. CC {ECO:0000269|PubMed:35025765}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA60261.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/283/RECQL"; 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; L36140; AAA60261.1; ALT_FRAME; mRNA. DR EMBL; D37984; BAA07200.1; -; mRNA. DR EMBL; BT007119; AAP35783.1; -; mRNA. DR EMBL; AK291627; BAF84316.1; -; mRNA. DR EMBL; AC006559; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471094; EAW96434.1; -; Genomic_DNA. DR EMBL; BC001052; AAH01052.1; -; mRNA. DR CCDS; CCDS31756.1; -. DR PIR; A58836; A55311. DR RefSeq; NP_002898.2; NM_002907.3. DR RefSeq; NP_116559.1; NM_032941.2. DR RefSeq; XP_005253518.1; XM_005253461.3. DR RefSeq; XP_005253519.1; XM_005253462.4. DR RefSeq; XP_005253520.1; XM_005253463.3. DR RefSeq; XP_005253521.1; XM_005253464.3. DR PDB; 2V1X; X-ray; 2.00 A; A/B=49-616. DR PDB; 2WWY; X-ray; 2.90 A; A/B=49-616. DR PDB; 4U7D; X-ray; 3.40 A; A/B/C/D=49-616. DR PDB; 6JTZ; X-ray; 2.80 A; A/B=282-616. DR PDBsum; 2V1X; -. DR PDBsum; 2WWY; -. DR PDBsum; 4U7D; -. DR PDBsum; 6JTZ; -. DR AlphaFoldDB; P46063; -. DR SMR; P46063; -. DR BioGRID; 111897; 112. DR DIP; DIP-29216N; -. DR IntAct; P46063; 44. DR MINT; P46063; -. DR STRING; 9606.ENSP00000416739; -. DR BindingDB; P46063; -. DR ChEMBL; CHEMBL1293236; -. DR GlyGen; P46063; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P46063; -. DR MetOSite; P46063; -. DR PhosphoSitePlus; P46063; -. DR SwissPalm; P46063; -. DR BioMuta; RECQL; -. DR DMDM; 218512113; -. DR EPD; P46063; -. DR jPOST; P46063; -. DR MassIVE; P46063; -. DR MaxQB; P46063; -. DR PaxDb; 9606-ENSP00000416739; -. DR PeptideAtlas; P46063; -. DR ProteomicsDB; 55713; -. DR Pumba; P46063; -. DR TopDownProteomics; P46063; -. DR Antibodypedia; 4055; 118 antibodies from 21 providers. DR CPTC; P46063; 1 antibody. DR DNASU; 5965; -. DR Ensembl; ENST00000421138.6; ENSP00000395449.2; ENSG00000004700.16. DR Ensembl; ENST00000444129.7; ENSP00000416739.2; ENSG00000004700.16. DR GeneID; 5965; -. DR KEGG; hsa:5965; -. DR MANE-Select; ENST00000444129.7; ENSP00000416739.2; NM_002907.4; NP_002898.2. DR UCSC; uc001rex.4; human. DR AGR; HGNC:9948; -. DR CTD; 5965; -. DR DisGeNET; 5965; -. DR GeneCards; RECQL; -. DR HGNC; HGNC:9948; RECQL. DR HPA; ENSG00000004700; Low tissue specificity. DR MalaCards; RECQL; -. DR MIM; 600537; gene. DR MIM; 620370; phenotype. DR neXtProt; NX_P46063; -. DR OpenTargets; ENSG00000004700; -. DR PharmGKB; PA34315; -. DR VEuPathDB; HostDB:ENSG00000004700; -. DR eggNOG; KOG0353; Eukaryota. DR GeneTree; ENSGT00940000157013; -. DR HOGENOM; CLU_001103_12_5_1; -. DR InParanoid; P46063; -. DR OMA; FKLSTMV; -. DR OrthoDB; 5474026at2759; -. DR PhylomeDB; P46063; -. DR TreeFam; TF323555; -. DR BRENDA; 3.6.4.12; 2681. DR PathwayCommons; P46063; -. DR SignaLink; P46063; -. DR BioGRID-ORCS; 5965; 7 hits in 1151 CRISPR screens. DR ChiTaRS; RECQL; human. DR EvolutionaryTrace; P46063; -. DR GeneWiki; RECQL; -. DR GenomeRNAi; 5965; -. DR Pharos; P46063; Tbio. DR PRO; PR:P46063; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P46063; Protein. DR Bgee; ENSG00000004700; Expressed in buccal mucosa cell and 209 other cell types or tissues. DR ExpressionAtlas; P46063; baseline and differential. DR GO; GO:0005694; C:chromosome; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB. DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:GO_Central. DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB. DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central. DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB. DR CDD; cd18015; DEXHc_RecQ1; 1. DR CDD; cd18794; SF2_C_RecQ; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032284; RecQ_Zn-bd. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR NCBIfam; TIGR00614; recQ_fam; 1. DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1. DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF16124; RecQ_Zn_bind; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR Genevisible; P46063; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Direct protein sequencing; KW Disease variant; DNA-binding; Helicase; Hydrolase; Isomerase; KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Zinc. FT CHAIN 1..649 FT /note="ATP-dependent DNA helicase Q1" FT /id="PRO_0000205049" FT DOMAIN 100..275 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 300..451 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 481..592 FT /note="Winged-helix domain" FT /evidence="ECO:0000269|PubMed:19151156" FT REGION 595..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 219..222 FT /note="DEVH box" FT COMPBIAS 606..621 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..639 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 119 FT /evidence="ECO:0000305|PubMed:19151156" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 120 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:19151156, FT ECO:0007744|PDB:2V1X" FT BINDING 453 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:19151156, FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D" FT BINDING 471 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:19151156, FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D" FT BINDING 475 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:19151156, FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D" FT BINDING 478 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:19151156, FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D" FT MOD_RES 514 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 522 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 597 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 602 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6AYJ1" FT MOD_RES 634 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VARIANT 102 FT /note="V -> I (in dbSNP:rs1065751)" FT /id="VAR_034679" FT VARIANT 372 FT /note="V -> I (in dbSNP:rs2230003)" FT /id="VAR_051732" FT VARIANT 459 FT /note="A -> S (in RECON; likely pathogenic; reduces DNA FT helicase activity on a forked duplex DNA substrate; FT decreases ATPase activity; reduces DNA-binding; defect in FT repairing abortive TOP1/topoisomerase 1 and FT TOP2/topoisomerase 2 cleavage complexes; failure to FT efficiently restart replication following exposure to FT genotoxins, such as hydroxyurea (HU) and methyl methane FT sulfonate (MMS); no impact on nuclear localization and FT interaction with PARP1; no effect on capacity to promote FT single-strand DNA annealing; dbSNP:rs1055710310)" FT /evidence="ECO:0000269|PubMed:35025765" FT /id="VAR_088584" FT VARIANT 487 FT /note="K -> T (in dbSNP:rs6501)" FT /evidence="ECO:0000269|PubMed:7961977" FT /id="VAR_016140" FT VARIANT 495 FT /note="D -> H (in dbSNP:rs6499)" FT /id="VAR_016141" FT MUTAGEN 119 FT /note="K->A: Abrogates helicase activity." FT /evidence="ECO:0000269|PubMed:15886194" FT MUTAGEN 511..514 FT /note="TPLK->APLA: Considerably reduced DNA unwinding and FT branch migration on Holliday junctions, small change in DNA FT annealing." FT /evidence="ECO:0000269|PubMed:25831490" FT MUTAGEN 528 FT /note="R->A: Reduced DNA unwinding and branch migration on FT Holliday junctions, small change in DNA annealing." FT /evidence="ECO:0000269|PubMed:25831490" FT MUTAGEN 555..572 FT /note="LKEDYSFTAYATISYLKI->AA: Complete loss of DNA fork FT unwinding, retains ATPase activity (in a 49-616 residue FT fragment)." FT /evidence="ECO:0000269|PubMed:19151156" FT MUTAGEN 560..567 FT /note="SFTAYATI->AA: Complete loss of DNA fork unwinding, FT retains ATPase activity (in a 49-616 residue fragment)." FT /evidence="ECO:0000269|PubMed:19151156" FT MUTAGEN 564 FT /note="Y->A: Nearly complete loss of DNA fork unwinding, FT retains ATPase activity (in a 49-616 residue fragment)." FT /evidence="ECO:0000269|PubMed:19151156" FT CONFLICT 1 FT /note="M -> S (in Ref. 2; BAA07200)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="A -> D (in Ref. 1; AAA60261)" FT /evidence="ECO:0000305" FT CONFLICT 453 FT /note="C -> S (in Ref. 1; AAA60261)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="T -> A (in Ref. 1; AAA60261)" FT /evidence="ECO:0000305" FT CONFLICT 617 FT /note="E -> K (in Ref. 3; AAP35783 and 7; AAH01052)" FT /evidence="ECO:0000305" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 76..85 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 96..104 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 121..128 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 130..137 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 141..154 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 167..178 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 191..195 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 213..219 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 221..224 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:2WWY" FT HELIX 233..239 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 248..256 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 259..268 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 286..292 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 297..308 FT /evidence="ECO:0007829|PDB:2V1X" FT TURN 309..314 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 316..320 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 324..336 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 350..361 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 364..370 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 383..390 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 395..402 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 412..418 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 420..429 FT /evidence="ECO:0007829|PDB:2V1X" FT TURN 430..432 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:6JTZ" FT HELIX 436..447 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 454..462 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 476..479 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 484..488 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 490..505 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 512..519 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 525..527 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 539..551 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 554..561 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 566..572 FT /evidence="ECO:0007829|PDB:2V1X" FT HELIX 574..580 FT /evidence="ECO:0007829|PDB:2V1X" FT STRAND 587..591 FT /evidence="ECO:0007829|PDB:2V1X" SQ SEQUENCE 649 AA; 73457 MW; F616DC3191F79391 CRC64; MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL EDSDAGASNE YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI NVTMAGKEVF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP EDKTTVHRKW SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA //